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        <title>The International Journal of Biochemistry and Cell Biology via MedWorm.com</title>
        <description>MedWorm.com provides a medical RSS filtering service. Over 6000 RSS medical sources are combined and output via different filters. This feed contains the latest items from the 'The International Journal of Biochemistry and Cell Biology' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=The+International+Journal+of+Biochemistry+and+Cell+Biology&t=The+International+Journal+of+Biochemistry+and+Cell+Biology&s=Search&f=source]]></link>
        <lastBuildDate>Thu, 09 Feb 2012 13:38:45 +0100</lastBuildDate>
        <item>
            <title>Aggrecan: Beyond cartilage and into the brain.</title>
            <link>http://www.medworm.com/index.php?rid=5658948&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22297263%26dopt%3DAbstract</link>
            <description>Authors: Morawski M, BrÃ¼ckner G, Arendt T, Matthews RT
    Abstract
    Aggrecan is well-studied in cartilage but its expression and function in the central nervous system has only recently begun to be appreciated. Aggrecan plays an important role in the organization of the neural extracellular space by binding and organizing hyaluronan to the cell surface through interactions with link protein and tenascins forming a large aggregated quaternary complex. While all members of the lectican family to which aggrecan belongs are thought to mediate similar roles in organizing the neural matrix, aggrecan is unique in that it is the only family member found almost exclusively in an enigmatic matrix substructure called the perineuronal net. Current work has established a critical role for perineur...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658948</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5658948</guid>        </item>
        <item>
            <title>Bral1: &quot;Superglue&quot; for the extracellular matrix in the brain white matter.</title>
            <link>http://www.medworm.com/index.php?rid=5658947&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22300985%26dopt%3DAbstract</link>
            <description>This article reviews the current knowledge about the structure, expression and function of this link protein.
    PMID: 22300985 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658947</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5658947</guid>        </item>
        <item>
            <title>PSA-NCAM: Synaptic functions mediated by its interactions with proteoglycans and glutamate receptors.</title>
            <link>http://www.medworm.com/index.php?rid=5658946&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22300986%26dopt%3DAbstract</link>
            <description>Authors: Senkov O, Tikhobrazova O, Dityatev A
    Abstract
    Dynamic regulation of glycosylation of the neural cell adhesion molecule (NCAM) by an unusual large negatively charged polysialic acid (PSA) is the major prerequisite for correct formation of brain circuitries during development and for normal synaptic plasticity, learning and memory in the adult. Traditionally, PSA is viewed as a de-adhesive highly hydrated molecule, which interferes with cell adhesion and promotes cellular/synaptic dynamics by steric hindrance. Analysis of synaptic functions of PSA-NCAM highlighted additional features of this molecule. First, PSA promotes interaction of NCAM with heparan sulfate proteoglycans and thus stimulates synaptogenesis. Second, PSA-NCAM modulates glutamate receptors: it restrains acti...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658946</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5658946</guid>        </item>
        <item>
            <title>Carboxy-terminus of CXCR7 regulates receptor localization and function.</title>
            <link>http://www.medworm.com/index.php?rid=5658945&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22300987%26dopt%3DAbstract</link>
            <description>Authors: Ray P, Mihalko LA, Coggins NL, Moudgil P, Ehrlich A, Luker KE, Luker GD
    Abstract
    Chemokine receptor CXCR7 is essential for normal development, and this receptor promotes initiation and progression of diseases including cancer and autoimmunity. To understand normal and pathologic functions of CXCR7 and advance development of therapeutic agents, there is a need to define structural domains that regulate this receptor. We generated mutants of CXCR7 with deletion of different lengths of the predicted intracellular tail and analyzed effects on CXCR7 signaling and function in cell-based assays. While wild-type CXCR7 predominantly localized to intracellular vesicles, progressive deletion of the carboxy terminus redistributed the receptor to the plasma membrane. Truncating the int...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658945</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5658945</guid>        </item>
        <item>
            <title>Chondroitin sulfate: A key molecule in the brain matrix.</title>
            <link>http://www.medworm.com/index.php?rid=5639395&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22265655%26dopt%3DAbstract</link>
            <description>Authors: Kwok JC, Warren P, Fawcett JW
    Abstract
    Chondroitin sulfate is a glycosaminoglycan composed of N-acetylgalactosamine and glucuronic acid. It attaches to a core protein to form chondroitin sulfate proteoglycan (CSPG). Being a major component of the brain extracellular matrix, CSPGs are involved in neural development, axon pathfinding and guidance, plasticity and also regeneration after injury in the nervous system. In this review, we shall discuss the structure, the biosynthetic pathway, its functions in the nervous system and how we can improve regeneration in the nervous system by modulating its structure and binding properties.
    PMID: 22265655 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5639395</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5639395</guid>        </item>
        <item>
            <title>d-Serine: A key to synaptic plasticity?</title>
            <link>http://www.medworm.com/index.php?rid=5639393&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22266400%26dopt%3DAbstract</link>
            <description>Authors: Henneberger C, Bard L, Rusakov DA
    Abstract
    Two discoveries have put d-serine in the spotlight of neuroscience. First, d-serine was detected in brain tissue at high levels. Second, it was found to act on the N-methyl-d-aspartate receptor (NMDAR). This receptor is central to use-dependent synaptic plasticity, the cellular process which is widely believed to underlie learning. The ensuing quest for the mechanisms of d-serine synthesis, release and clearance, as well as for its physiological significance has provided a wealth of experimental evidence implicating d-serine in synaptic plasticity. However some key questions remain unanswered. Which cells release d-serine and upon what stimuli? Is d-serine supply dynamically regulated? What is the fate of released d-serine? Answer...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5639393</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5639393</guid>        </item>
        <item>
            <title>Ephs and ephrins: Emerging therapeutic targets in neuropathology.</title>
            <link>http://www.medworm.com/index.php?rid=5639394&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22265656%26dopt%3DAbstract</link>
            <description>Authors: Attwood BK, Patel S, Pavlak R
    Abstract
    Eph receptors have been the subject of intense research since their discovery. Their widespread pattern of expression, involvement in a variety of important cellular phenomena and unique mode of action have stimulated interest in their role in health and disease across biological and medical domains. However, the function of Ephs in nervous system development and plasticity remains the best characterised. Recent advances suggest that Ephs play an important role in the development of brain pathologies. This review focuses on their basic structure and function and discusses the latest research on their role in neurological diseases.
    PMID: 22265656 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5639394</comments>
            <pubDate>Fri, 13 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5639394</guid>        </item>
        <item>
            <title>Citrate carrier promoter is target of peroxisome proliferator-activated receptor alpha and gamma in hepatocytes and adipocytes.</title>
            <link>http://www.medworm.com/index.php?rid=5621310&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249025%26dopt%3DAbstract</link>
            <description>Authors: Damiano F, Gnoni GV, Siculella L
    Abstract
    Citrate carrier (CiC), a mitochondrial inner membrane protein, is an essential component of the shuttle system which transports acetyl-CoA from mitochondria to the cytosol where lipogenesis occurs. CiC is regulated by SREBP-1, a transcription factor that controls the expression of several lipogenic genes. CiC is also implicated in cholesterol synthesis, glycolysis and gluconeogenesis, suggesting that besides SREBP-1 other transcription factors could modulate the expression of its gene. Here, we provide evidences demonstrating that CiC expression is regulated by peroxisome proliferator-activated receptor (PPAR) alpha and gamma in hepatocytes and adipocytes, respectively. CiC expression increased in rat BRL-3A hepatocytes treated wit...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5621310</comments>
            <pubDate>Tue, 10 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5621310</guid>        </item>
        <item>
            <title>Murine embryonic stem cell-derived hepatocytes correct metabolic liver disease after serial liver repopulation.</title>
            <link>http://www.medworm.com/index.php?rid=5621307&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249028%26dopt%3DAbstract</link>
            <description>In conclusion, ES cell-derived hepatocytes were capable of liver repopulation and correction of metabolic defects after serial transplantation. Our results are an important piece of evidence to support future clinical applications of ES cell-derived hepatocytes in treating liver diseases.
    PMID: 22249028 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5621307</comments>
            <pubDate>Tue, 10 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5621307</guid>        </item>
        <item>
            <title>Presence of urotensin-II receptors at the cell nucleus: Specific tissue distribution and hypoxia induced modulation.</title>
            <link>http://www.medworm.com/index.php?rid=5621312&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22245063%26dopt%3DAbstract</link>
            <description>Authors: Nguyen TT, LÃ©tourneau M, Chatenet D, Fournier A
    Abstract
    Urotensin II (UII) and its receptor UT, is widely expressed in the cardiovascular and central nervous system, where they exert regulatory actions under both physiological and pathological conditions. Our study, aimed at investigating the presence of functional nuclear UT in various rat and monkey tissues as well as in human cell lines, demonstrated for the first time by western blot analysis and confocal immunofluorescence a tissue-specific nuclear expression of this receptor (heart and central nervous system). This nuclear UT was further characterized pharmacologically through radioligand binding studies using specific ligands of the urotensinergic system, as well as somatostatin. In 2D-gel experiments, we have obs...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5621312</comments>
            <pubDate>Mon, 09 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5621312</guid>        </item>
        <item>
            <title>High glucose induces renal mesangial cell proliferation and fibronectin expression through JNK/NF-ÎºB/NADPH oxidase/ROS pathway, which is inhibited by resveratrol.</title>
            <link>http://www.medworm.com/index.php?rid=5621311&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22245600%26dopt%3DAbstract</link>
            <description>Authors: Zhang L, Pang S, Deng B, Qian L, Chen J, Zou J, Zheng J, Yang L, Zhang C, Chen X, Liu Z, Le Y
    Abstract
    Renal hypertrophy and extracellular matrix accumulation are early features of diabetic nephropathy. Hyperglycemia-induced oxidative stress is implicated in the etiology of diabetic nephropathy. Resveratrol has potent antioxidative and protective effects on diabetic nephropathy. We aimed to examine whether high glucose (HG)-induced NADPH oxidase activation and reactive oxygen species (ROS) production contribute to glomerular mesangial cell proliferation and fibronectin expression and the effect of resveratrol on HG action in mesangial cells. By using rat mesangial cell line and primary mesangial cells, we found that NADPH oxidase inhibitor (apocynin) and ROS inhibitor (N-a...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5621311</comments>
            <pubDate>Mon, 09 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5621311</guid>        </item>
        <item>
            <title>Diverse biological functions of the SPARC family of proteins.</title>
            <link>http://www.medworm.com/index.php?rid=5621309&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249026%26dopt%3DAbstract</link>
            <description>Authors: Bradshaw AD
    Abstract
    The SPARC family of proteins represents a diverse group of proteins that modulate cell interaction with the extracellular milieu. The eight members of the SPARC protein family are modular in nature. Each shares a follistatin-like domain and an extracellular calcium binding E-F hand motif. In addition, each family member is secreted into the extracellular space. Some of the shared activities of this family include, regulation of extracellular matrix assembly and deposition, counter-adhesion, effects on extracellular protease activity, and modulation of growth factor/cytokine signaling pathways. Recently, several SPARC family members have been implicated in human disease pathogenesis. This review discusses recent advances in the understanding of the func...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5621309</comments>
            <pubDate>Mon, 09 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5621309</guid>        </item>
        <item>
            <title>Breast cancer stem cells.</title>
            <link>http://www.medworm.com/index.php?rid=5621308&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249027%26dopt%3DAbstract</link>
            <description>Authors: Velasco-VelÃ¡zquez MA, Homsi N, De La Fuente M, Pestell RG
    Abstract
    Breast cancer stem cells (BCSCs) constitute a subpopulation of tumor cells that express stem cell-associated markers and have a high capacity for tumor generation in vivo. Identification of BCSCs from tumor samples or breast cancer cell lines has been based mainly on CD44(+)/CD24(-/low) or ALDH(+) phenotypes. BCSCs isolation has allowed the analysis of the molecular mechanisms involved in their origin, self-renewal, differentiation into tumor cells, resistance to radiation therapy and chemotherapy, and invasiveness and metastatic ability. Molecular genetic analysis using knockout animals and inducible transgenics has identified NF-ÎºB, c-Jun, p21(CIP1), and Forkhead-like-protein Dach1 in BCSC expansion and...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5621308</comments>
            <pubDate>Mon, 09 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5621308</guid>        </item>
        <item>
            <title>The link between small heat shock proteins and the immune system.</title>
            <link>http://www.medworm.com/index.php?rid=5621314&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22233974%26dopt%3DAbstract</link>
            <description>Authors: van Noort JM, Bsibsi M, Nacken P, Gerritsen WH, Amor S
    Abstract
    There is now compelling evidence that members of the family of small heat shock proteins (HSP) can be secreted by a variety of different types of cells. Secretion of small HSP may at times represent altruistic delivery of supporting and stabilizing factors from one cell to another. A probably more general effect of extracellular small HSP, however, is exerted by their ability to activate macrophages and macrophage-like cells. When doing so, small HSP induce an immune-regulatory state of activation, stimulating macrophages to suppress inflammation. For this reason, small HSP deserve consideration as broadly applicable therapeutic agents for inflammatory disorders. In one particular case, however, adaptive immun...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5621314</comments>
            <pubDate>Thu, 05 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5621314</guid>        </item>
        <item>
            <title>Thioredoxin-1 and protein disulfide isomerase catalyze the reduction of similar disulfides in HIV gp120.</title>
            <link>http://www.medworm.com/index.php?rid=5621318&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22230366%26dopt%3DAbstract</link>
            <description>Authors: Reiser K, FranÃ§ois KO, Schols D, Bergman T, JÃ¶rnvall H, Balzarini J, Karlsson A, Lundberg M
    Abstract
    HIV-1 enters cells via interaction of the viral glycoprotein gp120, the host cell surface receptor CD4 and the co-receptors CCR5 or CXCR4. For entry, gp120 undergoes conformational changes that depend on the reduction of one or more disulfides. Previous studies indicate that protein disulfide isomerase (PDI), thioredoxin-1 (Trx1), and glutaredoxin-1 (Grx1) catalyze gp120 reduction, but their specific disulfide targets are not known. Here, it was demonstrated that PDI and Trx1 have similar gp120 disulfide targets as determined by labeling after reduction, but with some pattern differences, including overall stronger labeling with Trx1 than with PDI. Furthermore, uneven lab...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5621318</comments>
            <pubDate>Tue, 03 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5621318</guid>        </item>
        <item>
            <title>Bax inhibitor-1 regulates the expression of P450 2E1 through enhanced lysosome activity.</title>
            <link>http://www.medworm.com/index.php?rid=5621317&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22230367%26dopt%3DAbstract</link>
            <description>In this study, we explored the role of Bax inhibitor-1 (BI-1) on the expression of P450 2E1 and related ROS production. P450 2E1 protein, not mRNA, was expressed at relatively low levels in BI-1 plasmid-transfected cells (BI-1 cells) compared with neomycin-resistant vector-transfected cells (Neo cells). When exposed to ER stress, P450 2E1 expression and activity and ER membrane lipid peroxidation increased in both Neo cells and BI-1 cells, but to a lesser degree in BI-1 cells. This observation correlated with the lower level of ER stress in BI-1 cells than Neo cells. To examine the BI-1-associated P450 2E1 degradation mechanism, cells were treated with the lysosome inhibitor, bafilomycin and the proteasome inhibitor, MG132. Bafilomycin recovered the reduced P450 2E1 expression in BI-1 cell...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5621317</comments>
            <pubDate>Tue, 03 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5621317</guid>        </item>
        <item>
            <title>Adiponectin oligomerization state and adiponectin receptors airway expression in chronic obstructive pulmonary disease.</title>
            <link>http://www.medworm.com/index.php?rid=5621313&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22233975%26dopt%3DAbstract</link>
            <description>In conclusion, we demonstrated that in COPD, the higher levels of Acrp30 are associated with the significantly increase of HMW representing the most biologically active forms. The important role of Acrp30 in pathophysiological conditions of lung is supported also by the modulation of AdipoRs with the down regulation of AdipoR2. The low expression of AdipoR2 could suggest a specific role of this receptor, mainly implicated in Acrp30 effects on inflammation and oxidative stress. Thus, total Acrp30, HMW and its receptors could be considered critical targets to improve diagnostic and therapeutic strategies for lung diseases.
    PMID: 22233975 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5621313</comments>
            <pubDate>Tue, 03 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5621313</guid>        </item>
        <item>
            <title>Cellular retinol-binding protein 1 (CRBP-1) regulates osteogenenesis and adipogenesis of mesenchymal stem cells through inhibiting RXRÎ±-induced Î²-catenin degradation.</title>
            <link>http://www.medworm.com/index.php?rid=5621316&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22230368%26dopt%3DAbstract</link>
            <description>In this study, we investigated the cellular effects of CRBP1 on osteogenic and adipogenic differentiation of bone marrow derived MSCs in vitro and in vivo. Our results showed that CRBP1 overexpression promoted osteogenic differentiation of bone marrow derived MSCs, while inhibited their adipogenic differentiation. We also demonstrated that the possible underlying mechanism for CRBP1 promoting osteogenic differentiation of MSCs was by inhibiting RXRÎ±-induced Î²-catenin degradation, maintaining Î²-catenin and pERK1/2 at higher levels. These findings reveal a potential role of CRBP1 in the regulation of Î²-catenin turnover which can greatly affect the process of osteogenesis and adipogenesis of MSCs.
