<?xml version="1.0" encoding="iso-8859-1"?>
<!-- generator="FeedCreator 1.7.2" -->
<rss version="2.0">
    <channel>
        <title>Molecular and Cellular Biochemistry 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 'Molecular and Cellular Biochemistry' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Molecular+and+Cellular+Biochemistry&t=Molecular+and+Cellular+Biochemistry&s=Search&f=source]]></link>
        <lastBuildDate>Sat, 20 Mar 2010 16:01:42 +0100</lastBuildDate>
        <item>
            <title>Non-genomic effects of thyroid hormone in adult cardiac myocytes: relevance to gene expression and cell growth.</title>
            <link>http://www.medworm.com/index.php?rid=3379449&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20232113%26dopt%3DAbstract</link>
            <description>In this study, we sought to determine whether TH activates intracellular signalling pathways in the adult cardiac myocytes and whether such activation modulates cell growth and the expression of target proteins important in cardiac function. We demonstrate that TH promotes a rapid increase in the phosphorylation of several kinases, ERK1/2, PKCdelta, p38-MAPK and Akt. This activation is inhibited by triiodothyroacetic acid (triac), which is a TH analogue known to displace the hormone from membrane bound receptors, indicating that this TH effect is mediated through a cell membrane-initiated mechanism. Furthermore, using specific inhibitors of the TH-activated kinases, we show that the long-term effects of TH on the expression of sarcoplasmic reticulum Ca(2+)-ATPase (SERCA), alpha- and beta-m...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3379449</comments>
            <pubDate>Tue, 16 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3379449</guid>        </item>
        <item>
            <title>SSeCKS promote beta-amyloid-induced PC12 cells neurotoxicity by up-regulating tau phosphorylation in Alzheimer's disease.</title>
            <link>http://www.medworm.com/index.php?rid=3379448&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20232114%26dopt%3DAbstract</link>
            <description>In this study, Abeta-induced apoptosis and tau phosphorylation were investigated in differentiated PC12 cells. This Abeta-induced tau phosphorylation paralleled with the increase of expression and phosphorylation of Src-suppressed protein kinase C substrate (SSeCKS). By knocking down the expression of SSeCKS, Abeta-induced apoptosis and tau hyperphosphorylation in PC12 cells were partially rescued, and were increased further due to the overexpression of SSeCKS in PC12 cells. Also, the cell apoptosis and tau hyperphosphorylation were strongly decreased when the cells were pretreated with the protein kinase C inhibitor, G&amp;#xF6;6983. In addition, Abeta-induced tau phosphorylation was also partially decreased due to the overexpression of SSeCKS in PC12cells. In summary, our data indicate that ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3379448</comments>
            <pubDate>Tue, 16 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3379448</guid>        </item>
        <item>
            <title>Amelioration of STZ-induced type 1 diabetic nephropathy by aqueous extract of Enicostemma littorale Blume and swertiamarin in rats.</title>
            <link>http://www.medworm.com/index.php?rid=3379447&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20229291%26dopt%3DAbstract</link>
            <description>Authors: Sonawane RD, Vishwakarma SL, Lakshmi S, Rajani M, Padh H, Goyal RK
    Diabetic nephropathy (DN) is one of the foremost causes of renal failure and a primary cause of diabetes mellitus related death. Previously, we have reported that aqueous extract of Enicostemma littorale has potential antidiabetic activity. In the present study, we have investigated the effect of aqueous extract of E. littorale 1 g/kg, p.o. and swertiamarin 50 mg/kg, p.o. daily for 3 weeks in type 1 DN complications in SD rats. DN was assessed by serum urea, creatinine, lipid profile and water intake levels. Treatment with aqueous extract of E. littorale and swertiamarin significantly decreased serum urea and creatinine and other parameters associated with the development of DN in type 1 diabetic rats. We have ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3379447</comments>
            <pubDate>Sun, 14 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3379447</guid>        </item>
        <item>
            <title>Establishment and characterization of multi-drug resistant, prostate carcinoma-initiating stem-like cells from human prostate cancer cell lines 22RV1.</title>