    PMID: 22230368 [PubMed - as supplied by publisher] (Source: The International Journal of...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5621316</comments>
            <pubDate>Mon, 02 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5621316</guid>        </item>
        <item>
            <title>Long chain ceramides and very long chain ceramides have opposite effects on human breast and colon cancer cell growth.</title>
            <link>http://www.medworm.com/index.php?rid=5621315&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22230369%26dopt%3DAbstract</link>
            <description>Authors: Hartmann D, Lucks J, Fuchs S, Schiffmann S, Schreiber Y, FerreirÃ³s N, Merkens J, Marschalek R, Geisslinger G, GrÃ¶sch S
    Abstract
    Ceramides are known to be key players in intracellular signaling and are involved in apoptosis, cell senescence, proliferation, cell growth and differentiation. They are synthesized by ceramide synthases (CerS). So far, six different mammalian CerS (CerS1-6) have been described. Recently, we demonstrated that human breast cancer tissue displays increased activity of CerS2, 4, and 6, together with enhanced generation of their products, ceramides C(16:0), C(24:0), and C(24:1). Moreover, these increases were significantly associated with tumor dignity. To clarify the impact of this observation, we manipulated cellular ceramide levels by overexpress...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5621315</comments>
            <pubDate>Mon, 02 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5621315</guid>        </item>
        <item>
            <title>The transforming growth factor-beta/bone morphogenetic protein signalling pathway in adipogenesis.</title>
            <link>http://www.medworm.com/index.php?rid=5578126&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22226816%26dopt%3DAbstract</link>
            <description>Authors: Margoni A, Fotis L, Papavassiliou AG
    Abstract
    Rising obesity epidemic makes the better understanding of transcription factor networks regulating adipogenesis very challenging. Adipogenesis begins with the commitment of pluripotent mesenchymal stem cells to the adipocyte lineage, followed by terminal differentiation of preadipocytes to mature adipocytes. Among the molecules that influence the decision of progenitor cells to become adipocytes are members of transforming growth factor-beta superfamily and particularly bone morphogenetic proteins. Transforming growth factor-beta and bone morphogenetic proteins exert their biological functions mainly through their downstream molecules, the Smads. Here, we review the role(s) of transforming growth factor-beta/bone morphogenetic ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5578126</comments>
            <pubDate>Sat, 31 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5578126</guid>        </item>
        <item>
            <title>A portrait of Transforming Growth Factor Î² superfamily signalling: Background matters.</title>
            <link>http://www.medworm.com/index.php?rid=5578125&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22226817%26dopt%3DAbstract</link>
            <description>Authors: Horbelt D, Denkis A, Knaus P
    Abstract
    Ligands of the Transforming Growth Factor Î² superfamily like Transforming Growth Factor Î² and Bone Morphogenetic Proteins govern developmental processes and regulate adult homeostasis by controlling cellular proliferation, survival, differentiation and migration. Aberrant signalling activity is associated with human disorders such as cancer, cardiovascular, musculoskeletal, or fibrotic disease. Upon binding to specific sets of cognate cell surface receptors, family members induce highly similar pathways which include canonical SMAD dependent signalling as well as pathways without direct involvement of SMAD proteins, which activate signalling molecules like mitogen-activated protein kinases or small GTPases. The diverse ligand functio...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5578125</comments>
            <pubDate>Sat, 31 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5578125</guid>        </item>
        <item>
            <title>White adipocytes: More than just fat depots.</title>
            <link>http://www.medworm.com/index.php?rid=5578127&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22222895%26dopt%3DAbstract</link>
            <description>Authors: Henry SL, Bensley JG, Wood-Bradley RJ, Cullen-McEwen LA, Bertram JF, Armitage JA
    Abstract
    Globally 30% of adults are overweight or obese. The white adipocyte is a major component of adipose tissue, and as the obesity epidemic increases it is critically important to understand the factors determining adipocyte development and function. Adipogenesis has two distinct phases; determination of the adipocyte from a multipotent stem cell, and terminal differentiation of a pre-adipocyte into a mature adipocyte. The environment encountered in early life can alter adipocyte number and size and potentially impact upon adipocyte endocrine function in adulthood. These alterations may contribute to the pathophysiology of chronic diseases and thus targeted therapy of the adipocyte has gr...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5578127</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5578127</guid>        </item>
        <item>
            <title>A non-covalent interaction between small ubiquitin-like modifier-1 and Zac1 regulates Zac1 cellular functions.</title>
            <link>http://www.medworm.com/index.php?rid=5578124&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22227369%26dopt%3DAbstract</link>
            <description>Authors: Liu ST, Chang YL, Wang WM, Chung MH, Lin WS, Chou WY, Huang SM
    Abstract
    Zac1, a zinc-finger protein that regulates apoptosis and cell cycle arrest 1, such as p53, can induce cell-cycle arrest and apoptosis. The transactivation and coactivation functions of Zac1 may occur at non-promyelocytic leukemia nuclear body (PML-NB) sites in the presence of other PML-NB components, including ubiquitin-conjugating 9 (Ubc9). It is unclear whether post-translational modification of Zac1 by the small ubiquitin-like modifier SUMO plays a role in the coactivation functions of Zac1 for the regulation of the p21 gene. Mutagenesis experiments revealed that the two SUMO-binding lysine residues of Zac1, K237 and K424, repress the transactivation activity of Zac1. Studies using a SUMO-1 C-termin...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5578124</comments>
            <pubDate>Tue, 27 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5578124</guid>        </item>
        <item>
            <title>Intracellular trafficking of P-glycoprotein.</title>
            <link>http://www.medworm.com/index.php?rid=5578128&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22212176%26dopt%3DAbstract</link>
            <description>Authors: Fu D, Arias IM
    Abstract
    Overexpression of P-glycoprotein (P-gp) is a major cause of multidrug resistance in cancer. P-gp is mainly localized in the plasma membrane and can efflux structurally and chemically unrelated substrates, including anticancer drugs. P-gp is also localized in intracellular compartments, such as endoplasmic reticulum (ER), Golgi, endosomes and lysosomes, and cycles between endosomal compartments and the plasma membrane in a microtubular-actin dependent manner. Intracellular trafficking pathways for P-gp and participation of different Rab proteins depend on cellular polarization and choice of primary culture, cell line or neoplasm. Interruption of P-gp trafficking to the plasma membrane increases intracellular P-gp accumulation and anticancer drug leve...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5578128</comments>
            <pubDate>Sat, 24 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5578128</guid>        </item>
        <item>
            <title>The N-terminal extension is essential for the formation of the active dimeric structure of liver peroxisomal alanine:glyoxylate aminotransferase.</title>
            <link>http://www.medworm.com/index.php?rid=5549740&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22198249%26dopt%3DAbstract</link>
            <description>Authors: Montioli R, Fargue S, Lewin J, Zamparelli C, Danpure CJ, Voltattorni CB, Cellini B
    Abstract
    Alanine:glyoxylate aminotransferase (AGT) is a pyridoxal-phosphate (PLP)-dependent enzyme. Its deficiency causes the hereditary kidney stone disease primary hyperoxaluria type 1. AGT is a highly stable compact dimer and the first 21 residues of each subunit form an extension which wraps over the surface of the neighboring subunit. Naturally occurring and artificial amino acid replacements in this extension create changes in the functional properties of AGT in mammalian cells, including relocation of the enzyme from peroxisomes to mitochondria. In order to elucidate the structural and functional role of this N-terminal extension, we have analyzed the consequences of its removal using...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5549740</comments>
            <pubDate>Mon, 19 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5549740</guid>        </item>
        <item>
            <title>Activation of P2X7R and downstream effects in bleomycin treated lung epithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=5549742&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22192844%26dopt%3DAbstract</link>
            <description>Authors: BlÃ¤sche R, Ebeling G, Srikanth P, Weinhold K, Kasper M, Barth K
    Abstract
    Changes in intracellular calcium concentration [Ca(2+)](i) are believed to influence the proliferation and differentiation of airway epithelial cells both in vivo and in vitro. In the present study, using mouse alveolar epithelial E10 cells, we demonstrated that the treatment of lung epithelial cells with BLM resulted in elevated intracellular Ca(2+) levels. BLM further increased P2rx7 mRNA expression and P2X7R protein levels, paralleled by increased PKC-Î²1 levels. BLM treatment or stimulation of the P2X7R with the P2X7R agonist BzATP induced translocation of PKC-Î²1 from the cytoplasm to the membrane. The expression of PKC-Î²1 was repressed by the P2X7R inhibitor oxATP, suggesting that PKC-Î²1 is d...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5549742</comments>
            <pubDate>Wed, 14 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5549742</guid>        </item>
        <item>
            <title>GATA-2 mediated regulation of normal hematopoietic stem/progenitor cell function, myelodysplasia and myeloid leukemia.</title>
            <link>http://www.medworm.com/index.php?rid=5549741&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22192845%26dopt%3DAbstract</link>
            <description>Authors: Rodrigues NP, Tipping AJ, Wang Z, Enver T
    Abstract
    Unremitting blood cell production throughout the lifetime of an organism is reliant on hematopoietic stem cells (HSCs). A rare and relatively quiescent cell type harbored in adult bone marrow, HSCs are, on entry into cell cycle fated to self-renew, undergo apoptosis or differentiate to progenitors (HPCs) that eventually yield specific classes of blood cells. Disruption of these HSC cell fate decisions is considered to be fundamental to the development of leukemia. Much effort has therefore been placed on understanding the molecular pathways that regulate HSC cell fate decisions and how these processes are undermined during leukemia. Transcription factors have emerged as critical regulators in this respect. Here we review t...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5549741</comments>
            <pubDate>Wed, 14 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5549741</guid>        </item>
        <item>
            <title>Cyclo(His-Pro) exerts anti-inflammatory effects by modulating NF-ÎºB and Nrf2 signalling.</title>
            <link>http://www.medworm.com/index.php?rid=5534318&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22185821%26dopt%3DAbstract</link>
            <description>Authors: Minelli A, Grottelli S, Mierla A, Pinnen F, Cacciatore I, Bellezza I
    Abstract
    Cyclo(His-Pro) is an endogenous cyclic dipeptide that exerts oxidative damage protection by selectively activating the transcription factor Nrf2 signalling pathway. Given the existence of a tight interplay of the Nrf2/NF-ÎºB systems and that the pro-inflammatory response is governed by transcription factor NF-ÎºB, here we sought to investigate whether and how cyclo(His-Pro) interferes with the cross-talk between the antioxidant Nrf2/heme oxygenase-1 and the pro-inflammatory NF-ÎºB pathways. By knocking down the Nrf2 gene, we confirmed that cyclo(His-Pro) inhibits NF-ÎºB nuclear accumulation induced by paraquat in rat pheochromocytoma PC12 cells via the Nrf2/heme oxygenase-1 pathway. The protectio...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534318</comments>
            <pubDate>Wed, 14 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534318</guid>        </item>
        <item>
            <title>X-linked inhibitor of apoptosis protein promotes the degradation of its antagonist, the pro-apoptotic ARTS protein.</title>
            <link>http://www.medworm.com/index.php?rid=5534317&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22185822%26dopt%3DAbstract</link>
            <description>Authors: Bornstein B, Edison N, Gottfried Y, Lev T, Shekhtman A, Gonen H, Rajalingam K, Larisch S
    Abstract
    ARTS (Sept4_i2) is a mitochondrial pro-apoptotic tumor suppressor protein. In response to apoptotic signals, ARTS translocates to the cytosol where it promotes caspase activation through caspase de-repression and proteasome mediated degradation of X-linked Inhibitor of Apoptosis Protein (XIAP). Here we show that XIAP regulates the levels of ARTS by serving as its ubiquitin ligase, thereby providing a potential feedback mechanism to protect against unwanted apoptosis. Using both in vitro and in vivo ubiquitination assays we found that ARTS is directly ubiquitinated by XIAP. Moreover, we found that XIAP-induced ubiquitination and degradation is prevented by removal of the first ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534317</comments>
            <pubDate>Wed, 14 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534317</guid>        </item>
        <item>
            <title>Chromatin structure of the LCR in the human Î²-globin locus transcribing the adult Î´- and Î²-globin genes.</title>
            <link>http://www.medworm.com/index.php?rid=5534320&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22178075%26dopt%3DAbstract</link>
            <description>Authors: Kima S, Kim YW, Shim SH, Kim CG, Kim A
    Abstract
    The Î²-like globin genes are transcribed in a developmental stage specific fashion in erythroid cells. The specific transcription of globin genes is conferred by the locus control region (LCR), but the chromatin structure of the LCR in the human adult Î²-globin locus transcribing the Î´- and Î²-globin genes is not clear. Here, we employed hybrid MEL cells that contain a human chromosome 11. The Î´- and Î²-globin genes were highly transcribed in hybrid MEL/ch11 cells after transcriptional induction. LCR HS3 and HS2 were strongly occupied by erythroid specific transcriptional activators and co-factors in the induced locus. These HSs, but not HS4 and HS1, were in close proximity with the active globin genes as revealed by high r...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534320</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534320</guid>        </item>
        <item>
            <title>Frog skin epithelium: Electrolyte transport and chytridiomycosis.</title>
            <link>http://www.medworm.com/index.php?rid=5534319&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22182598%26dopt%3DAbstract</link>
            <description>Authors: Campbell CR, Voyles J, Cook DI, Dinudom A
    Abstract
    One unique physiological characteristic of frogs is that their main route for intake of water is across the skin. In these animals, the skin acts in concert with the kidney and urinary bladder to maintain electrolyte homeostasis. Water absorption across the skin is driven by the osmotic gradient that develops as a consequence of solute transport. Our recent study demonstrated that chytridiomycosis, an infection of amphibian skin by the fungal pathogen, Batrachochytrium dendrobatidis, inhibits epithelial Na(+) channels, attenuating Na(+) absorption through the skin. In frogs that become severely affected by this fungus, systemic depletion of Na(+), K(+) and Cl(-) is thought to cause deterioration of cardiac electrical funct...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534319</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534319</guid>        </item>
        <item>
            <title>Cdc42: An important regulator of neuronal morphology.</title>
            <link>http://www.medworm.com/index.php?rid=5534322&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22172377%26dopt%3DAbstract</link>
            <description>Authors: Chen C, Wirth A, Ponimaskin E
    Abstract
    Regulation of neuronal morphology and activity-dependent synaptic modifications involves reorganization of the actin cytoskeleton. Dynamic changes of the actin cytoskeleton in many cell types are controlled by small GTPases of the Rho family, such as RhoA, Rac1 and Cdc42. As key regulators of both actin and microtubule cytoskeleton, Rho GTPases have also emerged as important regulators of dendrite and spine structural plasticity. Multiple studies suggest that Rac1 and Cdc42 are positive regulators promoting neurite outgrowth and growth cone protrusion, while the activation of RhoA induces stress fiber formation, leading to growth cone collapse and neurite retraction. This review focuses on recent advances in our understanding of the m...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534322</comments>
            <pubDate>Thu, 08 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534322</guid>        </item>
        <item>
            <title>SDF-1/CXCL12: Its role in spinal cord injury.</title>
            <link>http://www.medworm.com/index.php?rid=5534321&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22172378%26dopt%3DAbstract</link>
            <description>Authors: Jaerve A, Bosse F, MÃ¼ller HW
    Abstract
    The chemokine stromal cell-derived factor 1 (SDF-1/CXCL12), is not only the most ancient, but also one of the most potent chemotactic factors. Orchestrating the migration of cells as well as promoting axon outgrowth in the presence of myelin inhibitors, SDF-1 is fundamental to central nervous system development, homeostasis and traumatic injury. SDF-1 attracts endogenous stem/precursor cells and immune cells to the injury site and, upon local infusion, enhances axonal sprouting following spinal cord injury. Together these features make SDF-1 a very exciting molecule for spinal cord repair.
    PMID: 22172378 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534321</comments>
            <pubDate>Thu, 08 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534321</guid>        </item>
        <item>
            <title>NCAM2/OCAM/RNCAM: Cell adhesion molecule with a role in neuronal compartmentalization.</title>
            <link>http://www.medworm.com/index.php?rid=5534325&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22155300%26dopt%3DAbstract</link>
            <description>Authors: Winther M, Berezin V, Walmod PS
    Abstract
    Neural cell adhesion molecules 2 (NCAM2/OCAM/RNCAM), is a paralog of NCAM1. The protein exists in a transmembrane and a lipid-anchored isoform, and has an ectodomain consisting of five immunoglobulin modules and two fibronectin type 3 homology modules. Structural models of the NCAM2 ectodomain reveal that it facilitates cell adhesion through reciprocal interactions between the membrane-distal immunoglobulin modules. There are no known heterophilic NCAM2 binding partners, and NCAM2 is not glycosylated with polysialic acid, a posttranslational modification known to be a major modulator of NCAM1-mediated processes. This suggests that NCAM2 has a function or mode of action distinctly different from that of NCAM1. NCAM2 is primarily expr...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534325</comments>
            <pubDate>Fri, 02 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534325</guid>        </item>
        <item>
            <title>Withanone binds to mortalin and abrogates mortalin-p53 complex: Computational and experimental evidence.</title>
            <link>http://www.medworm.com/index.php?rid=5534323&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22155302%26dopt%3DAbstract</link>
            <description>We report the molecular dynamic simulations revealing the thermodynamic and structural stability of the withanone-mortalin complexes. We also demonstrate the experimental evidence of abrogation of mortalin-p53 complex by withanone resulting in nuclear translocation and functional reactivation of p53 in human cancer cells. The present study establishes a molecular interaction basis that could be used for screening and development of anticancer drugs with low toxicity to normal cells. Accurate knowledge of the 3D structure of mortalin would further enhance the potential of such analyses to understand the molecular basis of mortalin biology and mortalin based cancer therapy.
    PMID: 22155302 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biol...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534323</comments>
            <pubDate>Fri, 02 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534323</guid>        </item>
        <item>
            <title>Angiotensin signalling in pulmonary fibrosis.</title>
            <link>http://www.medworm.com/index.php?rid=5534324&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22155301%26dopt%3DAbstract</link>
            <description>Authors: Uhal BD, Li X, Piasecki CC, Molina-Molina M
    Abstract
    A large body of evidence demonstrates that angiotensin II and angiotensin receptors are required for the pathogenesis of experimental lung fibrosis. Angiotensin has a number of profibrotic effects on lung parenchymal cells that include the induction of growth factors for mesenchymal cells, extracellular matrix molecules, cytokines and increased motility of lung fibroblasts. Angiotensin is also proapoptotic for lung epithelial cells, and is synthesized by a local system (i.e., entirely within the lung tissue) after lung injury by a variety of agents of both xenobiotic and endogenous origins. Recent evidence shows that the counterregulatory molecule angiotensin 1-7, the product of the enzyme ACE-2, inhibits epithelial cell...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534324</comments>
            <pubDate>Wed, 30 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534324</guid>        </item>
        <item>
            <title>Upregulation of Polo-like kinase 2 gene expression by GATA-1 acetylation in human osteosarcoma MG-63 cells.</title>
            <link>http://www.medworm.com/index.php?rid=5534330&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22138223%26dopt%3DAbstract</link>
            <description>Authors: Shen T, Li Y, Yang L, Xu X, Liang F, Liang S, Ba G, Xue F, Fu Q
    Abstract
    Polo-like kinase 2 (Plk2) is a member of the serine/threonine protein kinase family involved in cell-cycle regulation and cellular response to stresses. It is of great interest to investigate the molecular mechanisms that control the expression of Plk2. Here, using real-time PCR and Western blot assays, we show that trichostatin A (TSA), a histone deacetylase inhibitor, upregulated Plk2 mRNA and protein expression in the human osteosarcoma MG-63 cell line. Luciferase activity analysis of the truncated Plk2 promoter indicated that the region from -1220 to -830 of the Plk2 promoter was sensitive to TSA. Moreover, using the electrophoresis mobility shift assay and chromatin immunoprecipitation assay, we ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534330</comments>
            <pubDate>Mon, 28 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534330</guid>        </item>
        <item>
            <title>Increase in cell viability by polyamines through stimulation of the synthesis of ppGpp regulatory protein and Ï‰ protein of RNA polymerase in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5534328&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22138225%26dopt%3DAbstract</link>
            <description>Authors: Terui Y, Akiyama M, Sakamoto A, Tomitori H, Yamamoto K, Ishihama A, Igarashi K, Kashiwagi K
    Abstract
    It is known that polyamines increase cell growth through stimulation of the synthesis of several kinds of proteins encoded by the so-called &quot;polyamine modulon&quot;. We recently reported that polyamines also increase cell viability at the stationary phase of cell growth through stimulation of the synthesis of ribosome modulation factor, a component of the polyamine modulon. Accordingly, we looked for other proteins involved in cell viability whose synthesis is stimulated by polyamines. It was found that the synthesis of ppGpp regulatory protein (SpoT) and Ï‰ protein of RNA polymerase (RpoZ) was stimulated by polyamines at the level of translation. Stimulation of the synthesis of...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534328</comments>
            <pubDate>Mon, 28 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534328</guid>        </item>
        <item>
            <title>Inhibition of MT1-MMP activity using functional antibody fragments selected against its hemopexin domain.</title>
            <link>http://www.medworm.com/index.php?rid=5534329&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22138224%26dopt%3DAbstract</link>
            <description>Authors: Basu B, Correa de Sampaio P, Mohammed H, Fogarasi M, Corrie P, Watkins NA, Smethurst PA, English WR, Ouwehand WH, Murphy G
    Abstract
    The membrane associated MMP, MT1-MMP, is a critical pericellular protease involved in tumour cell invasion and angiogenesis and is highly up-regulated in numerous human cancers. It therefore represents an exciting new therapeutic cancer-specific target. We have generated recombinant human scFv antibodies against the non-catalytic, hemopexin domain of MT1-MMP that modulate its interactions with collagen. One of these is an effective inhibitor of the invasive capacity of cancer cells and of angiogenesis in model systems. This demonstrates that targeting sites outside the catalytic domain presents a potential novel approach to proteinase inhibiti...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534329</comments>
            <pubDate>Sat, 26 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534329</guid>        </item>
        <item>
            <title>Dissection of Drosophila MTF-1 reveals a domain for differential target gene activation upon copper overload vs. copper starvation.</title>
            <link>http://www.medworm.com/index.php?rid=5534327&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22138226%26dopt%3DAbstract</link>
            <description>Authors: GÃ¼nther V, Waldvogel D, Nosswitz M, Georgiev O, Schaffner W
    Abstract
    Metal-responsive transcription factor-1 (MTF-1) is a zinc finger protein conserved from mammals to insects. It mediates protection against heavy metal load by activating the expression of metallothionein and other genes. In Drosophila, MTF-1 serves a dual function in that it not only helps to protect against heavy metal load but also induces the expression of Ctr1B, the gene for an intestinal copper importer, upon copper starvation. By dissecting Drosophila MTF-1 function, we have identified determinants for nuclear import and export, and characterized a phosphorylation site mutant (T127A) that differentially affects MTF-1 target genes. Further, by generating a series of fusion proteins with the heterolo...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534327</comments>
            <pubDate>Sat, 26 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534327</guid>        </item>
        <item>
            <title>A splicing variant leads to complete loss of function of betaine-homocysteine methyltransferase (BHMT) gene in hepatocellular carcinoma.</title>
            <link>http://www.medworm.com/index.php?rid=5534326&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22138536%26dopt%3DAbstract</link>
            <description>In conclusion, a transcription variant of exon 4 produces a loss of function of BHMT in human hepatocarcinoma. Whether this abnormal transcription of BHMT is part or consequence of liver carcinogenesis should deserve further investigations.
    PMID: 22138536 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534326</comments>
            <pubDate>Sat, 26 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534326</guid>        </item>
        <item>
            <title>PPARÎ³ suppression inhibits adipogenesis but does not promote osteogenesis of human mesenchymal stem cells.</title>
            <link>http://www.medworm.com/index.php?rid=5456182&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22120652%26dopt%3DAbstract</link>
            <description>In this study, using human MSCs as an in vitro model, we showed that the two isoforms of PPARÎ³, PPARÎ³1 and PPARÎ³2, were differentially induced during hMSC adipogenesis, whereas only PPARÎ³1 was detected during osteogenesis. BADGE and GW9662, two potential antagonists of PPARÎ³, as well as lentivirus-mediated knockdown of PPARÎ³, inhibited hMSC adipogenesis but did not significantly affect osteogenesis. PPARÎ³ knockdown did not significantly influence the expression level of the osteogenic transcription factor Runx2. Together, these results suggest that PPARÎ³ is not the master factor regulating mesenchymal lineage determination in human bone marrow.
    PMID: 22120652 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5456182</comments>
            <pubDate>Wed, 23 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5456182</guid>        </item>
        <item>
            <title>TGF-Î²-induced miR-21 negatively regulates the antiproliferative activity but has no effect on EMT of TGF-Î² in HaCaT cells.</title>
            <link>http://www.medworm.com/index.php?rid=5456183&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22119803%26dopt%3DAbstract</link>
            <description>Authors: Wang T, Zhang L, Shi C, Sun H, Wang J, Li R, Zou Z, Ran X, Su Y
    Abstract
    The transforming growth factor-Î² (TGF-Î²) signaling pathway plays important roles in maintaining normal tissue homeostasis, and is tightly controlled by a network of biomolecules. MicroRNAs (miRNAs) are small noncoding RNAs of âˆ¼22 nucleotides that regulate gene expression at posttranscriptional levels. Increasing evidence points to the important role of miRNAs in TGF-Î² signaling. OncomicroRNA miR-21 has been established as a key regulator of mesenchymal phenotype transition induced by TGF-Î². However, the effects of miR-21 on epithelial biology involved in TGF-Î² signaling pathway such as cytostatic program and epithelial to mesenchymal transition (EMT) processes are unclear. Here we show that miR...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5456183</comments>
            <pubDate>Tue, 22 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5456183</guid>        </item>
        <item>
            <title>UTF1 deficiency promotes retinoic acid-induced neuronal differentiation in P19 embryonal carcinoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=5456187&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22107969%26dopt%3DAbstract</link>
            <description>Authors: Lin CH, Yang CH, Chen YR
    Abstract
    UTF1 (undifferentiated embryonic cell transcription factor 1) is a marker for the pluripotency of embryonic stem cells. We found that UTF1-deficient clones, which were isolated from P19 embryonal carcinoma (EC) cells, showed higher neuron-differentiating potentials than the parental cell line. Consistent with this result, suppression of UTF1 expression in P19 cells by RNA interference enhanced retinoic acid (RA)-induced neuronal differentiation. Moreover, reconstitution of UTF1 expression in UTF1-deficient clones decreased their ability to undergo neuronal differentiation. Interestingly, the growth rates of UTF1-deficient P19 cells did not differ from that of parental cells in adherent cultures, but were increased in embryoid bodies during...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5456187</comments>
            <pubDate>Thu, 17 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5456187</guid>        </item>
        <item>
            <title>EBV encoded miR-BHRF1-1 potentiates viral lytic replication by downregulating host p53 in nasopharyngeal carcinoma.</title>
            <link>http://www.medworm.com/index.php?rid=5456186&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22108199%26dopt%3DAbstract</link>
            <description>Authors: Li Z, Chen X, Li L, Liu S, Yang L, Ma X, Tang M, Bode AM, Dong Z, Sun L, Cao Y
    Abstract
    miRNAs (microRNAs) are a class of non-coding small RNAs. The Epstein-Barr-virus (EBV) encoded miR-BHRF1-1 is barely expressed in most nasopharyngeal carcinoma (NPC) cells with EBV latent infection. Here, we used a strategy of overexpression and inhibition of miR-BHRF1-1 and showed that miR-BHRF1-1 is involved in TPA-induced accumulation of EBV lytic proteins and viral copies in late lytic cycle. The data further suggested that the miR-BHRF1-1-potentiated induction of EBV lytic replication was accompanied by inhibiting p53 expression. Our results demonstrated that the EBV original pathogen miR-BHRF1-1 is involved in the control of EBV late lytic replication by directly targeting the host...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5456186</comments>
            <pubDate>Thu, 17 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5456186</guid>        </item>
        <item>
            <title>Interplay between microtubule dynamics and intracellular organization.</title>
            <link>http://www.medworm.com/index.php?rid=5456185&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22108200%26dopt%3DAbstract</link>
            <description>Authors: de Forges H, Bouissou A, Perez F
    Abstract
    Microtubules are hollow tubes essential for many cellular functions such as cell polarization and migration, intracellular trafficking and cell division. They are polarized polymers composed of Î± and Î² tubulin that are, in most cells, nucleated at the centrosome at the center of the cell. Microtubule plus-ends are oriented towards the periphery of the cell and explore the cytoplasm in a very dynamic manner. Microtubule alternate between phases of growth and shrinkage in a manner described as dynamic instability. Their dynamics is highly regulated by multiple factors: tubulin post-translational modifications such as detyrosination or acetylation, and microtubule-associated proteins, among them the plus-tip tracking proteins. This ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5456185</comments>
            <pubDate>Thu, 17 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5456185</guid>        </item>
        <item>
            <title>Intermolecular association between caspase-mediated cleavage fragments of phospholipase D1 protects against apoptosis.</title>
            <link>http://www.medworm.com/index.php?rid=5456184&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22108201%26dopt%3DAbstract</link>
            <description>Authors: Jang YH, Min DS
    Abstract
    Phospholipase D plays an anti-apoptotic role but little is known about dynamics of phospholipase D turnover during apoptosis. We have recently identified phospholipase D1 as a new substrate of caspases which generates the N-terminal and C-terminal fragment of phospholipase D1. In the present study, we tried to investigate whether association of the caspase cleavage fragments may be involved in regulation of apoptosis. Ectopically expressed C-terminal fragment, but not N-terminal fragment of phospholipase D1, is exclusively imported into the nucleus via a nuclear localization sequence; however, endogenous C-terminal fragment of phospholipase D1 from etoposide-induced apoptotic cells and Alzheimer's disease brain tissues with active caspase-3, was lo...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5456184</comments>
            <pubDate>Thu, 17 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5456184</guid>        </item>
        <item>
            <title>Identification of specific miRNAs targeting proteins of the apical junctional complex that simulate the probiotic effect of E. coli Nissle 1917 on T84 epithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=5456188&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22101077%26dopt%3DAbstract</link>
            <description>This study identifies miRNAs involved in the maintenance of intercellular junctions and barrier integrity. For the functional identification of barrier affecting miRNAs, we took advantage of the barrier-enforcing effects of the probiotic bacterium Escherichia coli Nissle 1917 (EcN) which can be monitored by enhanced transepithelial resistance (TER). miRNA-profiling of T84 monolayers prior and after co-incubation with EcN revealed for the first time differentially regulated miRNAs (miR-203, miR-483-3p, miR-595) targeting tight junction (TJ) proteins. Using real-time PCR, Western blotting and specific miRNA mimics, we showed that these miRNAs are involved in the regulation of barrier function by modulating the expression of regulatory and structural components of tight junctional complexes. ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5456188</comments>
            <pubDate>Tue, 15 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5456188</guid>        </item>
        <item>
            <title>Myostatin inhibits brown adipocyte differentiation via regulation of Smad3-mediated Î²-catenin stabilization.</title>
            <link>http://www.medworm.com/index.php?rid=5456192&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22094186%26dopt%3DAbstract</link>
            <description>Authors: Kim WK, Choi HR, Park SG, Ko Y, Bae KH, Lee SC
    Abstract
    Brown adipocytes play an important role in regulating energy balance, and there is a good correlation between obesity and the amount of brown adipose tissue. Although the molecular mechanism of white adipocyte differentiation has been well characterized, brown adipogenesis has not been studied extensively. Moreover, extracellular factors that regulate brown adipogenic differentiation are not fully understood. Here, we assessed the mechanism of the regulatory action of myostatin in brown adipogenic differentiation using primary brown preadipocytes. Our results clearly showed that differentiation of brown adipocytes was significantly inhibited by myostatin treatment. In addition, myostatin-induced suppression of brown a...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5456192</comments>
            <pubDate>Fri, 11 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5456192</guid>        </item>
        <item>
            <title>A comparison of glycine- and ivermectin-mediated conformational changes in the glycine receptor ligand-binding domain.</title>
            <link>http://www.medworm.com/index.php?rid=5456191&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22094187%26dopt%3DAbstract</link>
            <description>Authors: Wang Q, Lynch JW
    Abstract
    Glycine receptor chloride channels are Cys-loop receptor proteins that isomerize between a low affinity closed state and a high affinity ion-conducting state. There is currently much interest in understanding the mechanisms that link affinity changes with conductance changes. This essentially involves an agonist binding in the glycine receptor ligand-binding site initiating local conformational changes that propagate in a wave towards the channel gate. However, it has proved difficult to convincingly distinguish those agonist-induced domain movements that are critical for triggering activation from those that are simply local deformations to accommodate ligands in the site. We employed voltage-clamp fluorometry to compare conformational changes in...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5456191</comments>
            <pubDate>Fri, 11 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5456191</guid>        </item>
        <item>
            <title>Molecular analysis of Plasmodium falciparum co-chaperone Aha1 supports its interaction with and regulation of Hsp90 in the malaria parasite.</title>
            <link>http://www.medworm.com/index.php?rid=5456189&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22100910%26dopt%3DAbstract</link>
            <description>In this study, a putative co-chaperone P. falciparum Aha1 (PfAha1) was identified and investigated for its interaction and regulation of PfHsp90. A previous genome-wide yeast two-hybrid study failed to identify PfAha1's association with PfHsp90, which prompted us to use a directed assay to investigate their interaction. PfAha1 was shown to interact with PfHsp90 via the in vivo split-ubiquitin assay and the association was confirmed in vitro by GST pull-down experiments. The GST pull-down assay further revealed PfAha1's interaction with PfHsp90 to be dependent on MgCl(2) and ATP, and was competed by co-chaperone Pfp23 that binds PfHsp90 under the same condition. In addition, the PfHsp90-PfAha1 complex was found to be sensitive to disruption by high salt, indicating a polar interaction betwe...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5456189</comments>
            <pubDate>Fri, 11 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5456189</guid>        </item>
        <item>
            <title>Four-and-a-half-LIM protein 1 down-regulates estrogen receptor Î± activity through repression of AKT phosphorylation in human breast cancer cell.</title>
            <link>http://www.medworm.com/index.php?rid=5456190&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22094188%26dopt%3DAbstract</link>
            <description>Authors: Zhang F, Feng F, Yang P, Li Z, You J, Xie W, Gao X, Yang J
    Abstract
    The Four-and-a-half LIM protein 1 (FHL-1) is a member of LIM-only protein family. It plays important roles in proliferation and apoptosis regulation of certain hepatocellular carcinoma and human breast cancer. Estrogen receptor Î± (ERÎ±) is involved in the development and progression of human breast cancer. IGF/PI3K/AKT signaling pathway also plays certain roles in the program and regulation of human breast cancer and ovary cancer. However, the biological function of FHL-1 in regulation of human breast cancer and in the cross-talk of estrogen and IGF signaling pathway remains largely unknown. In this paper, we show that FHL-1 protein interacts with ERÎ± and AKT. FHL-1 represses the translation and transcri...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5456190</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5456190</guid>        </item>
        <item>
            <title>Oxaloacetate: A novel neuroprotective for acute ischemic stroke.</title>
            <link>http://www.medworm.com/index.php?rid=5419652&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22085530%26dopt%3DAbstract</link>
            <description>Authors: Campos F, Sobrino T, Ramos-Cabrer P, Castillo J
    Abstract
    It is well established that glutamate acts as an important mediator of neuronal degeneration during cerebral ischemia. Different kind of glutamate antagonists have been used to reduce the deleterious effects of glutamate. However, their preclinical success failed to translate into practical treatments. Far from the classical use of glutamate antagonists employed so far, the systemic administration of oxaloacetate represents a novel neuroprotective strategy to minimize the deleterious effect of glutamate in the brain tissue after ischemic stroke. The neuroprotective effect of oxaloacetate is based on the capacity of this molecule to reduce the brain and blood glutamate levels as a result of the activation of the blood...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419652</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419652</guid>        </item>
        <item>
            <title>A butyrolactone derivative suppressed lipopolysaccharide-induced autophagic injury through inhibiting the autoregulatory loop of p8 and p53 in vascular endothelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=5419651&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22085531%26dopt%3DAbstract</link>
            <description>The objective of the present study is to investigate whether and how 3BDO inhibits LPS-induced VEC autophagic injury. Our results showed that LPS induced autophagy and led to increase of reactive oxygen species (ROS) and decrease of mitochondrial membrane potential (MMP) in Human umbilical vein vascular endothelial cells (HUVECs). Furthermore, LPS significantly increased p8 and p53 protein levels and the nuclear translocation of p53. All of these effects of LPS on HUVECs were strongly inhibited by 3BDO. Importantly, the ROS scavenger N-acetylcysteine (NAC) could inhibited LPS-induced autophagy and knockdown of p8 by RNA interference inhibited the autophagy, p53 protein level increase, the translocation of p53 into nuclei and the ROS level increase induced by LPS in HUVECs. The data suggest...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419651</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419651</guid>        </item>
        <item>
            <title>Both mitogen-activated protein kinase (MAPK)/extracellular-signal-regulated kinases (ERK) 1/2 and phosphatidylinositide-3-OH kinase (PI3K)/Akt pathways regulate activation of E-twenty-six (ETS)-like transcription factor 1 (Elk-1) in U138 glioblastoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=5419653&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22085529%26dopt%3DAbstract</link>
            <description>Authors: Mut M, Lule S, Demir O, Kurnaz IA, Vural I
    Abstract
    Epidermal growth factor (EGF) and its receptor (EGFR) have been shown to play a significant role in the pathogenesis of glioblastoma. In our study, the EGFR was stimulated with EGF in human U138 glioblastoma cells. We show that the activated mitogen-activated protein kinase (MAPK)/extracellular-signal-regulated kinases (ERK) 1/2 pathway phosphorylated the E twenty-six (ETS)-like transcription factor 1 (Elk-1) mainly at serine 383 residue. Mitogen-activated protein kinase kinase (MEK) 1/2 inhibitor, UO126 and ERK inhibitor II, FR180204 blocked the Elk-1 phosphorylation and activation. The phosphatidylinositide-3-OH kinase (PI3K)/Akt pathway was also involved in the Elk-1 activation. Activation of the Elk-1 led to an increa...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419653</comments>
            <pubDate>Mon, 07 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419653</guid>        </item>
        <item>
            <title>Activation of VEGFR-2 signaling in response to moderate dose of ultraviolet B promotes survival of normal human keratinocytes.</title>
            <link>http://www.medworm.com/index.php?rid=5419664&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22062947%26dopt%3DAbstract</link>
            <description>Authors: Zhu JW, Wu XJ, Luo D, Lu ZF, Cai SQ, Zheng M
    Abstract
    Mounting evidence indicates that signaling via VEGF receptors (VEGFRs) extends beyond blood vessel formation. Recently, VEGFRs are also found to be constitutively expressed in keratinocytes and epidermal appendages. Here, we show that the expression of VEGFRs (including VEGFR-1, VEGFR-2, and NRP-1) was significantly enhanced by moderate dose of ultraviolet B (UVB) in normal human keratinocytes and epidermis. The elevated expression of VEGFRs by UVB was independent of autocrine stimulation by their natural ligand, VEGF, but mainly mediated through hypoxia and oxidative stress. Moderate dose UVB also promoted tyrosine phosphorylation of VEGFR-1 and VEGFR-2, this effect was again VEGF independent. Both Î± and Î´ isoforms o...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419664</comments>
            <pubDate>Thu, 03 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419664</guid>        </item>
        <item>
            <title>Endoplasmic reticulum stress signaling is involved in silver nanoparticles-induced apoptosis.</title>
            <link>http://www.medworm.com/index.php?rid=5419659&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22064246%26dopt%3DAbstract</link>
            <description>Authors: Zhang R, Piao MJ, Kim KC, Kim AD, Choi JY, Choi J, Hyun JW
    Abstract
    Although silver nanoparticles (AgNPs) have been reported to exert strong acute toxic effects on various cultured cells by inducing oxidative stress, the molecular mechanisms by which AgNPs-damaged cells are unknown. Because the endoplasmic reticulum (ER) may play an important role in the response to oxidative stress-induced damage and is quite sensitive to oxidative damage, we hypothesized that AgNPs may exert cytotoxic effects on cells by modulating ER stress. In our study, AgNPs resulted in cytotoxicity and apoptotic cell death when analyzing cell viability, DNA fragmentation and the apoptotic sub-G(1) population. Flow cytometry and confocal microscopy indicated that the cells were sensitive to AgNPs wit...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419659</comments>
            <pubDate>Thu, 03 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419659</guid>        </item>
        <item>
            <title>Overexpression of polo-like kinase 1 and its clinical significance in human non-small cell lung cancer.</title>
            <link>http://www.medworm.com/index.php?rid=5419658&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22064247%26dopt%3DAbstract</link>
            <description>Authors: Wang ZX, Xue D, Lu BB, Bian HB, Pan X, Yin YM
    Abstract
    Polo-like kinase 1 is a serine/threonine kinase which plays an essential role in mitosis and malignant transformation. The aim of this study was to investigate the prognostic significance of polo-like kinase 1 expression and determine its possibility as a therapeutic target in non-small cell lung cancer. Semi-quantitative RT-PCR assay was performed to detect polo-like kinase 1 mRNA expression in non-small cell lung cancer cells or tissues. Immunohistochemistry was performed to detect polo-like kinase 1 protein expression in 100 non-small cell lung cancer tissue samples, and the associations of polo-like kinase 1 expression with clinicopathological factors or prognosis of non-small cell lung cancer patients were evaluat...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419658</comments>
            <pubDate>Thu, 03 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419658</guid>        </item>
        <item>
            <title>Cooperativity between inhibition of cytosolic K+ efflux and AMPK activation during suppression of hypoxia-induced cellular apoptosis.</title>
            <link>http://www.medworm.com/index.php?rid=5419657&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22064248%26dopt%3DAbstract</link>
            <description>In conclusion, our study highlights a novel bimodal effect wherein cooperativity between restoration of K+ homeostasis and a sustainable 'metabolic quiescence' induced by AMPK activation appeared indispensible for curtailing hypoxia-induced apoptosis.