            <link>http://www.medworm.com/index.php?rid=3360074&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20224986%26dopt%3DAbstract</link>
            <description>Authors: Liu T, Xu F, Du X, Lai D, Liu T, Zhao Y, Huang Q, Jiang L, Huang W, Cheng W, Liu Z
    Multi-drug resistance is an important element which leads to ineffectiveness of chemotherapeutics. To identify subpopulations of cancerous prostate cells with mutli-drug resistance and cancer stem-cell properties has recently become a major research interest. We identified a subpopulation from the prostate cancer cell line 22RV1, which have high surface expression of both CD117 and ABCG2. We found this subpopulation of cells termed CD117(+)/ABCG2(+) also overexpress stem cells markers such as Nanog, Oct4, Sox2, Nestin, and CD133. These cells are highly prolific and are also resistant to treatment with a variety of chemotherapeutics such as casplatin, paclitaxel, adriamycin, and methotrexate. In ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3360074</comments>
            <pubDate>Fri, 12 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3360074</guid>        </item>
        <item>
            <title>Expression of PE_PGRS 62 protein in Mycobacterium smegmatis decrease mRNA expression of proinflammatory cytokines IL-1beta, IL-6 in macrophages.</title>
            <link>http://www.medworm.com/index.php?rid=3360083&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20221673%26dopt%3DAbstract</link>
            <description>In this study, we expressed PE_PGRS 62 gene in a non-pathogenic fast growing Mycobacterium smegmatis strain and found that the recombinant Mycobacterium smegmatis decreased macrophages livability in a dosage-dependent manner and time-dependent manner, compared with parental strain containing the vector only. To explore whether PE_PGRS 62 modulates the gene expression profile of macrophages, we stimulated macrophages by the M. smegmatis strain expressing PE_PGRS 62 as well as the control strains, followed by real-time RT-PCR assay for the mRNA expression level of IL-1beta, IL-6, and iNOS. The results showed that the expression of IL-1beta, IL-6 in macrophages were down-regulated by stimulation with the M. smegmatis strain expressing PE_PGRS 62 compared to the control strains (P &amp;lt; 0.05). ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3360083</comments>
            <pubDate>Thu, 11 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3360083</guid>        </item>
        <item>
            <title>Effects of metformin on glucose metabolism of perfused rat livers.</title>
            <link>http://www.medworm.com/index.php?rid=3352848&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20217188%26dopt%3DAbstract</link>
            <description>Authors: de Souza Silva FM, Rocha Alves da Silva MH, Bracht A, Eller GJ, Constantin RP, Yamamoto NS
    Although metformin has been used to treat type 2 diabetes for several decades, the mechanism of its action on glucose metabolism remains controversial. To further assess the effect of metformin on glucose metabolism this work was undertaken to investigate the acute actions of metformin on glycogenolysis, glycolysis, gluconeogenesis, and ureogenesis in perfused rat livers. Metformin (5 mM) inhibited oxygen consumption and increased glycolysis and glycogenolysis in livers from fed rats. In perfused livers of fasted rats, the drug (concentrations higher than 1.0 mM) inhibited oxygen consumption and glucose production from lactate and pyruvate. Gluconeogenesis and ureogenesis from alanine we...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3352848</comments>
            <pubDate>Tue, 09 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3352848</guid>        </item>
        <item>
            <title>Influence of gel and powdered formulations of coenzyme Q10 on metabolic parameters in rats.</title>
            <link>http://www.medworm.com/index.php?rid=3352850&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20213261%26dopt%3DAbstract</link>
            <description>In conclusion, both gel- and powdered-formulations of Co Q10 significantly influenced the metabolic parameters assessed in a favorable fashion, with the powdered-formulation more effective on SBP and the gel-formulation more effective on overcoming hepatic DNA fragmentation. From the data, we conclude that the choice of the formulation containing Co Q10 to be used should be based on the desired healthful benefits.