    PMID: 22064248 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419657</comments>
            <pubDate>Thu, 03 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419657</guid>        </item>
        <item>
            <title>Chromatin remodelling protein SMAR1 inhibits p53 dependent transactivation by regulating acetyl transferase p300.</title>
            <link>http://www.medworm.com/index.php?rid=5419656&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22074660%26dopt%3DAbstract</link>
            <description>Authors: Sinha S, Malonia SK, Mittal SP, Mathai J, Pal JK, Chattopadhyay S
    Abstract
    Acetylation of p53 is indispensable for its transcriptional activities and induction of apoptosis upon DNA damage. Here, we show that chromatin remodelling protein SMAR1 inhibits p53 acetylation and p53 dependent apoptosis by repressing p300 expression in response to DNA damage. The repression of p300 expression by SMAR1 is relieved upon treatment with proteosomal inhibitors MG132 and Lactacystin. We demonstrate that SMAR1 interacts with p53-p300 transcriptional complex and SMAR1 overexpression antagonizes p300 interaction with p53 and suppresses activation of p53 apoptotic targets and p53 regulated miRNA miR-34a. Conversely, knockdown of SMAR1 promotes p300 accumulation and p53 acetylation while ec...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419656</comments>
            <pubDate>Thu, 03 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419656</guid>        </item>
        <item>
            <title>Comparative proteomic analysis to dissect differences in signal transduction in activating TSH receptor mutations in the thyroid.</title>
            <link>http://www.medworm.com/index.php?rid=5419655&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22074661%26dopt%3DAbstract</link>
            <description>This study revealed (1) differences in the expression of Rab proteins suggesting an increased TSHR internalization in mutTSHR but not in the WT-TSHR; (2) differential stimulation of PI3K/Akt signaling in mutTSHR vs. WT-TSHR cells, (3) activation of Epac, impairing short-time Akt phosphorylation in both, mutTSHR and WT-TSHR cells. Based on the analysis of global changes in protein expression patterns, our findings underline the complexity of gain-of-function TSHR signaling in thyrocytes, which extends beyond pure cAMP and/or IP formation. Moreover, evidence for augmented endocytosis in the mutTSHR, adds to a new concept of TSHR signaling in thyroid autonomy. Further studies are required to clarify whether the observed differences in Rab, PI3K and Epac signaling may contribute to differences...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419655</comments>
            <pubDate>Thu, 03 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419655</guid>        </item>
        <item>
            <title>Pigment epithelium-derived factor reduces the PDGF-induced migration and proliferation of human aortic smooth muscle cells through PPARÎ³ activation.</title>
            <link>http://www.medworm.com/index.php?rid=5419654&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22074662%26dopt%3DAbstract</link>
            <description>Authors: Wang SH, Liang CJ, Wu JC, Huang JJ, Chien HF, Tsai JS, Yen YS, Tseng YC, Lue JH, Chen YL
    Abstract
    Our previous study demonstrated that pigment epithelium-derived factor (PEDF) plays an important role in the proliferation and migration of human aortic smooth muscle cells (HASMCs). In the present study, we examined whether PEDF inhibited platelet-derived growth factor (PDGF)-stimulated HASMC migration and proliferation. PEDF dose-dependently reduced PDGF-induced HASMC migration and proliferation in vitro and also arrested cell cycle progression in the G0/G1 phase, and this was associated with decreased expression of cyclin D1, cyclin E, CDK2, CDK4, and p21(Cip1) and increased expression of the cyclin-dependent kinase inhibitor p27(Kip1). The antiproliferative and antimigrato...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419654</comments>
            <pubDate>Thu, 03 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419654</guid>        </item>
        <item>
            <title>RhoA and Rho kinase mediate cyclosporine A and sirolimus-induced barrier tightening in renal proximal tubular cells.</title>
            <link>http://www.medworm.com/index.php?rid=5419663&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22062948%26dopt%3DAbstract</link>
            <description>Authors: Martin-Martin N, Dan Q, Amoozadeh Y, Waheed F, McMorrow T, Ryan MP, SzÃ¡szi K
    Abstract
    The regulation and maintenance of the paracellular transport in renal tubular epithelia is vital for kidney functions. Combination of the immunosuppressant drugs cyclosporine A (CsA) and sirolimus (SRL) exerts powerful immunosuppression, but also causes nephrotoxicity. We have previously shown that CsA and SRL elevate transepithelial resistance (TER) in kidney tubular cells partly through MEK/ERK1/2. In this work we examined the hypothesis that the RhoA pathway in the barrier may also be mediating effects of CsA and SRL. We show that CsA and the CsA/SRL combination activated RhoA, induced cofilin phosphorylation and promoted stress fiber generation. The Rho kinase (ROK) inhibitor, Y27632...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419663</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419663</guid>        </item>
        <item>
            <title>MicroRNA212/132 family: Molecular transducer of neuronal function and plasticity.</title>
            <link>http://www.medworm.com/index.php?rid=5419662&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22062950%26dopt%3DAbstract</link>
            <description>Authors: Tognini P, Pizzorusso T
    Abstract
    MicroRNAs (miRNAs) are small non-coding RNAs that mediate post-transcriptional gene silencing. It is increasingly clear that miRNAs are key regulatory factors for a tight gene expression control. MiRNAs are involved in many aspects of organism development and function, in physiological and pathological conditions. MiRNA expression varies with cell type, tissue and developmental stages. The microRNA212/132 family is one of the most studied miRNA family due to the involvement of miR132 and miR212 in important cellular processes, especially in the brain. MiR132 and miR212 have been implicated in tissue development and in the formation and plasticity of neuronal connections. The main aim of this review is to highlight recent discoveries about m...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419662</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419662</guid>        </item>
        <item>
            <title>Characterization of glyceraldehyde-3-phosphate dehydrogenase as a novel transferrin receptor.</title>
            <link>http://www.medworm.com/index.php?rid=5419661&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22062951%26dopt%3DAbstract</link>
            <description>Authors: Kumar S, Sheokand N, Mhadeshwar MA, Raje CI, Raje M
    Abstract
    A majority of cells obtain of transferrin (Tf) bound iron via transferrin receptor 1 (TfR1) or by transferrin receptor 2 (TfR2) in hepatocytes. Our study establishes that cells are capable of acquiring transferrin iron by an alternate pathway via GAPDH. These findings demonstrate that upon iron depletion, GAPDH functions as a preferred receptor for transferrin rather than TfR1 in some but not all cell types. We utilized CHO-TRVb cells that do not express TfR1 or TfR2 as a model system. A knockdown of GAPDH in these cells resulted in a decrease of not only transferrin binding but also associated iron uptake. The current study also demonstrates that, unlike TfR1 and TfR2 which are localized to a specific membrane f...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419661</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419661</guid>        </item>
        <item>
            <title>Endoplasmic reticulum: ER stress regulates mitochondrial bioenergetics.</title>
            <link>http://www.medworm.com/index.php?rid=5419660&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22064245%26dopt%3DAbstract</link>
            <description>Authors: Bravo R, Gutierrez T, Paredes F, Gatica D, Rodriguez AE, Pedrozo Z, Chiong M, Parra V, Quest AF, Rothermel BA, Lavandero S
    Abstract
    Endoplasmic reticulum (ER) stress activates an adaptive unfolded protein response (UPR) that facilitates cellular repair, however, under prolonged ER stress, the UPR can ultimately trigger apoptosis thereby terminating damaged cells. The molecular mechanisms responsible for execution of the cell death program are relatively well characterized, but the metabolic events taking place during the adaptive phase of ER stress remain largely undefined. Here we discuss emerging evidence regarding the metabolic changes that occur during the onset of ER stress and how ER influences mitochondrial function through mechanisms involving calcium transfer, the...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419660</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419660</guid>        </item>
        <item>
            <title>Biochemical and molecular analysis of the interaction between ERK2 MAP kinase and hypoxia inducible factor-1Î±.</title>
            <link>http://www.medworm.com/index.php?rid=5279760&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21807114%26dopt%3DAbstract</link>
            <description>Authors: Karapetsas A, Giannakakis A, Pavlaki M, Panayiotidis M, Sandaltzopoulos R, Galanis A
    Abstract
    The mitogen activated protein kinase (MAPK) signaling pathways play significant roles in fundamental cellular processes, such as cell growth and differentiation. It has been shown that the specificity and efficacy of phosphorylation by MAP kinases rely upon distinct MAPK-docking domains (D-domains) found in a wide range of MAPK substrates including the ETS-transcription factor Elk-1. Importantly, the MAPK signaling cascade converges with the hypoxia-induced signaling pathway. The key regulator of hypoxia signaling is the heterodimeric transcription factor hypoxia inducible factor-1 (HIF-1). The Î±-subunit of HIF-1 (HIF-1Î±) is a substrate for the ERK2 MAP kinase. Unraveling the in...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5279760</comments>
            <pubDate>Mon, 03 Oct 2011 23:47:30 +0100</pubDate>
            <guid isPermaLink="false">5279760</guid>        </item>
        <item>
            <title>Streptozotocin-induced diabetes affects in rat liver citrate carrier gene expression by transcriptional and posttranscriptional mechanisms.</title>
            <link>http://www.medworm.com/index.php?rid=5279738&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21820077%26dopt%3DAbstract</link>
            <description>Authors: Damiano F, Mercuri E, Stanca E, Gnoni GV, Siculella L
    Abstract
    Citrate carrier (CiC), also known as tricarboxylate carrier, is an integral protein of the mitochondrial inner membrane. It is an essential component of the shuttle system by which mitochondrial acetyl-CoA, primer for both fatty acid and cholesterol synthesis, is transported into the cytosol, where lipogenesis occurs. Here, we report the effect of streptozotocin-induced diabetes on the activity and expression of CiC in rat liver mitochondria. A significant reduction of CiC activity and a parallel decline in the abundance of CiC mRNA were found in liver from diabetic rats. Diabetes did not influence CiC mRNA stability, whereas nuclear run-on assay revealed that the transcriptional rate of CiC mRNA decreased, whe...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5279738</comments>
            <pubDate>Mon, 03 Oct 2011 23:46:49 +0100</pubDate>
            <guid isPermaLink="false">5279738</guid>        </item>
        <item>
            <title>The candidate tumor suppressor SASH1 interacts with the actin cytoskeleton and stimulates cell-matrix adhesion.</title>
            <link>http://www.medworm.com/index.php?rid=5279734&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21820526%26dopt%3DAbstract</link>
            <description>Authors: Martini M, Gnann A, Scheikl D, Holzmann B, Janssen KP
    Abstract
    SASH1, a member of the SLY-family of signal adapter proteins, is a candidate tumor suppressor in breast and colon cancer. Reduced expression of SASH1 is correlated with aggressive tumor growth, metastasis formation, and inferior prognosis. However, the biological role of SASH1 remains largely unknown. To unravel the function of SASH1, we have analyzed the intracellular localization of endogenous SASH1, and have generated structural SASH1 mutants. SASH1 localized to the nucleus as well as to the cytoplasm in epithelial cells. In addition, SASH1 was enriched in lamellipodia and membrane ruffles, where it co-distributed with the actin cytoskeleton. Moreover, we demonstrate a novel interaction of SASH1 with the onc...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5279734</comments>
            <pubDate>Mon, 03 Oct 2011 23:46:38 +0100</pubDate>
            <guid isPermaLink="false">5279734</guid>        </item>
        <item>
            <title>Damage-specific DNA binding protein 1 (DDB1): A protein with a wide range of functions.</title>
            <link>http://www.medworm.com/index.php?rid=5279700&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21959250%26dopt%3DAbstract</link>
            <description>Authors: Iovine B, Iannella ML, Bevilacqua MA
    Abstract
    Damage-specific DNA binding protein 1 (DDB1) is a multifunctional protein that was first isolated as a subunit of a heterodimeric complex that recognises the UV-induced DNA lesions in the nucleotide excision repair pathway. DDB1 and DDB2 form a complex that promotes the global genome repair (GG-NER), whereas DDB1 and Cockayne syndrome group A protein (CSA) form a complex that contributes to the transcription-coupled repair (TC-NER) pathway. DDB1 is also a component of an ubiquitin-E3 ligase complex and functions as substrate or adapter protein between Cullin 4A (Cul4A) and CUL4-associated factors (DCAFs) to target substrates for ubiquitination. CUL4-DDB1 E3-ligase complex regulates the selective proteolysis of key proteins in D...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5279700</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5279700</guid>        </item>
        <item>
            <title>Nuclear positioning: Mechanisms and functions.</title>
            <link>http://www.medworm.com/index.php?rid=5279683&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21959251%26dopt%3DAbstract</link>
            <description>Authors: Dupin I, Etienne-Manneville S
    Abstract
    The nucleus is the largest organelle in the cell and its position is dynamically controlled in space and time, although the functional significance of this dynamic regulation is not always clear. Nuclear movements are mediated by the cytoskeleton which transmits pushing or pulling forces onto the nuclear envelope. Recent studies have shed light on the mechanisms regulating nuclear positioning inside the cell. While microtubules have been known for a long time to be key players in nuclear positioning, the actin and cytoplasmic intermediate filament cytoskeletons have been implicated in this function more recently and various molecular links between the nuclear envelope and cytoplasmic elements have been identified. In this review, we s...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5279683</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5279683</guid>        </item>
        <item>
            <title>Proteomics reveals a switch in CDK1-associated proteins upon M-phase exit during the Xenopus laevis oocyte to embryo transition.</title>
            <link>http://www.medworm.com/index.php?rid=5279668&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21959252%26dopt%3DAbstract</link>
            <description>Authors: Marteil G, GagnÃ© JP, Borsuk E, Richard-Parpaillon L, Poirier GG, Kubiak JZ
    Abstract
    Cyclin-dependent kinase 1 (CDK1) is a major M-phase kinase which requires the binding to a regulatory protein, Cyclin B, to be active. CDK1/Cyclin B complex is called M-phase promoting factor (MPF) for its key role in controlling both meiotic and mitotic M-phase of the cell cycle. CDK1 inactivation is necessary for oocyte activation and initiation of embryo development. This complex process requires both Cyclin B polyubiquitination and proteosomal degradation via the ubiquitin-conjugation pathway, followed by the dephosphorylation of the monomeric CDK1 on Thr161. Previous proteomic analyses revealed a number of CDK1-associated proteins in human HeLa cells. It is, however, unknown whether s...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5279668</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5279668</guid>        </item>
        <item>
            <title>Linoleic acid induces an EMT-like process in mammary epithelial cells MCF10A.</title>
            <link>http://www.medworm.com/index.php?rid=5279718&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21945809%26dopt%3DAbstract</link>
            <description>Authors: Espinosa-Neira R, Mejia-Rangel J, Cortes-Reynosa P, Salazar EP
    Abstract
    Epidemiological studies and animal models suggest an association between high levels of dietary fat intake and an increased risk of developing breast cancer. Epithelial-mesenchymal-transition (EMT) is a process, by which epithelial cells are transdifferentiated to a mesenchymal state, and it has been implicated in cancer progression, including invasion and metastasis. Linoleic acid (LA) induces proliferation and invasion in breast cancer cells. However, the role of LA on the EMT process in human mammary epithelial cells remains to be studied. In the present study, we demonstrate that LA induces a transient down-regulation of E-cadherin expression, accompanied with an increase of Snail1, Snail2, Twist1,...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5279718</comments>
            <pubDate>Fri, 16 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5279718</guid>        </item>
        <item>
            <title>Small peptides derived from somatotropin domain-containing proteins inhibit blood and lymphatic endothelial cell proliferation, migration, adhesion and tube formation.</title>
            <link>http://www.medworm.com/index.php?rid=5229873&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21920451%26dopt%3DAbstract</link>
            <description>Authors: Lee E, Rosca EV, Pandey NB, Popel AS
    Abstract
    Angiogenesis is thoroughly balanced and regulated in health; however, it is dysregulated in many diseases including cancer, age-related macular degeneration, cardiovascular diseases such as coronary and peripheral artery diseases and stroke, abnormal embryonic development, and abnormal wound healing. In addition to angiogenesis, lymphangiogenesis is pivotal for maintaining the immune system, homeostasis of body fluids and lymphoid organs; dysregulated lymphangiogenesis may cause inflammatory diseases and lymph node mediated tumor metastasis. Anti-angiogenic or anti-lymphangiogenic small peptides may play an important role as therapeutic agents normalizing angiogenesis or lymphangiogenesis in disease conditions. Several novel en...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5229873</comments>
            <pubDate>Tue, 06 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5229873</guid>        </item>
        <item>
            <title>PAK4 phosphorylates myosin regulatory light chain and contributes to FcÎ³ receptor-mediated phagocytosis.</title>
            <link>http://www.medworm.com/index.php?rid=5218880&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21907820%26dopt%3DAbstract</link>
            <description>In this study, we show that p21-activated kinase 4 contributes to FcÎ³ receptor-mediated uptake downstream of actin cup formation by regulating phosphorylation of myosin regulatory light chain. siRNA-mediated knockdown of p21-activated kinase 4 leads to reduced myosin regulatory light chain phosphorylation at Serine 19, with a corresponding reduction in phospho-myosin regulatory right chain localised to bound immunoglobulin G-opsonised red blood cells. p21-activated kinase 4 phosphorylates myosin light chain 9 at Serine 19 in vitro and RNA interference against myosin light chain 9 implicates this isoform, but not myosin light chain 12A or 12B, in FcÎ³ receptor-mediated uptake. Taken together, these data indicate that p21-activated kinase 4 regulates regulatory myosin light chain phosphoryl...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218880</comments>
            <pubDate>Sat, 03 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218880</guid>        </item>
        <item>
            <title>Shiga toxin 1 is more dependent on the P proteins of the ribosomal stalk for depurination activity than Shiga toxin 2.</title>
            <link>http://www.medworm.com/index.php?rid=5218879&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21907821%26dopt%3DAbstract</link>
            <description>Authors: Chiou JC, Li XP, Remacha M, Ballesta JP, Tumer NE
    Abstract
    Shiga toxins produced by Escherichia coli O157:H7 are responsible for food poisoning and hemolytic uremic syndrome (HUS). The A subunits of Shiga toxins (Stx1A and Stx2A) inhibit translation by depurinating a specific adenine in the large rRNA. To determine if Stx1A and Stx2A require the ribosomal stalk for depurination, their activity and cytotoxicity were examined in the yeast P protein deletion mutants. Stx1A and Stx2A were less toxic and depurinated ribosomes less in a strain lacking P1/P2 on the ribosome and in the cytosol (Î”P2) than in a strain lacking P1/P2 on the ribosome, but containing free P2 in the cytosol (Î”P1). To determine if cytoplasmic P proteins facilitated depurination, Stx1A and Stx2A were exp...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218879</comments>
            <pubDate>Sat, 03 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218879</guid>        </item>
        <item>
            <title>The role of lysosomes in iron metabolism and recycling.</title>
            <link>http://www.medworm.com/index.php?rid=5218878&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21907822%26dopt%3DAbstract</link>
            <description>Authors: Kurz T, Eaton JW, Brunk UT
    Abstract
    Iron is the most abundant transition metal in the earth's crust. It cycles easily between ferric (oxidized; Fe(III)) and ferrous (reduced; Fe(II)) and readily forms complexes with oxygen, making this metal a central player in respiration and related redox processes. However, 'loose' iron, not within heme or iron-sulfur cluster proteins, can be destructively redox-active, causing damage to almost all cellular components, killing both cells and organisms. This may explain why iron is so carefully handled by aerobic organisms. Iron uptake from the environment is carefully limited and carried out by specialized iron transport mechanisms. One reason that iron uptake is tightly controlled is that most organisms and cells cannot efficiently exc...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218878</comments>
            <pubDate>Sat, 03 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218878</guid>        </item>
        <item>
            <title>Reps2: A cellular signaling and molecular trafficking nexus.</title>
            <link>http://www.medworm.com/index.php?rid=5218877&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21907823%26dopt%3DAbstract</link>
            <description>Authors: Badway JA, Baleja JD
    Abstract
    Since its discovery in the late 1990s as a signaling molecule in the Ras/Ral pathway, Reps2 has emerged as an important player in receptor-mediated endocytosis. Reps2 contains Eps15 homology (EH) domains, proline-rich regions, and a coiled-coil domain that engage in several protein-protein interactions to coordinate the internalization of various receptors with molecular signaling. Reps2 has clinical importance as it suppresses the ability of its binding partner RalBP1 to transport chemotherapeutic drugs, such as doxorubicin, out of a cell. Reps2 is also dysregulated during the progression of prostate cancer and is a potential biomarker for breast and prostate cancer.