    PMID: 20213261 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3352850</comments>
            <pubDate>Sun, 07 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3352850</guid>        </item>
        <item>
            <title>Comparative effects of a novel plant-based calcium supplement with two common calcium salts on proliferation and mineralization in human osteoblast cells.</title>
            <link>http://www.medworm.com/index.php?rid=3352849&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20213262%26dopt%3DAbstract</link>
            <description>Authors: Adluri RS, Zhan L, Bagchi M, Maulik N, Maulik G
    Calcium is an essential mineral to support bone health and serves as a major therapeutic intervention to prevent and delay the incidence of osteoporosis. Many individuals do not obtain the optimum amount of calcium from diets and depend on bioavailable calcium supplements. The present study was conducted to examine the effect of a novel plant-based calcium supplement, derived from marine algae, and contains high levels of calcium, magnesium, and other bone supporting minerals [commercially known as AlgaeCal (AC)], on proliferation, mineralization, and oxidative stress in cultured human osteoblast cells, and compared with inorganic calcium carbonate and calcium citrate salts. Cultured human fetal osteoblast cells (hFOB 1.19) were ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3352849</comments>
            <pubDate>Sun, 07 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3352849</guid>        </item>
        <item>
            <title>ROS-NFkappaBeta mediates TGF-beta1-induced expression of urokinase-type plasminogen activator, matrix metalloproteinase-9 and cell invasion.</title>
            <link>http://www.medworm.com/index.php?rid=3339899&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20204677%26dopt%3DAbstract</link>
            <description>Authors: Tobar N, Villar V, Santibanez JF
    TGF-beta1 has been postulated as a pro-oncogenic factor in the late step of the tumoral progression. In transformed cells, TGF-beta1 enhances the capacity to degrade the extracellular matrix, cell invasiveness and epithelial-mesenchymal transition, which are crucial steps for metastasis. Urokinase-type plasminogen activator (uPA) and matrix metalloproteinase-9 (MMP-9) are critical components in cell migration and invasion induced by TGF-beta1, however, the exact mechanism by which TGF-beta1 regulates uPA and MMP-9 is not well elucidated so far. In the present study, we analyzed the role of ROS-NFkappaBeta, signal as mediator in the cell malignity enhancement by TGF-beta1. We found that TGF-beta1 activates NFkappaBeta, through Rac1-NOXs-ROS-depe...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3339899</comments>
            <pubDate>Fri, 05 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3339899</guid>        </item>
        <item>
            <title>The glycan profile of endothelial cells in the present of tumor-conditioned medium and potential roles of beta-1,6-GlcNAc branching on HUVEC conformation.</title>
            <link>http://www.medworm.com/index.php?rid=3339898&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20204678%26dopt%3DAbstract</link>
            <description>In conclusion, our results strongly suggested that the carbohydrate composition of endothelial cell surface is very important for the cells to exert their physiological effects correlated with cancer extravasation.
    PMID: 20204678 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3339898</comments>
            <pubDate>Fri, 05 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3339898</guid>        </item>
        <item>
            <title>Antiproliferative effect of peripheral benzodiazepine receptor antagonist PK11195 in rat mammary tumor cells.</title>
            <link>http://www.medworm.com/index.php?rid=3339900&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20204676%26dopt%3DAbstract</link>
            <description>This study aims to establish the antiproliferative effects of PK11195, a peripheral benzodiazepine receptor antagonist (PBR) in rat mammary tumor cells. Breast tumors were induced by administration of a carcinogen, dimethylbenz[a]anthracene to 50-day-old female rats maintained on a standard AIN-76A diet with casein as the protein source. The tumors were developed approximately after 120 days. The tumors were of grade I (20%), grade II (60%), and grade III (20%). The tumors were isolated and cultured in DMEM/F12 media with supplements. We characterized the properties of the isolated cells and study the effect of PK11195 on those cells. We were successful in growing breast tumor cells up to 30 passages for cellular characterization. These cells had high reactivity with Ki-67 and PCNA antibod...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3339900</comments>
            <pubDate>Thu, 04 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3339900</guid>        </item>
        <item>
            <title>Kynurenine-induced photo oxidative damage to lens in vitro: protective effect of caffeine.</title>
            <link>http://www.medworm.com/index.php?rid=3339897&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20204679%26dopt%3DAbstract</link>
            <description>Authors: Varma SD, Hegde KR
    Photochemical generation of reactive species of oxygen in the lens and aqueous and consequent physiological damage to the tissue has been implicated in the genesis of human cataracts. The present studies were undertaken to examine the feasibility of possible prevention of such damage to the lens initiated by UV activation of kynurenine, a well-known photosensitizer in the human lens. The studies were done by organ culturing intact mouse lenses in medium containing kynurenine and exposed to UVA. Tissue damage was assessed by the inhibition of its ability to carry active transport of rubidium ions and the associated decrements in the levels of GSH and ATP. These deleterious effects were significantly prevented by caffeine, an alkaloid present in many common be...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3339897</comments>
            <pubDate>Thu, 04 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3339897</guid>        </item>
        <item>
            <title>Alterations in Ca(2+) homeostasis in rat erythrocytes with atrazine treatment: positive modulation by vitamin E.</title>
            <link>http://www.medworm.com/index.php?rid=3327862&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20195705%26dopt%3DAbstract</link>
            <description>Authors: Singh M, Sandhir R, Kiran R
    A very low level of intra-erythrocytic calcium content is very important for normal physiology of cells. In the present study, our main objective was to investigate the effects of atrazine toxicity on Ca(2+) homeostasis and modulation by vitamin E. Experimental animals were orally administered atrazine (300 mg kg(-1) body weight, daily) and vitamin E (100 mg kg(-1) body weight, daily). All studies were carried out for 7, 14, and 21 days in male Wistar rats. Erythrocyte membranes were prepared and were analyzed for lipid peroxidation (LPO) and membrane bound ATPases. Furthermore, Ca(2+) homeostasis was evaluated in erythrocytes. The present findings indicated that atrazine exposure induced oxidative stress which was associated with significant increa...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3327862</comments>
            <pubDate>Sat, 27 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3327862</guid>        </item>
        <item>
            <title>E4BP4 is a cardiac survival factor and essential for embryonic heart development.</title>
            <link>http://www.medworm.com/index.php?rid=3318918&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20186462%26dopt%3DAbstract</link>
            <description>In this study, Dot-blot hybridization assays using Dig-labeled RNA probes revealed that the E4BP4 gene was expressed in cardiac tissue from several species including, monkey, dog, rabbit, and human. Western blot analysis showed that the E4BP4 protein was consistently present in all of these four species. Furthermore, immunohistochemistry revealed that the E4BP4 protein was overexpressed in diseased heart tissue in comparison with normal heart tissue. In addition, the overexpression of E4BP4 in vitro activated cell survival signaling pathway of cardiomyocytes. At last, siRNA-mediated knock down of E4BP4 in zebrafish resulted in malformed looping of the embryonic heart tube and decreased heart beating. Based on these results, we conclude that E4BP4 plays as a survival factor in heart and E4B...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3318918</comments>
            <pubDate>Fri, 26 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3318918</guid>        </item>
        <item>
            <title>Cbl-b promotes chemotherapy-induced apoptosis in rat basophilic leukemia cells by suppressing PI3K/Akt activation and enhancing MEK/ERK activation.</title>
            <link>http://www.medworm.com/index.php?rid=3308399&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20177738%26dopt%3DAbstract</link>
            <description>In this study, VP-16-induced RBL-2H3 cells apoptosis was accompanied by the activation of Akt and ERK. The PI3K inhibitor LY294002, not the ERK inhibitor PD98059, enhanced the apoptosis. In addition, down-regulation of Cbl-b was also detected. Over expression of Cbl-b significantly enhanced VP-16-induced cell apoptosis with inhibition of Akt activity, while a dominant negative (DN) RING Finger domain mutation completely abolished this enhancement. On the other hand, ERK activity was enhanced by Cbl-b, and the ERK inhibitor PD98059 reversed Cbl-b-enhanced apoptosis. The consistent results were also showed in the process of Ara-c treatment. These observations indicate that Cbl-b promotes RBL-2H3 apoptosis induced by VP-16 or Ara-c, probably through inhibition of Akt and activation of ERK.
  ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3308399</comments>
            <pubDate>Wed, 24 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3308399</guid>        </item>
        <item>
            <title>Diphenyl diselenide and diphenyl ditelluride: neurotoxic effect in brain of young rats, in vitro.</title>
            <link>http://www.medworm.com/index.php?rid=3308396&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20179992%26dopt%3DAbstract</link>
            <description>This study examined whether maturity of rat brain may be relevant for the sensitivity to diphenyl diselenide (PhSe)(2) and diphenyl ditelluride (PhTe)(2) on [(3)H]glutamate uptake and release, in vitro. Brain synaptosomes were isolated from young (14- and 30-day-old) and adult rats and incubated at different concentrations of (PhSe)(2) or (PhTe)(2). The results demonstrated that the highest concentration (100 muM) of (PhSe)(2) and (PhTe)(2) inhibited the [(3)H]glutamate uptake by synaptosomes of brain at all ages. In the adult brain, (PhSe)(2) did not inhibit the [(3)H]glutamate uptake at the lowest concentration (10 muM). The highest concentration of (PhTe)(2) inhibited the [(3)H]glutamate uptake more in the 14-day-old than in the 30-day-old rats or adult rats. In the 30-day-old animals, ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3308396</comments>
            <pubDate>Wed, 24 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3308396</guid>        </item>