    PMID: 21907823 [PubMed - as supplied by publisher] (Source: The Internat...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218877</comments>
            <pubDate>Sat, 03 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218877</guid>        </item>
        <item>
            <title>A novel 65-mer peptide imitates the synergism of superoxide dismutase and glutathione peroxidase.</title>
            <link>http://www.medworm.com/index.php?rid=5218876&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21911079%26dopt%3DAbstract</link>
            <description>Authors: Yan F, Yan G, Lv S, Shen N, Mu Y, Chen T, Gong P, Xu Y, Lv L, Liu J, Shen J, Luo G
    Abstract
    Reactive oxygen species (ROS) are involved in cell growth, differentiation, and death. Excessive amounts of ROS (e.g., O(2)(-), H(2)O(2), and HO) play a role in aging as well as in many human diseases. Superoxide dismutase (SOD) and glutathione peroxidase (GPx) are critical antioxidant enzymes in living organisms. SOD catalyzes the dismutation of O(2)(-) to H(2)O(2), and GPx catalyzes the reduction of H(2)O(2) and other harmful peroxides by glutathione (GSH). They not only function in catalytic processes but also protect each other, resulting in more efficient removal of ROS, protection of cells against injury, and maintenance of the normal metabolism of ROS. To imitate the synergis...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218876</comments>
            <pubDate>Sat, 03 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218876</guid>        </item>
        <item>
            <title>Medaka osmotic stress transcription factor 1b (Ostf1b/TSC22D3-2) triggers hyperosmotic responses of different ion transporters in medaka gill and human embryonic kidney cells via the JNK signalling pathway.</title>
            <link>http://www.medworm.com/index.php?rid=5218881&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21907305%26dopt%3DAbstract</link>
            <description>This study reports for the first time on the osmo-sensing signal cascade that related to the medaka osmotic stress transcription factor 1 (Ostf1), a hypertonic induced immediate early gene, under hypertonic stress. Quantitative real-time PCR showed the rapid increase of Ostf1 in gill after transfer of medaka from fresh water to 50% seawater; particularly Ostf1b whose mRNA expression increased to 4 folds at 0.5h and reached to 10 folds at 6h after the transfer. The in vivo knockdown of Ostf1b profoundly inhibited SEK and JNK phosphorylation, but not p38 and ERK phosphorylation in the medaka gill tissue. To further investigate the possible role of Ostf1b in the JNK pathway, Ostf1b was ectopically expressed in HEK293 cells. Results indicated that Ostf1b is a downstream target of SEK and JNK a...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218881</comments>
            <pubDate>Thu, 01 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218881</guid>        </item>
        <item>
            <title>O-Acetylated peptidoglycan: Controlling the activity of bacterial autolysins and lytic enzymes of innate immune systems.</title>
            <link>http://www.medworm.com/index.php?rid=5218882&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21889603%26dopt%3DAbstract</link>
            <description>Authors: Moynihan PJ, Clarke AJ
    Abstract
    The O-acetylation of peptidoglycan is now known to occur in 50 different bacterial species, both Gram positive and Gram negative, including a number of important human pathogens. This modification to the essential cell wall component of bacteria provides both a level of control over endogenous autolysins and protection from the lysozymes of innate immune systems. In this review, we describe the details of the pathways for peptidoglycan O-acetylation that are now beginning to emerge and we explore the possibility that the associated enzymes may present new candidates for antibacterial targets.
    PMID: 21889603 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218882</comments>
            <pubDate>Wed, 24 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218882</guid>        </item>
        <item>
            <title>Targeting angiogenesis with compounds from the extracellular matrix.</title>
            <link>http://www.medworm.com/index.php?rid=5175515&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21864705%26dopt%3DAbstract</link>
            <description>Authors: Belotti D, Foglieni C, Resovi A, Giavazzi R, Taraboletti G
    Abstract
    The extracellular matrix (ECM) is the central element of a pericellular network of bioactive molecules. It orchestrates molecular interactions, availability and activity, acting as a key regulator of cell functions and complex biological processes, including physiological and pathological angiogenesis. The ECM serves as a source of both stimulatory and inhibitory angiogenesis regulatory factors. The observation that several endogenous inhibitors of angiogenesis derive from the ECM proves its importance in physiological angiogenesis, and point to the ECM as a precious source of therapeutic agents for angiogenesis-driven diseases, including cancer growth and metastatic dissemination. This review focuses on t...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175515</comments>
            <pubDate>Tue, 16 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175515</guid>        </item>
        <item>
            <title>BRCA1 is required for hMLH1 stabilization following doxorubicin-induced DNA damage.</title>
            <link>http://www.medworm.com/index.php?rid=5175514&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21864706%26dopt%3DAbstract</link>
            <description>In this study, we show that the activation of the MMR component hMLH1 in response to doxorubicin (DOX) treatment requires the presence of BRCA1 and that this phenomenon is mediated by an ATM/ATR dependent phosphorylation of the hMLH1 Ser-406 residue. BRCA1 is an oncosuppressor protein with a central role in the DNA damage response and it is a critical component of the ATM/ATR mediated checkpoint signaling. Starting from a previous finding in which we demonstrated that hMLH1 is able to bind to BRCA1, in this study we asked whether BRCA1 might be the bridge for ATM/ATR dependent phosphorylation of the hMLH1 molecular partner. We found that: (i) the negative modulation of BRCA1 expression is able to produce a remarkable reversal of hMLH1 stabilization, (ii) BRCA1 is required for post-translat...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175514</comments>
            <pubDate>Mon, 15 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175514</guid>        </item>
        <item>
            <title>Tumour necrosis factor-stimulated gene (TSG)-6 controls epithelial-mesenchymal transition of proximal tubular epithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=5175513&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21864707%26dopt%3DAbstract</link>
            <description>Authors: Bommaya G, Meran S, Krupa A, Phillips AO, Steadman R
    Abstract
    Progressive renal disease is characterized by accumulation of extracellular matrix in the renal cortex. Proximal tubular cells (PTC) may contribute to disease through a process of epithelial-mesenchymal-transition (EMT): phenotypic change, disruption of the tubular basement membrane and migration into the interstitium. Hyaluronan (HA) synthesis and its extracellular organization by hyaladherins affect cell fate in other systems: this study investigated the role of the hyaladherin, tumour necrosis factor-stimulated gene (TSG)-6, in PTC EMT triggered in vitro by transforming growth factor (TGF)Î²1. TGFÎ²1 triggered the loss of PTC epithelial phenotype with 60% decreased expression of E-cadherin and 2-3-fold induct...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175513</comments>
            <pubDate>Mon, 15 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175513</guid>        </item>
        <item>
            <title>Nuclear translocation of Sgt1 depends on its phosphorylation state.</title>
            <link>http://www.medworm.com/index.php?rid=5175512&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21864708%26dopt%3DAbstract</link>
            <description>Authors: Prus W, Zabka M, Bieganowski P, Filipek A
    Abstract
    Recently we have shown that the Sgt1 (suppressor of G2 allele of Skp1) protein translocates to the nucleus due to heat shock and that the Ca(2+)-bound form of S100A6 is required for Sgt1 translocation (Prus and Filipek, 2010). In this work we studied the influence of Sgt1 phosphorylation on nuclear translocation. By means of two-dimensional (2D) electrophoresis we showed that in the protein extract of heat-shocked human epidermoid carcinoma (HEp-2) cells a higher level of a basic, most probably non-phosphorylated, form of Sgt1 can be detected. Also, we found a more efficient translocation of Sgt1 induced by heat shock when casein kinase II inhibitor was added to the cells. To confirm the role of Sgt1 phosphorylation/dephos...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175512</comments>
            <pubDate>Mon, 15 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175512</guid>        </item>
        <item>
            <title>Mitochondrial respiratory control and early defects of oxidative phosphorylation in the failing human heart.</title>
            <link>http://www.medworm.com/index.php?rid=5175511&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21871578%26dopt%3DAbstract</link>
            <description>Authors: Lemieux H, Semsroth S, Antretter H, HÃ¶fer D, Gnaiger E
    Abstract
    Heart failure is a consequence of progressive deterioration of cardiac performance. Little is known about the role of impaired oxidative phosphorylation in the progression of the disease, since previous studies of mitochondrial injuries are restricted to end-stage chronic heart failure. The present study aimed at evaluating the involvement of mitochondrial dysfunction in the development of human heart failure. We measured the control of oxidative phosphorylation with high-resolution respirometry in permeabilized myocardial fibres from donor hearts (controls), and patients with no or mild heart failure but presenting with heart disease, or chronic heart failure due to dilated or ischemic cardiomyopathy. The ca...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175511</comments>
            <pubDate>Mon, 15 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175511</guid>        </item>
        <item>
            <title>Notch signaling and Notch signaling modifiers.</title>
            <link>http://www.medworm.com/index.php?rid=5157239&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21854867%26dopt%3DAbstract</link>
            <description>Authors: Wanga MM
    Abstract
    Originally discovered nearly a century ago, the Notch signaling pathway is critical for virtually all developmental programs and modulates an astounding variety of pathogenic processes. The DSL (Delta, Serrate, LAG-2 family) proteins have long been considered canonical activators of the core Notch pathway. More recently, a wide and expanding network of non-canonical extracellular factors has also been shown to modulate Notch signaling, conferring newly appreciated complexity to this evolutionarily conserved signal transduction system. Here, I review current concepts in Notch signaling, with a focus on work from the last decade elucidating novel extracellular proteins that up- or down-regulate signal potency.
    PMID: 21854867 [PubMed - as supplied by pub...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5157239</comments>
            <pubDate>Thu, 11 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5157239</guid>        </item>
        <item>
            <title>Fas/FasL-dependent and -independent activation of caspase-8 in doxorubicin-treated human breast cancer MCF-7 cells: ADAM10 down-regulation activates Fas/FasL signaling pathway.</title>
            <link>http://www.medworm.com/index.php?rid=5157238&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21854868%26dopt%3DAbstract</link>
            <description>Authors: Liu WH, Chang LS
    Abstract
    The contribution of Fas-mediated death pathway to doxorubicin-induced death of MCF-7 cells is not unambiguously elucidated. Thus, this study was conducted to explore doxorubicin-induced Fas/FasL signaling pathway activation in MCF-7 cells and doxorubicin-resistant MCF-7 (MCF-7/Dox) cells. Doxorubicin-induced caspase-8 activation was found to be mediated through Akt/ERK inactivation and FasL-independent Fas pathway in MCF-7 cells, while caspase-8 activation in MCF-7/Dox cells depended exclusively on FasL-stimulated Fas pathway. Suppression of caspase-8 activation restored the viability of doxorubicin-treated MCF-7 cells and MCF-7/Dox cells. Contrary to FasL surface expression exclusively detected in MCF-7/Dox cells, intracellular FasL expression wa...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5157238</comments>
            <pubDate>Thu, 11 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5157238</guid>        </item>
        <item>
            <title>The emerging role of nuclear factor kappa B in renal cell carcinoma.</title>
            <link>http://www.medworm.com/index.php?rid=5157237&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21854869%26dopt%3DAbstract</link>
            <description>Authors: Morais C, Gobe G, Johnson DW, Healy H
    Abstract
    Renal cell carcinoma (RCC), the commonest type of kidney cancer, is a highly metastatic and the deadliest of all urologic cancers. Despite the development of many novel chemotherapeutics in recent years, metastatic RCC remains an incurable and lethal disease. The imperative for the identification of novel molecular targets and more effective therapeutics for metastatic RCC remain. One promising target is the transcription factor nuclear factor kappa B (NF-ÎºB). NF-ÎºB is unique in the sense that it regulates all important aspects of RCC biology that pose challenge to conventional therapy - resistance to apoptosis, angiogenesis and multi-drug resistance. Aberrations in the von Hippel Lindau gene (VHL) are the most important ris...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5157237</comments>
            <pubDate>Thu, 11 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5157237</guid>        </item>
        <item>
            <title>Different roles of p53 in the regulation of DNA damage caused by 1,2-heteroannelated anthraquinones and doxorubicin.</title>
            <link>http://www.medworm.com/index.php?rid=5157234&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21856437%26dopt%3DAbstract</link>
            <description>Authors: Chang YL, Lee HJ, Liu ST, Lin YS, Chen TC, Hsieh TY, Huang HS, Huang SM
    Abstract
    The anthracyclin antibiotic agent doxorubicin (DXR) has been widely used as a chemotherapeutic drug for more than 40 years, but its clinical use has been limited by its cardiotoxicity. The mechanism of action of DXR remains uncertain and controversial. A series of 1,2-heteroannelated anthraquinones and anthra[1,2-d]imidazole-6,11-dione compounds were synthesized and their cytotoxicity profiles were analyzed using the National Cancer Institute 60 (NCI 60) platform and human telomerase inhibition assays. In the current study, three of the 1,2-heteroannelated anthraquinones, NSC745795, NSC745885 and NSC745887, were found to differ from each other with respect to their effects on cell cycle regula...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5157234</comments>
            <pubDate>Thu, 11 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5157234</guid>        </item>
        <item>
            <title>Migraine: Role of the TRESK two-pore potassium channel.</title>
            <link>http://www.medworm.com/index.php?rid=5157236&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21855646%26dopt%3DAbstract</link>
            <description>Authors: LafreniÃ¨re RG, Rouleau GA
    Abstract
    Migraine is a severe episodic headache disorder affecting one in five people. Genetic studies have identified mutations in the CACNA1, ATP1A2 and SCN1A genes in the rare familial hemiplegic migraine. Recently, a mutation in the KCNK18 gene, encoding the TRESK two-pore domain potassium channel, was described in a large family with migraine with aura. This review will elaborate on the possible role of the TRESK channel in regulating neuronal excitability, its role in migraine pathogenesis, and on promising therapeutic opportunities targeting this channel.
    PMID: 21855646 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5157236</comments>
            <pubDate>Mon, 08 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5157236</guid>        </item>
        <item>
            <title>Far upstream element binding protein 1 activates translation of p27(Kip1) mRNA through its internal ribosomal entry site.</title>
            <link>http://www.medworm.com/index.php?rid=5157235&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21855647%26dopt%3DAbstract</link>
            <description>In this study, Far Upstream Element (FUSE) Binding Protein 1 (FBP1) was shown to directly bind to the human p27 5'-UTR and to promote IRES activity. An eight-nucleotide element downstream of a U-rich region within the 5'-UTR was important for FBP1 binding and p27 IRES activity. Overexpression of FBP1 enhanced endogenous p27 levels and stimulated translation initiation. In contrast, repression of FBP1 by siRNA transfection downregulated endogenous p27 protein levels. Using rabbit reticulocyte lysates, FBP1 stimulated p27 mRNA translation in vitro. The central domain of FBP1, containing four K homology motifs, was required for p27 5'-UTR RNA binding and the N terminal domain was important for translational activation. These findings indicate that FBP1 is a novel activator of p27 translation ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5157235</comments>
            <pubDate>Mon, 08 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5157235</guid>        </item>
        <item>
            <title>Nonsense mutations of the bHLH transcription factor TWIST2 found in Setleis Syndrome patients cause dysregulation of periostin.</title>
            <link>http://www.medworm.com/index.php?rid=5099478&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21801849%26dopt%3DAbstract</link>
            <description>Authors: Franco HL, Casasnovas JJ, Leon RG, Friesel R, Ge Y, Desnick RJ, Cadilla CL
    Setleis Syndrome (OMIM ID: 227260) is a rare autosomal recessive disease characterized by abnormal facial development. Recently, we have reported that two nonsense mutations (c.486C&amp;gt;T [Q119X] and c.324C&amp;gt;T [Q65X]) of the basic helix-loop-helix (bHLH) transcription factor TWIST2 cause Setleis Syndrome. Here we show that periostin, a cell adhesion protein involved in connective tissue development and maintenance, is down-regulated in Setleis Syndrome patient fibroblast cells and that periostin positively responds to manipulations in TWIST2 levels, suggesting that TWIST2 is a transactivator of periostin. Functional analysis of the TWIST2 mutant form (Q119X) revealed that it maintains the ability to lo...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5099478</comments>
            <pubDate>Mon, 25 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5099478</guid>        </item>
        <item>
            <title>Extracellular signal-regulated kinase1/2 activated by fluid shear stress promotes osteogenic differentiation of human bone marrow-derived mesenchymal stem cells through novel signaling pathways.</title>
            <link>http://www.medworm.com/index.php?rid=5099469&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21810479%26dopt%3DAbstract</link>
            <description>Authors: Liu L, Shao L, Li B, Zong C, Li J, Zheng Q, Tong X, Gao C, Wang J
    It is a classical signaling pathway that the activation of extracellular signal-regulated kinase1/2 (ERK1/2) results in the phosphorylation of runt-related transcription factor 2 (Runx2) and thereby initiates the transcription of osteogenic genes. Recently, it is found that the activation of ERK1/2 resulted from fluid shear stress (FSS) also increased the expression of Runx2 and Î²1 integrins, and finally enhanced osteogenic differentiation. However, it has been remained largely unknown how ERK1/2 regulates the expression of Runx2 and Î²1 integrins. We use the perfusion culture system to produce FSS exerting on human bone marrow-derived mesenchymal stem cells (hMSCs) and thus activate ERK1/2. Our study demonstra...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5099469</comments>
            <pubDate>Mon, 25 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5099469</guid>        </item>
        <item>
            <title>AWP1 binds to tumor necrosis factor receptor-associated factor 2 (TRAF2) and is involved in TRAF2-mediated nuclear factor-kappaB signaling.</title>
            <link>http://www.medworm.com/index.php?rid=5099468&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21810480%26dopt%3DAbstract</link>
            <description>In this study, we identified the zinc-finger protein AWP1 as a tumor necrosis factor receptor-associated factor 2-interacting protein through yeast two-hybrid screening. We found that AWP1 directly interacted with the C-terminal tumor necrosis factor receptor-associated factor (TRAF) domain of tumor necrosis factor receptor-associated factor 2. Knockdown of AWP1 using small hairpin RNA significantly decreased nuclear factor kappaB activity but increased tumor necrosis factor alpha (TNFÎ±)-induced apoptosis, presumably by decreasing the induction of nuclear factor kappaB-responsive anti-apoptotic molecules, including FICE-like inhibitory protein (FLIP), X-linked inhibitor of apoptosis protein (XIAP), Bcl-2, and Bcl-xL. In contrast, overexpression of wild-type AWP1 inhibited nuclear factor k...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5099468</comments>
            <pubDate>Mon, 25 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5099468</guid>        </item>
        <item>
            <title>Basic fibroblast growth factor regulates glucose metabolism through glucose transporter 1 induced by hypoxia-inducible factor-1Î± in adipocytes.</title>
            <link>http://www.medworm.com/index.php?rid=5099467&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21810481%26dopt%3DAbstract</link>
            <description>Authors: Kihira Y, Yamano N, Izawa-Ishizawa Y, Ishizawa K, Ikeda Y, Tsuchiya K, Tamaki T, Tomita S
    Hypoxia-inducible factor-1Î± (HIF-1Î±), which is a transcription factor that enhances glycolysis in cells in response to hypoxia, is induced in hypertrophied adipocytes in obesity. Recent studies have shown that growth factors are able to induce HIF-1Î± by mechanisms independent of hypoxia. Since basic fibroblast growth factor (bFGF), an angiogenic factor, is concentrated in expanding adipose tissue, the possible effects of bFGF on regulation of HIF-1Î± in adipocytes were investigated. Treatment of differentiated 3T3-L1 adipocytes with bFGF induced HIF-1Î±. Concomitantly, glucose transporter 1 (GLUT1), which is a target gene of HIF-1Î±, was induced at both mRNA and protein levels and was ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5099467</comments>
            <pubDate>Mon, 25 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5099467</guid>        </item>
        <item>
            <title>Sirt1 deacetylates c-Myc and promotes c-Myc/Max association.</title>
            <link>http://www.medworm.com/index.php?rid=5099477&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21807113%26dopt%3DAbstract</link>
            <description>In this study, we show that Sirt1 interacts physically with the C-terminus of c-Myc and deacetylates c-Myc both in vitro and in vivo. Moreover, the deacetylation of c-Myc by Sirt1 promotes its association with Max, a partner essential for its activation, thereby facilitating c-Myc transactivation activity on hTERT promoter. Finally, inhibition of endogenous Sirt1 in K562 cells by either RNAi or its inhibitor NAM causes the overall decrease of c-Myc target genes expression, including hTERT, cyclinD2 and LDHA, which further suppress cell proliferation and arrest cell cycle at G1/S phase. Thus, our results demonstrate the positive effect of Sirt1 on c-Myc activity by efficiently enhancing c-Myc/Max association in human leukemia cell line K562, suggesting a potential role of Sirt1 in tumorigen...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5099477</comments>
            <pubDate>Thu, 21 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5099477</guid>        </item>
        <item>
            <title>Biochemical and molecular analysis of the interaction between ERK2 MAP kinase and hypoxia inducible factor-1Î±</title>
            <link>http://www.medworm.com/index.php?rid=5099476&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21807114%26dopt%3DAbstract</link>
            <description>Authors: Karapetsas A, Giannakakis A, Pavlaki M, Panayiotidis M, Sandaltzopoulos R, Galanis A
    The mitogen activated protein kinase (MAPK) signaling pathways play significant roles in fundamental cellular processes, such as cell growth and differentiation. It has been shown that the specificity and efficacy of phosphorylation by MAP kinases rely upon distinct MAPK-docking domains (D-domains) found in a wide range of MAPK substrates including the ETS-transcription factor Elk-1. Importantly, the MAPK signaling cascade converges with the hypoxia-induced signaling pathway. The key regulator of hypoxia signaling is the heterodimeric transcription factor hypoxia inducible factor-1 (HIF-1). The Î±-subunit of HIF-1 (HIF-1Î±) is a substrate for the ERK2 MAP kinase. Unraveling the interplay of th...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5099476</comments>
            <pubDate>Thu, 21 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5099476</guid>        </item>
        <item>
            <title>Drosha regulates hMSCs cell cycle progression through a miRNA independent mechanism.</title>
            <link>http://www.medworm.com/index.php?rid=5099480&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21794839%26dopt%3DAbstract</link>
            <description>Authors: Oskowitz AZ, Penfornis P, Tucker A, Prockop DJ, Pochampally R
    Recently we demonstrated that the miRNA regulate human mesenchymal stem cells (hMSCs) differentiation. To determine the role of the miRNA pathway in hMSCs proliferation, Drosha and Dicer knockdown hMSCs were generated using a lentiviral based tetracycline inducible shRNA. hMSCs with reduced Drosha expression had a significantly reduced proliferation rate, while hMSCs with reduced Dicer expression displayed a proliferation rate similar to untransduced cells. Cell cycle analysis identified that unlike Dicer knockdown, Drosha knockdown hMSCs contained an increased number of G1 phase cells, with a reduced level of cells in S phase, compared to controls. ELISAs of hMSCs revealed decreased levels of pRB and stable levels ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5099480</comments>
            <pubDate>Tue, 19 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5099480</guid>        </item>
        <item>
            <title>Plant lectins: Targeting programmed cell death pathways as antitumor agents.</title>
            <link>http://www.medworm.com/index.php?rid=5099479&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21798364%26dopt%3DAbstract</link>
            <description>Authors: Fu LL, Zhou CC, Yao S, Yu JY, Liu B, Bao JK
    Lectins, a group of highly diverse, carbohydrate-binding proteins of non-immune origin that are ubiquitously distributed in plants, animals and fungi, are well-characterized to have numerous links a wide range of pathological processes, most notably cancer. In this review, we present a brief outline of the representative plant lectins including Ricin-B family, proteins with legume lectin domains and GNA family that can induce cancer cell death via targeting programmed cell death pathways. Amongst these above-mentioned lectins, we demonstrate that mistletoe lectins (MLs), Ricin, Concanavalin A (ConA) and Polygonatum cyrtonema lectin (PCL) can lead to cancer cell programmed death via targeting apoptotic pathways. In addition, we show t...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5099479</comments>
            <pubDate>Tue, 19 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5099479</guid>        </item>
        <item>
            <title>Safrole oxide induces human umbilical vein endothelial cell transdifferentiation to 5-hydroxytryptaminergic neuron-like cells through tropomyosin receptor kinase A/cyclooxygenase 2/nuclear factor-kappa B/interleukin 8 signaling.</title>
            <link>http://www.medworm.com/index.php?rid=5052104&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21777689%26dopt%3DAbstract</link>
            <description>In this study, we first validated that these cells induced by safrole oxide were functional 5-hydroxytryptaminergic neuron-like cells. Then, we performed microarray analysis of safrole oxide-treated and -untreated human umbilical vein endothelial cells. Safrole oxide elevated the levels of cyclooxygenase 2 (COX-2), interleukin-8 (IL-8) and reactive oxygen species (ROS), which was accompanied by nuclear factor-kappa B (NF-ÎºB) nuclear translocation during the transdifferentiation. Blockade of tropomyosin receptor kinase A (TrkA) by an inhibitor or short hairpin RNA inhibited the levels of COX-2/IL-8 and the nuclear translocation of NF-ÎºB but did not suppress the increased ROS level. As a result, cells underwent apoptosis. Therefore, via TrkA, safrole oxide may induce endothelial cell trans...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5052104</comments>
            <pubDate>Tue, 12 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5052104</guid>        </item>
        <item>
            <title>Identification and characterization of the immunogenic cytotoxic TvCP39 proteinase gene of Trichomonas vaginalis.</title>
            <link>http://www.medworm.com/index.php?rid=5052103&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21777690%26dopt%3DAbstract</link>
            <description>In conclusion, our data support TvCP39 as one of the surface proteinases that is glycosylated and is involved in trichomonal cytotoxicity. Thus, TvCP39 is the first glycosylated cysteine proteinase detected in T. vaginalis.
    PMID: 21777690 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5052103</comments>
            <pubDate>Mon, 11 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5052103</guid>        </item>
        <item>
            <title>Multivariate geometrical analysis of catalytic residues in the penicillin-binding proteins.</title>
            <link>http://www.medworm.com/index.php?rid=5052105&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21740978%26dopt%3DAbstract</link>
            <description>Authors: Bobba S, Gutheil WG
    Penicillin-binding proteins (PBPs) are bacterial enzymes involved in the final stages of cell wall biosynthesis, and are targets of the Î²-lactam antibiotics. They can be subdivided into essential high-molecular-mass (HMM) and non-essential low-molecular-mass (LMM) PBPs, and further divided into subclasses based on sequence homologies. PBPs can catalyze transpeptidase or hydrolase (carboxypeptidase and endopeptidase) reactions. The PBPs are of interest for their role in bacterial cell wall biosynthesis, and as mechanistically interesting enzymes which can catalyze alternative reaction pathways using the same catalytic machinery. A global catalytic residue comparison seemed likely to provide insight into structure-function correlations within the PBPs. More ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5052105</comments>
            <pubDate>Tue, 28 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5052105</guid>        </item>
        <item>
            <title>Type 2 deiodinase at the crossroads of thyroid hormone action.</title>
            <link>http://www.medworm.com/index.php?rid=4960476&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21679772%26dopt%3DAbstract</link>
            <description>This article reviews the cellular and molecular aspects of D2 regulation and the current models of D2-mediated thyroid hormone signaling.
    PMID: 21679772 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4960476</comments>
            <pubDate>Sun, 12 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4960476</guid>        </item>
        <item>
            <title>On diphtheria toxin fragment A release into the cytosol-Cytochalasin D effect and involvement of actin filaments and eukaryotic elongation factor 2.</title>
            <link>http://www.medworm.com/index.php?rid=4960477&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21664484%26dopt%3DAbstract</link>
            <description>Authors: BektaÅŸ M, HacÄ±osmanoÄŸlu E, Ozerman B, Varol B, Nurten R, Bermek E
    Diphtheria toxin has been well characterized in terms of its receptor binding and receptor mediated endocytosis. However, the precise mechanism of the cytosolic release of diphtheria toxin fragment A from early endosomes is still unclear. Various reports differ regarding the requirement for cytosolic factors in this process. Here, we present data indicating that the distribution of actin filaments due to cytochalasin D action enhances the retention of diphtheria toxin in early endosomes. Treating cells with cytochalasin D reduces the cytosolic fragment A activity and leads to changes in the intracellular distribution and size of early endosomes with toxin cargo. F-actin and eukaryotic elongation factor 2 can ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4960477</comments>
            <pubDate>Sat, 11 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4960477</guid>        </item>
        <item>
            <title>Reactive oxygen species participate in the p38-mediated apoptosis induced by potassium deprivation and staurosporine in cerebellar granule neurons.</title>
            <link>http://www.medworm.com/index.php?rid=4960475&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21683152%26dopt%3DAbstract</link>
            <description>Authors: Ramiro-CortÃ©s Y, Guemez-Gamboa A, MorÃ¡n J
    Apoptosis induced by low potassium (K5) or staurosporine in cerebellar granule neurons triggers an increase in reactive oxygen species (ROS) levels. ROS inhibition by antioxidants or inhibitors of the NADPH oxidase (NOX) activity reduces the apoptosis induced by both stimuli. It has been reported that JNK mediates the apoptosis induced by K5 but not by staurosporine. No information is available about the role of other signaling pathways such as p38 in staurosporine-induced apoptosis, and whether p38 activation could be related to ROS levels induced by both K5 and staurosporine. Here, we explored this possibility and found that K5 activates p38 and ATF2 and that the inhibition of p38 activity prevents the apoptosis induced by this tre...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4960475</comments>
            <pubDate>Sat, 11 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4960475</guid>        </item>
        <item>
            <title>Ubiquitin-dependent mitochondrial protein degradation.</title>
            <link>http://www.medworm.com/index.php?rid=4960474&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21683801%26dopt%3DAbstract</link>
            <description>Authors: Heo JM, Rutter J
    Progressive mitochondrial failure is tightly associated with the onset of many age-related human pathologies. This tight connection results from the double-edged sword of mitochondrial respiration, which is responsible for generating both ATP and ROS, as well as from risks that are inherent to mitochondrial biogenesis. To prevent and treat these diseases, a precise understanding of the mechanisms that maintain functional mitochondria is necessary. Mitochondrial protein quality control is one of the mechanisms that protect mitochondrial integrity, and increasing evidence implicates the cytosolic ubiquitin/proteasome system (UPS) as part of this surveillance network. In this review, we will discuss our current understanding of UPS-dependent mitochondrial protein...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4960474</comments>
            <pubDate>Sat, 11 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4960474</guid>        </item>
        <item>
            <title>TLR-mediated induction of pro-allergic cytokine IL-33 in ocular mucosal epithelium.</title>
            <link>http://www.medworm.com/index.php?rid=4960473&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21684348%26dopt%3DAbstract</link>
            <description>Authors: Zhang L, Lu R, Zhao G, Pflugfelder SC, Li DQ
    Interleukin (IL) 33 has been recently identified as a ligand to the ST2 receptor that mediates Th2-dominant allergic inflammation. The purpose of this study was to explore the role of toll-like receptor (TLR)-mediated innate immunity in IL-33 induction by mucosal epithelium. Human corneal tissues and cultured primary human corneal epithelial cells (HCECs) were treated with a variety of viral or bacterial components without or with different inhibitors to evaluate the IL-33 regulation and signaling pathways. The level of mRNA expression was determined by reverse transcription and real time PCR, and protein was measured by ELISA, immunostaining and Western blotting. IL-33 mRNA and protein were largely induced by various microbial comp...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4960473</comments>
            <pubDate>Sat, 11 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4960473</guid>        </item>
        <item>
            <title>Progesterone synthesis by human placental mitochondria is sensitive to PKA inhibition by H89.</title>
            <link>http://www.medworm.com/index.php?rid=4960472&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21689781%26dopt%3DAbstract</link>
            <description>Authors: Gomez-Concha C, Flores-Herrera O, Olvera-Sanchez S, Espinosa-Garcia MT, Martinez F
    The transfer of cholesterol to mitochondria, which might involve the phosphorylation of proteins, is the rate-limiting step in human placental steroidogenesis. Protein kinase A (PKA) activity and its role in progesterone synthesis by human placental mitochondria were assessed in this study. The results showed that PKA and phosphotyrosine phosphatase D1 are associated with syncytiotrophoblast mitochondrial membrane by an anchoring kinase cAMP protein-121. The (32)P-labeled of four major proteins was analyzed. The specific inhibitor of PKA, H89, decreased progesterone synthesis in mitochondria while in mitochondrial steroidogenic contact sites protein-phosphorylation was diminished, suggesting tha...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4960472</comments>
            <pubDate>Sat, 11 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4960472</guid>        </item>
        <item>
            <title>Drosophila arf72A acts as an essential regulator of endoplasmic reticulum quality control and suppresses autosomal-dominant retinopathy.</title>
            <link>http://www.medworm.com/index.php?rid=4960471&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21693198%26dopt%3DAbstract</link>
            <description>Authors: Lee J, Lee J, Ju BG
    The eukaryotic endoplasmic reticulum operates multiple quality control mechanisms to ensure that only properly folded proteins are exported to their final destinations via the secretory pathway and those that are not are destroyed via the degradation pathway. However, molecular mechanisms underlying such regulated exportation to these distinct routes are unknown. In this article, we report the role of Drosophila arf72A - the fly homologue of the mammalian Arl1 - in the quality checks of proteins and in the autosomal-dominant retinopathy. ARF72A localizes to the Golgi membranes of Drosophila photoreceptor cells, consistent with mammalian Arl1 localization in cell culture systems. A loss of arf72A function changes the membrane character of the endoplasmic ret...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4960471</comments>
            <pubDate>Sat, 11 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4960471</guid>        </item>
        <item>
            <title>A calcium-insensitive attenuated nitrosative stress response contributes significantly in the radioresistance of Sf9 insect cells.</title>
            <link>http://www.medworm.com/index.php?rid=4960480&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21658466%26dopt%3DAbstract</link>
            <description>Authors: Suman S, Seth RK, Chandna S