        <item>
            <title>Newly identified tumor-associated role of human Sharpin.</title>
            <link>http://www.medworm.com/index.php?rid=3308395&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20179993%26dopt%3DAbstract</link>
            <description>Authors: Jung J, Kim JM, Park B, Cheon Y, Lee B, Choo SH, Koh SS, Lee S
    In order to discover previously unidentified cancer-associated genes, we analyzed genome-wide differences in gene expression between tumor biopsies and normal tissues. Among those differentially regulated genes, we identified Sharpin (Shank-associated RH domain-interacting protein) as a commonly up-regulated gene in multiple human cancer types. Although rat Sharpin is reported to interact with Shank1, a multidomain scaffold protein localized in postsynaptic densities, its exact roles are unknown. Whereas human Sharpin homologue was primarily localized in the cytosol of cultured cells, they were detected in both cytosol and nucleus of the cells from ovarian and liver cancer tissues using immunohistochemical staining...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3308395</comments>
            <pubDate>Wed, 24 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3308395</guid>        </item>
        <item>
            <title>Acid-sensing ion channel 1a mediates acid-induced increases in intracellular calcium in rat articular chondrocytes.</title>
            <link>http://www.medworm.com/index.php?rid=3308394&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20179994%26dopt%3DAbstract</link>
            <description>Authors: Yuan FL, Chen FH, Lu WG, Li X, Wu FR, Li JP, Li CW, Wang Y, Zhang TY, Hu W
    Acid-sensing ion channels (ASICs) are cationic channels that are activated by extracellular acidification and implicated in pain perception, ischemic stroke, mechanosensation, learning, and memory. It has been shown that ASIC1a is an extracellular pH sensor in the central and peripheral nervous systems, but its physiological and pathological roles in non-neural cells are poorly understood. We demonstrated a novel physiological function of ASIC1a in rat articular chondrocytes. The expression of ASIC1a mRNA and protein in rat articular chondrocytes was evaluated by reverse transcriptase polymerase chain reaction (RT-PCR) and Western blotting. The distribution of ASIC1a protein located in articular chondro...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3308394</comments>
            <pubDate>Wed, 24 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3308394</guid>        </item>
        <item>
            <title>Alterations in the content and physiological role of sphingomyelin in plasma membranes of cells cultured in three-dimensional matrix.</title>
            <link>http://www.medworm.com/index.php?rid=3308400&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20177737%26dopt%3DAbstract</link>
            <description>Authors: Lupanova T, Stefanova N, Petkova D, Staneva G, Jordanova A, Koumanov K, Pankov R, Momchilova A
    The three-dimensional (3D) cell culture approach offers a means to study cells under conditions that mimic an in vivo environment, thus avoiding the limitations imposed by the conventional two-dimensional (2D) monolayer cell cultures. By using this approach we demonstrated significant differences in the plasma membrane phospholipid composition and susceptibility to oxidation in cells cultured in three-dimensional environment compared to conventional monolayer cultures. The plasma membrane sphingomyelin (SM), which is a functionally active membrane phospholipid, was markedly increased in plasma membranes of 3D cells. To analyze the mechanisms underlying SM accumulation, we determined ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3308400</comments>
            <pubDate>Tue, 23 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3308400</guid>        </item>
        <item>
            <title>Mechanism for the regulation of mammalian cGMP phosphodiesterase6. 2: Isolation and characterization of the transducin-activated form.</title>
            <link>http://www.medworm.com/index.php?rid=3308398&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20177739%26dopt%3DAbstract</link>
            <description>Authors: Yamazaki A, Tatsumi M, Bondarenko VA, Kurono S, Komori N, Matsumoto H, Matsuura I, Hayashi F, Yamazaki RK, Usukura J
    Rod photoreceptor cGMP phosphodiesterase (PDE6) consists of a catalytic subunit complex (Palphabeta) and two inhibitory subunits (Pgamma). In the accompanying article, using bovine photoreceptor outer segment homogenates, we show that Pgamma as a complex with the GTP-bound transducin alpha subunit (GTP-Talpha) dissociates from Palphabetagammagamma on membranes, and the Palphabetagammagamma becomes Pgamma-depleted. Here, we identify and characterize the Pgamma-depleted PDE. After incubation with or without guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS), Palphabeta complexes are extracted. When a hypotonic buffer is used, Palphabetagammagamma, Palphabetagamma, an...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3308398</comments>
            <pubDate>Tue, 23 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3308398</guid>        </item>
        <item>
            <title>Focal adhesion kinase mediates TGF-beta1-induced renal tubular epithelial-to-mesenchymal transition in vitro.</title>
            <link>http://www.medworm.com/index.php?rid=3308397&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20177740%26dopt%3DAbstract</link>
            <description>In conclusion, FAK may play a crucial role in mediating TGF-beta1-induced EMT through the activation of Akt pathway.