    Lepidopteran insects/insect cells display 50-100 times higher radioresistance than humans, and are evolutionarily closest to mammals amongst all radioresistant organisms known. Compared to mammalian cells, Lepidopteran cells (TN-368, Sf9) display more efficient antioxidant system and DNA repair and suffer considerably less radiation-induced DNA/cytogenetic damage and apoptosis. Recent studies indicate that a considerably lower radiation-induced oxidative stress may significantly reduce macromolecular damage in Lepidopteran cells. Since nitrosative stress contributes in radiation-induced cellular damage, we investigated its nature in the Î³-irradiated Sf9 cells (derived from Spodoptera frugiperda; order Lepidoptera; family Noctuidae) and compared wit...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4960480</comments>
            <pubDate>Tue, 31 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4960480</guid>        </item>
        <item>
            <title>Acute myeloid leukemia: A central role for the ETS factor ERG.</title>
            <link>http://www.medworm.com/index.php?rid=4960479&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21664289%26dopt%3DAbstract</link>
            <description>Authors: Martens JH
    Acute myeloid leukemia is a cancer of the myeloid lineage, characterized by the rapid proliferation of immature progenitor cells which accumulate in the bone marrow and interfere with the production of normal blood cells. Aberrant regulation of E-twenty-six (ETS) specific transcription factors such as PU.1 (SPI1) is thought to play a major role in this type of leukemia. The importance of these factors in normal blood development is highlighted by the fact that numerous studies showed a direct link between hematopoietic defects and aberrant regulation of ETS factor expression or expression of mutant forms. Apart from PU.1, another ETS factor, ERG, has emerged as a key player in normal hematopoiesis. Here, the role of this protein in normal and aberrant blood developm...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4960479</comments>
            <pubDate>Tue, 31 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4960479</guid>        </item>
        <item>
            <title>Adenomatous polyposis coli protein regulates the cellular response to DNA replication stress.</title>
            <link>http://www.medworm.com/index.php?rid=4960478&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21664290%26dopt%3DAbstract</link>
            <description>Authors: Brocardo MG, Borowiec JA, Henderson BR
    The adenomatous polyposis coli (APC) tumor suppressor traffics between nucleus and cytoplasm to perform distinct functions. Here we identify a specific role for APC in the DNA replication stress response. The silencing of APC caused an accumulation of asynchronous cells in early S phase and delayed S phase progression in cells released from hydroxyurea-mediated replication arrest. Immunoprecipitation assays revealed a selective binding of APC to replication protein A 32kDa subunit (RPA32), and the APC-RPA32 complex increased at chromatin after hydroxyurea treatment. Interestingly, APC knock-down prevented accumulation at chromatin of the stress-induced S33- and S29-phosphorylated forms of RPA32, and reduced the expression of ATR-phosphory...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4960478</comments>
            <pubDate>Sun, 29 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4960478</guid>        </item>
        <item>
            <title>Structure-activity relationship of ibogaine analogs interacting with nicotinic acetylcholine receptors in different conformational states.</title>
            <link>http://www.medworm.com/index.php?rid=4912088&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21642011%26dopt%3DAbstract</link>
            <description>Authors: Arias HR, Feuerbach D, Targowska-Duda KM, Jozwiak K
    The interaction of ibogaine analogs with nicotinic acetylcholine receptors (AChRs) in different conformational states was studied by functional and structural approaches. The results established that ibogaine analogs: (a) inhibit (Â±)-epibatidine-induced Ca(2+) influx in human embryonic muscle AChRs with the following potency sequence (IC(50) in Î¼M): (Â±)-18-methylaminocoronaridine (5.9Â±0.3)âˆ¼(Â±)-18-methoxycoronaridine (18-MC) (6.8Â±0.8)&amp;gt;(-)-ibogaine (17Â±3)âˆ¼(+)-catharanthine (20Â±1)&amp;gt;(Â±)-albifloranine (46Â±13), (b) bind to the [(3)H]TCP binding site with higher affinity when the Torpedo AChR is in the desensitized state compared to that in the resting state. Similar results were obtained using [(3)H]18-MC. These ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4912088</comments>
            <pubDate>Thu, 26 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4912088</guid>        </item>
        <item>
            <title>Core signaling pathways of survival/death in autophagy-related cancer networks.</title>
            <link>http://www.medworm.com/index.php?rid=4912089&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21640844%26dopt%3DAbstract</link>
            <description>Authors: Wang SY, Yu QJ, Zhang RD, Liu B
    Autophagy (macroautophagy), an evolutionarily conserved lysosomal degradation process, is implicated in a wide variety of pathological processes including cancer. Autophagy plays the Janus role in regulating several survival or death signaling pathways that may decide the fate of cancer cell. Accumulating evidence has revealed the core molecular machinery of autophagy in tumor initiation and progression; however, the intricate relationships between autophagy and cancer are still in its infancy. In this review, we summarize several key survival/death pathways such as mTOR subnetwork, Beclin 1 interactome, and p53 signaling that may play the crucial roles for the regulation of the autophagy-related cancer networks. Therefore, a better understandin...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4912089</comments>
            <pubDate>Wed, 25 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4912089</guid>        </item>
        <item>
            <title>Decreased expression of protease-activated receptor 4 in human gastric cancer.</title>
            <link>http://www.medworm.com/index.php?rid=4912090&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21635966%26dopt%3DAbstract</link>
            <description>In this study, differential expression of PAR4 was measured by real-time PCR (n=28) and tissue microarrays (n=74). We showed that PAR4 was located from basal to middle portions of normal gastric mucosa. PAR4 expression was remarkably decreased in gastric cancer tissues as compared with matched noncancerous tissues, especially in positive lymph node or low differentiation cancers. Furthermore, methylation of the PAR4 promoter in cell lines was assessed by treatment with 5-aza-2'-deoxycytidine and genomic bisulfite sequencing. AGS and N87 human gastric cancer cell lines did not express PAR4, as compared to HT-29 human colon cancer cell line with significant PAR4 expression. Treatment with 5-aza-2'-deoxycytidine restored PAR4 expression in AGS and N87 cells, which exhibited significantly more...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4912090</comments>
            <pubDate>Tue, 24 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4912090</guid>        </item>
        <item>
            <title>Macrolides: New therapeutic perspectives in lung diseases.</title>
            <link>http://www.medworm.com/index.php?rid=4912091&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21635965%26dopt%3DAbstract</link>
            <description>Authors: Guillot L, Tabary O, Nathan N, Corvol H, Clement A
    There is strong clinical evidence for the effectiveness of macrolides in the treatment of a number of chronic airway diseases through their immunomodulatory effects. Recently, new information has been released supporting the view that macrolides may also be beneficial in pathologic situations associated with altered repair of the alveolar structure, such as those observed in interstitial lung diseases and fibrosis. It is proposed that macrolides may contribute to lung regeneration through their actions on several components of the remodeling process. The present review provides new insights on the effects of macrolides on the regenerative response of alveolar epithelium to injury. It also discusses novel findings which suggest...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4912091</comments>
            <pubDate>Sun, 22 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4912091</guid>        </item>
        <item>
            <title>Mechanotransduction and the regulation of mTORC1 signaling in skeletal muscle.</title>
            <link>http://www.medworm.com/index.php?rid=4912092&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21621634%26dopt%3DAbstract</link>
            <description>Authors: Hornberger TA
    Mechanical stimuli play a major role in the regulation of skeletal muscle mass, and the maintenance of muscle mass contributes significantly to disease prevention and issues associated with the quality of life. Although the link between mechanical signals and the regulation of muscle mass has been recognized for decades, the mechanisms involved in converting mechanical information into the molecular events that control this process remain poorly defined. Nevertheless, our knowledge of these mechanisms is advancing and recent studies have revealed that signaling through a protein kinase called the mammalian target of rapamycin (mTOR) plays a central role in this event. In this review we will, (1) discuss the evidence which implicates mTOR in the mechanical regulat...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4912092</comments>
            <pubDate>Wed, 18 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4912092</guid>        </item>
        <item>
            <title>Mitochondria and endoplasmic reticulum: Mitochondria-endoplasmic reticulum interplay in type 2 diabetes pathophysiology.</title>
            <link>http://www.medworm.com/index.php?rid=4863119&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21605696%26dopt%3DAbstract</link>
            <description>Authors: Rieusset J
    Mitochondria and endoplasmic reticulum (ER) are two important metabolic organelles for the maintenance of cellular homeostasis and their functional defects are suspected to participate to the aetiology of type 2 diabetes (T2D). Particularly, excessive lipid intake and/or ectopic lipid accumulation in tissues (referred as lipotoxicity) are involved in alterations of both organelles and are closely linked to peripheral insulin resistance and defective insulin secretion. Since, mitochondria and ER are physically and functionally interconnected, their respective alterations during T2D could be interrelated. However, the mechanisms that coordinate the interplay between mitochondrial dysfunction and ER stress, and its relevance in the control of glucose homeostasis are un...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4863119</comments>
            <pubDate>Fri, 13 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4863119</guid>        </item>
        <item>
            <title>Mitochondria: A sulfhydryl oxidase and fission GTPase connect mitochondrial dynamics with pluripotency in embryonic stem cells.</title>
            <link>http://www.medworm.com/index.php?rid=4863120&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21605695%26dopt%3DAbstract</link>
            <description>Authors: Wilkerson DC, Sankar U
    Mitochondria have long been recognized as cellular energy power houses that also regulate cellular redox signaling to arbitrate cell survival. Recent studies of mitochondria in stem cells (SCs) demonstrate that they have critical roles beyond this traditional view. Embryonic (E) SCs, termed pluripotent for their ability to differentiate into all cell types within an organism, maintain a limited number of morphologically undifferentiated (electron translucent and poorly formed cristae) mitochondria. As these cells differentiate, their mitochondria undergo a tightly choreographed gain of number, mass and morphological complexity. Therefore, mechanisms that regulate mitochondrial growth, localization, division and partition must play active roles in the mai...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4863120</comments>
            <pubDate>Thu, 12 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4863120</guid>        </item>
        <item>
            <title>An acidic pH environment increases cell death and pro-inflammatory cytokine release in osteoblasts: The involvement of BAX Inhibitor-1.</title>
            <link>http://www.medworm.com/index.php?rid=4863124&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21601004%26dopt%3DAbstract</link>
            <description>In this study, using the MG63 osteoblast cell line and osteoblasts differentiated from stem cells, the role of BI-1 was studied. First, expression of BI-1 was confirmed in osteoblasts, as well as osteoclasts, in mouse tibiae bone immunohistochemistry. For evaluation of a recently published property of BI-1, an acidic pH-dependent Ca(2+) channel-like effect in osteoblasts, acidic pH-associated cell death, and pro-inflammatory cytokine release were examined. In MG63 osteoblasts, acidic pH induced a pH-dependent increase in cell death and ER stress, as determined by elevated expression of GRP78, CHOP, phospho-eIF2Î±, IRE-1Î±, spliced XBP-1, and phospho-JNK. In osteoblasts, mitochondrial Ca(2+) also showed a strong pH-dependent increase. BI-1 knock-down using siRNA protected cells against acid...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4863124</comments>
            <pubDate>Wed, 11 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4863124</guid>        </item>
        <item>
            <title>The impact of pericytes on the blood-brain barrier integrity depends critically on the pericyte differentiation stage.</title>
            <link>http://www.medworm.com/index.php?rid=4863123&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21601005%26dopt%3DAbstract</link>
            <description>In this study we analyzed the differentiation stage dependent influence of primary porcine brain capillary pericytes on the barrier integrity of primary porcine brain capillary endothelial cells. At first, we were able to induce two distinct differentiation stages of the primary pericytes in vitro. TGFÎ² treated pericytes expressed more Î±-SMA and actin while desmin, vimentin and nestin expression was decreased when compared to bFGF induced cells. Further analysis of Î±-SMA revealed that most of the pericytes differentiated with TGFÎ² expressed functional Î±-SMA while only few cells expressed functional Î±-SMA in the presence of bFGF. In addition the permeability factors VEGF, MMP-2 and MMP-9 were higher secreted by the Î±-SMA positive phenotype indicating a proangiogenic role of this TGFÎ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4863123</comments>
            <pubDate>Wed, 11 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4863123</guid>        </item>
        <item>
            <title>Caveolin-1 overexpression enhances androgen-dependent growth and proliferation in the mouse prostate.</title>
            <link>http://www.medworm.com/index.php?rid=4863121&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21601007%26dopt%3DAbstract</link>
            <description>Authors: Bryant KG, Camacho J, Jasmin JF, Wang C, Addya S, Casimiro MC, Fortina P, Balasubramaniam S, Knudsen KE, Schwarting R, Lisanti MP, Mercier I
    Prostate cancer (PCa) continues to be one of the leading causes of cancer- related deaths among American men. The prostate relies upon the androgen receptor (AR) to mediate the effects of androgens on normal growth, a reliance that is maintained during malignant prostate growth. Caveolin-1 (Cav-1), the main structural component of caveolae, has been shown to promote malignant growth and invasion of prostate tumors. In vitro work has shown that Cav-1 can act as an AR coactivator by enhancing its transciptional activity. However, it is unknown how Cav-1 affects androgen-dependent growth and signaling in vivo. To explore this role, a novel m...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4863121</comments>
            <pubDate>Wed, 11 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4863121</guid>        </item>
        <item>
            <title>Amyloid-Î²: The seeds of darkness.</title>
            <link>http://www.medworm.com/index.php?rid=4863125&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21601003%26dopt%3DAbstract</link>
            <description>Authors: Fodero-Tavoletti MT, Villemagne VL, Rowe CC, Masters CL, Barnham KJ, Cappai R
    Whilst the amyloid-Î² (AÎ²) hypothesis/centric theory continues to evolve, genetic, biochemical and pathological evidence still suggests that AÎ² is central to the etiology of Alzheimer's disease (AD). In particular, AÎ²-oligomers/soluble AÎ², may be an earlier determinant of Alzheimer's disease and better correlative of cognitive impairment. Whilst there are a number of AÎ²-oligomeric species in existence (making therapeutic and diagnostic biomarker choice cumbersome), their existence is in equilibrium with AÎ²-fibrils, the main constituent of cored plaques. Although Alzheimer's disease remains incurable, improvements to AÎ² immunotherapies and strategies to target AÎ² continue to evolve, with the r...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4863125</comments>
            <pubDate>Tue, 10 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4863125</guid>        </item>
        <item>
            <title>Small interfering RNA targeting integrin-linked kinase inhibited the growth and induced apoptosis in human bladder cancer cells.</title>
            <link>http://www.medworm.com/index.php?rid=4863122&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21601006%26dopt%3DAbstract</link>
            <description>In conclusion, these results suggest that ILK might be involved in the development of bladder cancer, and could be served as a novel potential therapy target for human bladder cancer. Our study may be of biological and clinical importance.
    PMID: 21601006 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4863122</comments>
            <pubDate>Tue, 10 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4863122</guid>        </item>
        <item>
            <title>Diabetes: New conductors for the peroxisome proliferator-activated receptor Î³ (PPARÎ³) orchestra.</title>
            <link>http://www.medworm.com/index.php?rid=4863126&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21558015%26dopt%3DAbstract</link>
            <description>Authors: Whitehead JP
    The PPARÎ³ nuclear receptor orchestrates fatty acid storage and glucose metabolism by coordinating the expression of genes involved in lipid uptake, adipogenesis and inflammation. It is a target for the insulin-sensitising thiazolidinediones (TZDs) which have been used to treat diabetes since the late nineties. Adverse secondary effects of TZDs have underpinned continued investigations into the molecular details governing PPARÎ³ regulation and new therapeutic approaches which represent the focus of this article. Recent findings position Cdk5 as a lead conductor of PPARÎ³. Cdk5 regulates PPARÎ³ directly, via phosphorylation, and may also inhibit it indirectly, via phosphorylation and activation of phospholipase D2 (PLD2) which generates the endogenous inhibitor cyc...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4863126</comments>
            <pubDate>Wed, 04 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4863126</guid>        </item>
        <item>
            <title>Structural requirements for the inhibition of calcium mobilization and mast cell activation by the pyrazole derivative BTP2.</title>
            <link>http://www.medworm.com/index.php?rid=4863127&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21558014%26dopt%3DAbstract</link>
            <description>Authors: Law M, Morales JL, Mottram LF, Iyer A, Peterson BR, August A
    Mast cells play a critical role in the development of the allergic response. Upon activation by allergens and IgE via the high affinity receptor for IgE (FcÉ›RI), these cells release histamine and other functional mediators that initiate and propagate immediate hypersensitivity reactions. Mast cells also secrete cytokines that can regulate immune activity. These processes are controlled, in whole or part, by increases in intracellular Ca(2+) induced by the FcÉ›RI. We show here that N-(4-(3,5-bis(trifluoromethyl)-1H-pyrazol-1-yl)phenyl)-4-methyl-1,2,3-thiadiazole-5-carboxamide (BTP2), a pyrazole derivative, inhibits activation-induced Ca(2+) influx in the rat basophil cell line RBL-2H3 and in bone marrow-derived mast ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4863127</comments>
            <pubDate>Tue, 03 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4863127</guid>        </item>
        <item>
            <title>Editorial for the directed issue: &quot;Metabolic pathways in cancer&quot;</title>
            <link>http://www.medworm.com/index.php?rid=4805673&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21554975%26dopt%3DAbstract</link>
            <description>Editorial for the directed issue: &quot;Metabolic pathways in cancer&quot;
    Int J Biochem Cell Biol. 2011 Apr 29;
    Authors: Atzori L, Griffin JL, Scherer PE, Irminger-Finger I
    
    PMID: 21554975 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4805673</comments>
            <pubDate>Thu, 28 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4805673</guid>        </item>
        <item>
            <title>Enhanced functional properties of corneal epithelial cells by coculture with embryonic stem cells via the integrin Î²1-FAK-PI3K/Akt pathway.</title>
            <link>http://www.medworm.com/index.php?rid=4805678&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21550417%26dopt%3DAbstract</link>
            <description>This study employed a novel strategy to generate stem-like corneal epithelial cells and promote the functional properties of these cells by coculture with embryonic stem cells. The primary corneal epithelial cells were labelled with GFP and cocultured with embryonic stem cells in a transwell or by direct cell-cell contact. The embryonic stem cells were pre-transfected with HSV-tk-puro plasmids and became sensitive to ganciclovir. After 10 days of coculture, the corneal epithelial cells were isolated by treating the cultures with ganciclovir to kill the embryonic stem cells. The expression of stem cell-associated markers (ABCG2, p63) increased whereas the differentiation mark (Keratin 3) decreased in corneal epithelial cells isolated from the cocultures as evaluated by RT-PCR and flow cytom...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4805678</comments>
            <pubDate>Wed, 27 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4805678</guid>        </item>
        <item>
            <title>NARP mutation and mtDNA depletion trigger mitochondrial biogenesis which can be modulated by selenite supplementation.</title>
            <link>http://www.medworm.com/index.php?rid=4805677&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21550418%26dopt%3DAbstract</link>
            <description>Authors: Wojewoda M, DuszyÅ„ski J, Szczepanowska J
    The importance of mitochondrial biogenesis in the pathogenesis of mitochondrial diseases has been widely recognised but little is known about it with regard to NARP (Neuropathy, Ataxia and Retinitis Pigmentosa) syndrome. Since such knowledge would contribute to the understanding of the pathogenesis of this disease, we designed a study to provide comprehensive overview of mitochondrial biogenesis in cybrid cells harboring NARP mutation (8993T&amp;gt;G). We also used Rho0 cells with the same nuclear background to show that distinct mtDNA defects lead to distinct cellular responses irrespective of nuclear genome. Mitochondrial biogenesis is regulated by mitochondria-to-nucleus (retrograde) communication which depends on intracellular signalin...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4805677</comments>
            <pubDate>Wed, 27 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4805677</guid>        </item>
        <item>
            <title>Knockdown of ribosomal protein S7 causes developmental abnormalities via p53 dependent and independent pathways in zebrafish.</title>
            <link>http://www.medworm.com/index.php?rid=4805676&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21550419%26dopt%3DAbstract</link>
            <description>Authors: Duan J, Ba Q, Wang Z, Hao M, Li X, Hu P, Zhang D, Zhang R, Wang H
    Ribosomal proteins (RPs), structural components of the ribosome involved in protein synthesis, are of significant importance in all organisms. Previous studies have suggested that some RPs may have other functions in addition to assembly of the ribosome. The small ribosomal subunits RPS7, has been reported to modulate the mdm2-p53 interaction. To further investigate the biological functions of RPS7, we used morpholino antisense oligonucleotides (MO) to specifically knockdown RPS7 in zebrafish. In RPS7-deficient embryos, p53 was activated, and its downstream target genes and biological events were induced, including apoptosis and cell cycle arrest. Hematopoiesis was also impaired seriously in RPS7-deficient embry...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4805676</comments>
            <pubDate>Wed, 27 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4805676</guid>        </item>
        <item>
            <title>Calreticulin is crucial for calcium homeostasis mediated adaptation and survival of thick ascending limb of Henle's loop cells under osmotic stress.</title>
            <link>http://www.medworm.com/index.php?rid=4805674&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21554974%26dopt%3DAbstract</link>
            <description>Authors: Bibi A, Agarwal NK, Dihazi GH, Eltoweissy M, Van Nguyen P, Mueller GA, Dihazi H
    The thick ascending limb of Henle's loop (TALH) is normally exposed to variable and often very high osmotic stress and involves different mechanisms to counteract this stress. ER resident calcium binding proteins especially calreticulin (CALR) play an important role in different stress balance mechanisms. To investigate the role of CALR in renal epithelial cells adaptation and survival under osmotic stress, two-dimensional fluorescence difference gel electrophoresis combined with mass spectrometry and functional proteomics were performed. CALR expression was significantly altered in TALH cells exposed to osmotic stress, whereas renal inner medullary collecting duct cells and interstitial cells expo...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4805674</comments>
            <pubDate>Wed, 27 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4805674</guid>        </item>
        <item>
            <title>Mutual regulation of hypoxic and retinoic acid related signalling in tubular proximal cells.</title>
            <link>http://www.medworm.com/index.php?rid=4805671&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21554977%26dopt%3DAbstract</link>
            <description>Authors: FernÃ¡ndez-Martinez AB, JimÃ©nez MI, HernÃ¡ndez IS, GarcÃ­a-Bermejo ML, Manzano VM, Fraile EA, de Lucio-CazaÃ±a FJ
    Ypoxia-inducible factor-1Î± (HIF-1Î±) and all-trans retinoic acid (ATRA) afford protection in several experimental models of kidney disease. HIF-1Î± protein is degraded under normoxia but stabilized by hypoxia, which activates its transcription factor function. ATRA activates another set of transcription factors, the retinoic acid receptors (RAR) Î±, Î² and Î³, which mediate its effects on target genes. ATRA also up-regulates the expression of RAR Î±, Î² and Î³ at the transcriptional level. Here we demonstrate the presence of mutual regulation of hypoxic and retinoic acid related signalling in tubular proximal cells. In human proximal tubular HK-2 cells we have fo...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4805671</comments>
            <pubDate>Wed, 27 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4805671</guid>        </item>
        <item>
            <title>The large GTPase dynamin2: A new player in connexin 43 gap junction endocytosis, recycling and degradation.</title>
            <link>http://www.medworm.com/index.php?rid=4805672&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21554976%26dopt%3DAbstract</link>
            <description>Authors: Gilleron J, Carette D, Fiorini C, Dompierre J, Macia E, Denizot JP, Segretain D, Pointis G
    Connexins (Cx) are key regulators of cell proliferation, differentiation and apoptosis. Cx trafficking and endocytosis need interactions with a large number of signaling and scaffolding proteins. We demonstrate herein that Cx43-GFP gap junction plaque endocytosis was blocked in cells transfected by the dominant-negative form of dynamin2 (Dyn2K44A) and by dynasore, an inhibitor of dynamin GTPase activity, which reduced the association between dynamin2 and Cx43. Our data also reveal that recruitment of the GTPase at the plasma membrane and its activation by c-Src are key events for Cx43 internalization. In addition they show that dynamin2 participated in internalization and degradation of ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4805672</comments>
            <pubDate>Tue, 26 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4805672</guid>        </item>
        <item>
            <title>Regulation of progesterone receptor activity by cyclin dependent kinases 1 and 2 occurs in part by phosphorylation of the SRC-1 carboxyl-terminus.</title>
            <link>http://www.medworm.com/index.php?rid=4805675&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21550420%26dopt%3DAbstract</link>
            <description>We described previously a novel role for cyclin A2/Cdk2 as a progesterone receptor (PR) coactivator. In reporter gene assays, cyclin A2 overexpression enhanced PR activity while inhibition of Cdk2 activity using the chemical inhibitor roscovitine or Cdk2 siRNA strongly inhibited PR activity. We demonstrate here that both Cdk1 and Cdk2 contribute to maximal induction of endogenous progestin responsive genes in T47D breast cancer cells. Our earlier studies suggested that the mechanism by which cyclin A2/Cdk2 enhances PR activity is via phosphorylation of steroid receptor coactivator-1 (SRC-1), which increases PR-SRC-1 interactions. To assess the importance of SRC-1 phosphorylation in the regulation of PR activity, SRC-1 was phosphorylated by cyclin A2/Cdk2 in vitro and seventeen phosphorylat...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4805675</comments>
            <pubDate>Wed, 20 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4805675</guid>        </item>
        <item>
            <title>Microtubule and kinesin/dynein-dependent, bi-directional transport of autolysosomes in neurites of PC12 cells.</title>
            <link>http://www.medworm.com/index.php?rid=4805681&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21530677%26dopt%3DAbstract</link>
            <description>Authors: Yang Y, Feng LQ, Zheng XX
    Autophagy, a major degradative pathway of the lysosomal system, has been implicated in various neurodegenerative diseases. During autophagic process, organelles and proteins are encapsulated in double-membrane vacuoles called autophagosomes, which finally fuse with lysosomes to form autolysosomes where incorporated materials are degraded. Despite extensive investigations in identifying the molecular components that participate in autophagy, little is known about routes and dynamics of autophagosomes/autolysosomes in the neurites of live cells. Hence, in the present study, we aim to investigate the biophysical characteristics of neuritic transport of autolysosomes in PC12 cells. Our study demonstrated that monomeric red fluorescence protein-light chain...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4805681</comments>
            <pubDate>Tue, 19 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4805681</guid>        </item>
        <item>
            <title>Targeting metabolic pathways for cancer therapy.</title>
            <link>http://www.medworm.com/index.php?rid=4805679&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21540123%26dopt%3DAbstract</link>
            <description>Authors: Kargul J, Laurent GJ
    
    PMID: 21540123 [PubMed - as supplied by publisher] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4805679</comments>
            <pubDate>Tue, 19 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4805679</guid>        </item>
        <item>
            <title>Hepatocyte growth factor-induced c-Src-phosphatidylinositol 3-kinase-AKT-mammalian target of rapamycin pathway inhibits dendritic cell activation by blocking IÎºB kinase activity.</title>
            <link>http://www.medworm.com/index.php?rid=4805680&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21536148%26dopt%3DAbstract</link>
            <description>Authors: Singhal E, Sen P
    Hepatocyte growth factor modulates activation and antigen-presenting cell function of dendritic cells. However, the molecular basis for immunoregulation of dendritic cells by hepatocyte growth factor is undefined. In the current study, we demonstrate that hepatocyte growth factor exhibits inhibitory effect on dendritic cell activation by blocking IÎºB kinase activity and subsequent nuclear factor-ÎºB activation. Inhibition of IÎºB kinase is mediated by hepatocyte growth factor-induced activation of c-Src. Proximal signaling events induced in dendritic cells by hepatocyte growth factor include a physical association of c-Src with the hepatocyte growth factor receptor c-MET and concomitant activation of c-Src. Activation of c-Src in turn establishes a complex co...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4805680</comments>
            <pubDate>Mon, 18 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4805680</guid>        </item>
        <item>
            <title>Oxidative stress contributes to the induction and persistence of TGF-Î²1 induced pulmonary fibrosis.</title>
            <link>http://www.medworm.com/index.php?rid=4755338&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21514399%26dopt%3DAbstract</link>
            <description>In this study, primary human lung fibroblasts, MRC-5 fibroblasts and A549 epithelial cells were exposed to recombinant active TGF-Î²1. An adenovirus vector that expresses human ECSOD (AdECSOD) was constructed and rats were endotracheally intubated with an adenoviral vector encoding active TGF-Î²1 (AdTGF-Î²1), AdECSOD or a control vector (AdDL70) alone or in combinations AdTGF-Î²1/AdDL70 or AdTGF-Î²1/AdECSOD. TGF-Î²1 alone induced fibrotic responses and significantly down-regulated endogenous ECSOD gene expression both in vitro and in vivo and caused oxidative stress in rat lung, associated with increased levels of activated TGF-Î²1 in lung fluid and tissue. ECSOD protein was markedly reduced in the interstitium and fibrotic foci in TGF-Î²1 induced experimental lung fibrosis. The fibrotic r...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4755338</comments>
            <pubDate>Wed, 13 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4755338</guid>        </item>
        <item>
            <title>Sarcoplasmic reticulum: Structural determinants and protein dynamics.</title>
            <link>http://www.medworm.com/index.php?rid=4755337&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21515402%26dopt%3DAbstract</link>
            <description>Authors: Sorrentino V
    The sarcoplasmic reticulum is a unique organelle found in muscle cells that is dedicated to the regulation of Ca(2+) homeostasis and activation of myofilament contraction. The functional requirement for an efficient and synchronous activation of Ca(2+) release from the SR, following the depolarization of the plasma membrane, accounts for the complex three-dimensional organization of internal membranes observed in muscle cells and for the localization of proteins at specific sites of the SR. Recent advancements in understanding the molecular basis of SR structure and function have greatly increased our understanding of muscle cellular physiology and biology. Parallel work has revealed that several human diseases affecting skeletal and cardiac tissues are linked to ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4755337</comments>
            <pubDate>Wed, 13 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4755337</guid>        </item>
        <item>
            <title>Thiol-based redox signalling: Rust never sleeps.</title>
            <link>http://www.medworm.com/index.php?rid=4755339&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21513814%26dopt%3DAbstract</link>
            <description>Authors: Wouters MA, Iismaa S, Fan SW, Haworth NL
    Cysteine residues in proteins are covalently modified under conditions of oxidative and nitrosative stress by oxidation, nitrosation, glutathionylation and disulfide formation. Modifications induce conformational changes in substrate proteins, effecting signal cascades that evoke a biological response. A growing number of structures with modified cysteines are allowing a piecemeal understanding of the mechanistic aspects of these signalling pathways to emerge. Conformational changes upon conjugation of nitric oxide and glutathione are generally small and often accompanied by a local increase in protein disorder. Burial of nitric oxide is also apparent, which may increase the timeframe of signalling. Conformational changes upon disulfide...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4755339</comments>
            <pubDate>Tue, 12 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4755339</guid>        </item>
        <item>
            <title>Signalling pathways from NADPH oxidase-4 to idiopathic pulmonary fibrosis.</title>
            <link>http://www.medworm.com/index.php?rid=4755340&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21513813%26dopt%3DAbstract</link>
            <description>Authors: Crestani B, Besnard V, Boczkowski J
    This review focuses on the roles of NADPH oxidase/NOX proteins in idiopathic pulmonary fibrosis (IPF) pathophysiology and in the signalling pathways involved in IPF. NOX proteins are membrane-associated multi-unit enzymes that catalyze the reduction of oxygen using NADPH as an electron donor. Recent studies indicate that NOX4 is induced in pulmonary fibroblasts in response to TGF-Î². TGF-Î² or PDGF induce myofibroblast proliferation, differentiation, migration, contractility and extracellular matrix production, through NOX4 and reactive oxygen species dependent SMAD2/3 phosphorylation. NOX4 is increased in pulmonary fibroblasts from IPF patients and deletion of Nox4 in mice prevents bleomycin-induced pulmonary fibrosis. These data strongly s...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4755340</comments>
            <pubDate>Mon, 11 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4755340</guid>        </item>
        <item>
            <title>C1 domain residues Lys 2092 and Phe 2093 are of major importance for the endocytic uptake of coagulation factor VIII.</title>
            <link>http://www.medworm.com/index.php?rid=4755342&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21497669%26dopt%3DAbstract</link>
            <description>Authors: Meems H, van den Biggelaar M, Rondaij M, van der Zwaan C, Mertens K, Meijer AB
    Factor VIII (FVIII) catabolism has been demonstrated to involve LDL receptor-related protein (LRP). We have established that antibody fragment KM33 inhibits cofactor function of FVIII by interacting with the membrane binding region 2092-2093 of the C1 domain. As KM33 also inhibits LRP-dependent uptake of FVIII, we now assessed the role of region 2092-2093 for LRP-dependent endocytosis. For this purpose, we employed functional fluorescent FVIII-YFP or -GFP derivatives and U87MG cells which express high levels of LRP. Confocal microscopy studies and flow cytometry analysis combined with siRNA technology showed that the fluorescent FVIII derivatives are indeed effectively internalized by U87MG cells in...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4755342</comments>
            <pubDate>Thu, 07 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4755342</guid>        </item>
        <item>
            <title>Intrinsically disordered proteins from A to Z.</title>
            <link>http://www.medworm.com/index.php?rid=4755341&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21501695%26dopt%3DAbstract</link>
            <description>Authors: Uversky VN
    The ideas that proteins might possess specific functions without being uniquely folded into rigid 3D-structures and that these floppy polypeptides might constitute a noticeable part of any given proteome would have been considered as a preposterous fiction 15 or even 10 years ago. The situation has changed recently, and the existence of functional yet intrinsically disordered proteins and regions has become accepted by a significant number of protein scientists. These fuzzy objects with fuzzy structures and fuzzy functions are among the most interesting and attractive targets for modern protein research. This review summarizes some of the major discoveries and breakthroughs in the field of intrinsic disorder by representing related concepts and definitions.
    PMID...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4755341</comments>
            <pubDate>Thu, 07 Apr 2011 23:00:00 +0100</pubDate>
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        <item>
            <title>c-Jun is required for TGF-Î²-mediated cellular migration via nuclear Ca(2+) signaling.</title>
            <link>http://www.medworm.com/index.php?rid=4755345&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21447400%26dopt%3DAbstract</link>
            <description>Authors: Janowski E, Jiao X, Katiyar S, Lisanti MP, Liu M, Pestell RG, Morad M
    Tumor progression involves the acquisition of invasiveness through a basement membrane. The c-jun proto-oncogene is overexpressed in human tumors and has been identified at the leading edge of human breast tumors. TGF-Î² plays a bifunctional role in tumorigenesis and cellular migration. Although c-jun and the activator protein 1 (AP-1) complex have been implicated in human cancer, the molecular mechanisms governing cellular migration via c-jun and the role of c-Jun in TGF-Î² signaling remains poorly understood. Here, we analyze TGF-Î² mediated cellular migration in mouse embryo fibroblasts using floxed c-jun transgenic mice. We compared the c-jun wild type with the c-jun knockout cells through the use of Cre...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4755345</comments>
            <pubDate>Sun, 03 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4755345</guid>        </item>
        <item>
            <title>Organelles in Focus launch.</title>
            <link>http://www.medworm.com/index.php?rid=4581505&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21354514%26dopt%3DAbstract</link>
            <description>Authors: Kargul J, Laurent GJ
    
    PMID: 21354514 [PubMed - in process] (Source: The International Journal of Biochemistry and Cell Biology)</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4581505</comments>
            <pubDate>Mon, 14 Mar 2011 14:45:36 +0100</pubDate>
            <guid isPermaLink="false">4581505</guid>        </item>
        <item>
            <title>Molecular mechanisms of human lipodystrophies: from adipocyte lipid droplet to oxidative stress and lipotoxicity.</title>
            <link>http://www.medworm.com/index.php?rid=4581501&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21392585%26dopt%3DAbstract</link>
            <description>Authors: Vigouroux C, Caron-Debarle M, Le Dour C, MagrÃ© J, Capeau J
    Adipose tissue is now recognized for its major role in the control of energy metabolism and insulin sensitivity. We review here the human lipodystrophies, that are rare conditions in which total or partial fat loss is associated with severe lipid and glucose abnormalities leading to diabetes with early cardiovascular and hepatic complications. The genetic origin of a number of human lipodystrophies has been recently unraveled, emphasizing the importance of proteins of previously unknown or unexpected functions. Major adipose functions were also illuminated when studying acquired forms of lipodystrophies linked to human immunodeficiency virus-antiretrovirals. Overall, most of the proteins or functions affected by mutat...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4581501</comments>
            <pubDate>Mon, 07 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4581501</guid>        </item>
        <item>
            <title>Aluminum, copper, iron and zinc differentially alter amyloid-AÎ²(1-42) aggregation and toxicity.</title>
            <link>http://www.medworm.com/index.php?rid=4581504&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21376832%26dopt%3DAbstract</link>
            <description>Authors: Bolognin S, Messori L, Drago D, Gabbiani C, Cendron L, Zatta P
    Amyloid-Î²(1-42) (AÎ²) is believed to play a crucial role in the ethiopathogenesis of Alzheimer's Disease (AD). In particular, its interactions with biologically relevant metal ions may lead to the formation of highly neurotoxic complexes. Here we describe the species that are formed upon reacting AÎ² with several biometals, namely copper, zinc, iron, and with non-physiological aluminum to assess whether different metal ions are able to differently drive AÎ² aggregation. The nature of the resulting AÎ²-metal complexes and of the respective aggregates was ascertained through a number of biophysical techniques, including electrospray ionization mass spectrometry, dynamic light scattering, fluorescence, transmission e...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4581504</comments>
            <pubDate>Sat, 05 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4581504</guid>        </item>
        <item>
            <title>Cytokines: signaling molecules controlling ovarian functions.</title>
            <link>http://www.medworm.com/index.php?rid=4581502&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21382504%26dopt%3DAbstract</link>
            <description>Authors: Sirotkin AV
    The present short review demonstrates an important role of different cytokines (colony stimulating factors, tumor necrosis factors, interleukins, antimullerian hormone, inhibin, activin, follistatin, bone morphogenetic proteins, growth and differentiation factors) in control of different ovarian functions-ovarian cell proliferation, apoptosis, folliculogenesis, luteogenesis, oogenesis, release of hormones, response to upstream hormonal regulators, fertility and, in some cases, in development of ovarian disorders. The possibility of practical application of these molecules for characterization, prediction and regulation the ovarian state including treatment of ovarian disorders is demonstrated.
    PMID: 21382504 [PubMed - as supplied by publisher] (Source: The Inte...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4581502</comments>
            <pubDate>Fri, 04 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4581502</guid>        </item>
        <item>
            <title>The transmembrane domain of podoplanin is required for its association with lipid rafts and the induction of epithelial-mesenchymal transition.</title>
            <link>http://www.medworm.com/index.php?rid=4581503&amp;cid=s_35635_60_f&amp;fid=35635&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21376833%26dopt%3DAbstract</link>
            <description>THE TRANSMEMBRANE DOMAIN OF PODOPLANIN IS REQUIRED FOR ITS ASSOCIATION WITH LIPID RAFTS AND THE INDUCTION OF EPITHELIAL-MESENCHYMAL TRANSITION.
    Int J Biochem Cell Biol. 2011 Mar 2;
    Authors: FernÃ¡ndez-MuÃ±oz B, Yurrita MM, MartÃ­n-Villar E, Carrasco-RamÃ­rez P, MegÃ­as D, Renart J, Quintanilla M
    Podoplanin is a transmembrane glycoprotein that is upregulated in cancer and was reported to induce an epithelial-mesenchymal transition (EMT) in MDCK cells. The promotion of EMT was dependent on podoplanin binding to ERM (ezrin, radixin, moesin) proteins through its cytoplasmic (CT) domain, which led to RhoA-associated kinase (ROCK)-dependent ERM phosphorylation. Using detergent-resistant membrane (DRM) assays, as well as transmembrane (TM) interactions and ganglioside GM1 binding, we ...</description>
            <author>The International Journal of Biochemistry and Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4581503</comments>
            <pubDate>Wed, 02 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4581503</guid>        </item>
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