    PMID: 20177740 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3308397</comments>
            <pubDate>Tue, 23 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3308397</guid>        </item>
        <item>
            <title>The structure of the 5'-untranslated region of mammalian poly(A) polymerase-alpha mRNA suggests a mechanism of translational regulation.</title>
            <link>http://www.medworm.com/index.php?rid=3308402&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20174964%26dopt%3DAbstract</link>
            <description>Authors: Rapti A, Trangas T, Samiotaki M, Ioannidis P, Dimitriadis E, Meristoudis C, Veletza S, Courtis N
    Poly(A)polymerase-alpha (PAPOLA) has been the most extensively investigated mammalian polyadenylating enzyme, mainly in regard to its multifaceted post-translational regulation. The possibility of translational regulation of this enzyme was addressed. The transcription start site was mapped and two uORFs, highly conserved among several species, were identified in the 211-bp long, GC-rich, 5' UTR of the PAPOLA mRNA. Mutation of the 5' proximal AUG resulted in increased translational efficiency of the adjacent coding sequence, whereas no significant effect was observed after mutation of the second AUG. These observations imply that translational regulation is among the conserved mech...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3308402</comments>
            <pubDate>Sun, 21 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3308402</guid>        </item>
        <item>
            <title>Betulinic acid inhibits the expression of hypoxia-inducible factor 1alpha and vascular endothelial growth factor in human endometrial adenocarcinoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=3308401&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20174965%26dopt%3DAbstract</link>
            <description>Authors: Karna E, Szoka L, Palka JA
    Although betulinic acid (BA) is known to induce apoptosis and antiangiogenic response in tumor cells, the underlying mechanism of its action is unknown. Deregulation of tissue collagen metabolism is one of the consequences of neoplastic transformation. The final step of collagen degradation is mediated by prolidase [E.C.3.4.13.9] which may play a role in angiogenesis. The formation of new blood vessels is regulated by the hypoxia-inducible factor 1 (HIF-1). The expression of HIF-1 correlates with hypoxia-induced angiogenesis as a result of the induction of vascular endothelial cell growth factor (VEGF). Since BA evokes anticancer activity, its effect on collagen biosynthesis, HIF-1alpha and VEGF expressions, as well as prolidase activity and expressi...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3308401</comments>
            <pubDate>Sun, 21 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3308401</guid>        </item>
        <item>
            <title>The dependence of enhanced lysosomal activity on the cellular aging of bovine aortic endothelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=3308465&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20174960%26dopt%3DAbstract</link>
            <description>Authors: Yoon J, Kim KJ, Choi YW, Shin HS, Kim YH, Min J
    Lysosomes are a cell organelle type processing antimicrobial activity. Here, we investigate the lysosomal activity in a primary cell line, bovine aortic endothelial cells (BAECs), during cellular aging, based on the antimicrobial activity of lysosomes isolated from BAECs at cell passages 4, 6, 8, and 10. Cytochemical analysis of lysosomes with LysoTracker reagent revealed the number of lysosome-like organelles surrounding the nucleus initially increased drastically in the BAECs and continued increasing gradually until passage 10. The lysosomes isolated from each successive passage of BAECs exhibited increased antimicrobial activity against Escherichia coli, and, in addition, an age-dependent increase in lysosome intensity coincid...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3308465</comments>
            <pubDate>Sat, 20 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3308465</guid>        </item>
        <item>
            <title>Human angiogenin presents neuroprotective and migration effects in neuroblastoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=3308448&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20174961%26dopt%3DAbstract</link>
            <description>In this study, we investigate whether human wild type ANG (wANG) and its variant K40I (mANG) maintain their divergent functional capacities in neuronal cells. To evaluate this, SH-SY5Y neuroblastoma cells were transfected with wANG and mANG DNA and identified both wild and mutant ANG are localized to nuclei and have no effects on proliferation. We have shown that human wANG prevented cell death under H(2)O(2)-induced oxidative stress in both SH-SY5Y and NSC-34 cells, tested by MTT assay. These effects were more enhanced in motor neuron cell NSC-34. wANG also played a role in cell migration, while mANG decreased these functional activities. Immunoblot analysis revealed that the intracellular signaling of ERK1/2 (at Thr183/Tyr185) was increased following transfection of the wANG gene, and si...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3308448</comments>
            <pubDate>Sat, 20 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3308448</guid>        </item>
        <item>
            <title>High fat diet induces ceramide and sphingomyelin formation in rat's liver nuclei.</title>
            <link>http://www.medworm.com/index.php?rid=3308404&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20174962%26dopt%3DAbstract</link>
            <description>Authors: Chocian G, Chabowski A, Zendzian-Piotrowska M, Harasim E, Lukaszuk B, G&amp;#xF3;rski J
    Obesity increases the risk for hepatic steatosis. Recent studies have demonstrated that high fat diet (HFD) may affect sphingolipid formation in skeletal muscles, heart, and other tissues. In this work we sought to investigate whether HFD feeding provokes changes in content and fatty acids (FAs) composition of sphingomyelin and ceramide at the level of liver and hepatic nuclei. Furthermore, we investigated whether the ceramide formation is related to the activity of either neutral sphingomyelinase (N-SMase) or acidic sphingomyelinase (A-SMase). Three weeks of HFD provision induced pronounced ceramide and sphingomyelin accumulation in both liver and hepatic nuclei, accompanied by increased activ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3308404</comments>
            <pubDate>Sat, 20 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3308404</guid>        </item>
        <item>
            <title>Alloxan reduces amplitude of ventricular myocyte shortening and intracellular Ca(2+) without altering L-type Ca (2+) current, sarcoplasmic reticulum Ca (2+) content or myofilament sensitivity to Ca (2+) in Wistar rats.</title>
            <link>http://www.medworm.com/index.php?rid=3308403&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20174963%26dopt%3DAbstract</link>
            <description>Authors: Salem KA, Qureshi A, Ljubisavijevic M, Oz M, Isaev D, Hussain M, Howarth FC
    Alloxan is widely used to induce diabetes mellitus in experimental animals. Recent studies have provided evidence that alloxan has direct actions on cardiac muscle contraction. The aim of this study was to further investigate the mechanisms underlying the effects of alloxan on ventricular myocyte shortening and intracellular Ca(2+) transport. Amplitude of myocyte shortening was reduced in a dose-dependent manner as the concentration of alloxan was increased in the range 10(-7)-10(-4) M. Amplitude of shortening was reduced (56.8 +/- 6.6%, n = 27) by 10(-6) M alloxan and was partially reversed during a 10 min washout. Amplitude of the Ca(2+) transient was also reduced (79.7 +/- 2.9%, n = 29) by 10(-6) M ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3308403</comments>
            <pubDate>Sat, 20 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3308403</guid>        </item>
        <item>
            <title>Overexpression of NYGGF4 (PID1) induces mitochondrial impairment in 3T3-L1 adipocytes.</title>
            <link>http://www.medworm.com/index.php?rid=3291161&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20165904%26dopt%3DAbstract</link>
            <description>In this study, we demonstrated that the overexpression of NYGGF4 in 3T3-L1 adipocytes decreased mitochondrial mass, mitochondrial DNA, and intracellular ATP synthesis. In addition, NYGGF4 overexpression also led to an imbalance of the mitochondrial dynamics and excess intracellular ROS production. Collectively, our results indicated that the overexpression of NYGGF4 caused mitochondrial dysfunction in adipocytes, which might be responsible for the development of NYGGF4-induced insulin resistance.
    PMID: 20165904 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3291161</comments>
            <pubDate>Thu, 18 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3291161</guid>        </item>
        <item>
            <title>Dichloroacetate (DCA) enhances tumor cell death in combination with oncolytic adenovirus armed with MDA-7/IL-24.</title>
            <link>http://www.medworm.com/index.php?rid=3291160&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20165905%26dopt%3DAbstract</link>
            <description>Authors: Xiao L, Li X, Niu N, Qian J, Xie G, Wang Y
    Dichloroacetate (DCA) is a metabolic modulator for the treatment of lactic acidosis and inherited mitochondrial diseases. A recent study showed that DCA treatment could induce apoptosis in many kinds of tumor cell lines via mitochondrial apoptotic pathway while sparing normal cells. ONYX-015 (dl 1520) is one of the oncolytic adenoviruses developed by the deletion of E1B-55kD gene of type 5 adenoviral DNA, and it replicates efficiently and selectively in tumor cells. ZD55-IL-24, an E1B-55kD deleted oncolytic adenovirus carrying interleukin-24 (IL-24, also called melanoma differentiation associated gene-7), had showed potent antitumor efficacy in a variety of tumor cells and exerted no apparent toxicity on normal cells. Given both the g...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3291160</comments>
            <pubDate>Thu, 18 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3291160</guid>        </item>
        <item>
            <title>Isolation and characterization of a novel zinc finger gene, ZNFD, activating AP1(PMA) transcriptional activities.</title>
            <link>http://www.medworm.com/index.php?rid=3284366&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20162441%26dopt%3DAbstract</link>
            <description>In this study, we isolate a novel C(2)H(2) ZNF (Zinc Finger) gene ZNFD. It contains an ORF (Open Reading Frame) with a length of 990 bp, encoding 329 amino acids. The predicted protein contains a C(2)H(2) zinc finger. RT-PCR analysis in 18 human adult tissues indicated that it was expressed in five human adult tissues. Green fluorescence protein localization analysis showed that human ZNFD was located in the nucleus of Hela cells. Overexpression of ZNFD in the COS7 cells activates the transcriptional activities of AP1(PMA) (Activator of protein 1, that responds specifically to phobol ester). Together the data indicate that ZNFD is probably a new type of C(2)H(2) ZFP and the ZNFD protein may act as a transcriptional activator in PKC (protein kinase C) signal pathway to mediate cellular func...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3284366</comments>
            <pubDate>Thu, 18 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3284366</guid>        </item>
        <item>
            <title>CBP knockdown inhibits angiotensin II-induced vascular smooth muscle cells proliferation through downregulating NF-kB transcriptional activity.</title>
            <link>http://www.medworm.com/index.php?rid=3284369&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20157765%26dopt%3DAbstract</link>
            <description>Authors: Yang J, Jiang H, Chen SS, Chen J, Xu SK, Li WQ, Wang JC
    CREB binding protein (CBP), a powerful transcriptional co-activator for various transcriptional factors, regulates cell behavior in many cell types. Angiotensin II (Ang II) contributes to vascular lesion by promoting vascular smooth muscle cells (VSMCs) proliferation and migration. Therefore, we examined whether CBP knockdown could suppress Ang II-induced VSMCs proliferation, and elucidated its underlying molecular mechanism. We constructed lentiviral vector expressing CBP-specific short hairpin RNAs (shRNAs) that efficiently silenced CBP. VSMCs proliferation was evaluated by bromodeoxyuridine (BrdU) incorporation assay. Protein and mRNA expression of CBP and relevant cytokines were examined by Western blot, ELISA, and re...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3284369</comments>
            <pubDate>Tue, 16 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3284369</guid>        </item>
        <item>
            <title>Notch signaling maintains proliferation and survival of the HL60 human promyelocytic leukemia cell line and promotes the phosphorylation of the Rb protein.</title>
            <link>http://www.medworm.com/index.php?rid=3284368&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20157766%26dopt%3DAbstract</link>
            <description>Authors: Li GH, Fan YZ, Liu XW, Zhang BF, Yin DD, He F, Huang SY, Kang ZJ, Xu H, Liu Q, Wu YL, Niu XL, Zhang L, Liu L, Hao MW, Han H, Liang YM
    The Notch signaling pathway has been implicated in the development of several leukemia and lymphoma. In order to investigate the relationship between Notch signaling and acute myeloid leukemia (AML), in this study, we expressed a recombinant Notch ligand protein, the DSL domain of the human Jagged1 fused with GST (GST-Jag1). GST-Jag1 could activate Notch signaling in the human promyelocytic leukemia cell line HL60, as shown by a reporter assay and the induced expression of Notch effector gene Hes1 and Hes5. However, GST-Jag1 had no effect on the proliferation and survival of HL60 cells. HL60 cells expressed both Notch ligands and receptors, and ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3284368</comments>
            <pubDate>Tue, 16 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3284368</guid>        </item>
        <item>
            <title>Lefty A attenuates the TGF-beta1-induced epithelial to mesenchymal transition of human renal proximal epithelial tubular cells.</title>
            <link>http://www.medworm.com/index.php?rid=3284367&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20157767%26dopt%3DAbstract</link>
            <description>Authors: Li Y, Zhang J, Fang L, Luo P, Peng J, Du X
    The epithelial to mesenchymal transition (EMT) is a crucial event for renal fibrosis that can be elicited by TGF-beta1/Smads signaling and its downstream mediator connective tissue growth factor (CTGF). As a distinct member of the TGF-beta superfamily, Lefty A has been shown to be significantly downregulated in the kidneys of patients with severe ureteral obstruction, suggesting its role in renal fibrosis induced by obstructive nephropathy. In order to determine whether Lefty A prevents TGF-beta1-induced EMT, human proximal tubule epithelial cells (HK-2) were stably transfected with Lefty A or control vectors and stimulated with 10 ng/ml TGF-beta1 for 48 h. The results show that stimulation with TGF-beta1 led to EMT including cell mor...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3284367</comments>
            <pubDate>Tue, 16 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3284367</guid>        </item>
        <item>
            <title>Sphingolipids of human umbilical cord vein and their alteration in preeclampsia.</title>
            <link>http://www.medworm.com/index.php?rid=3276518&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20155487%26dopt%3DAbstract</link>
            <description>Authors: Romanowicz L, Ba&amp;#x144;kowski E
    Preeclampsia is the most common pregnancy-associated pathological syndrome. It is accompanied by the accumulation of free fatty acids, acylglycerols and cholesterol esters in the umbilical cord vein (UCV). We evaluate the sphingolipid composition of UCV and its alteration in preeclampsia. The veins were taken from 10 newborns delivered by healthy mothers and 10 newborns delivered by mothers with preeclampsia. Thin layer chromatography, solid-phase extraction and high-performance liquid chromatography were employed for sphingolipid analyses. The UCV walls of newborns delivered by healthy mothers are abundant in sphingomyelins and ceramides, whereas the amounts of sphingoid bases are rather low. Preeclampsia is associated with a significant decrea...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276518</comments>
            <pubDate>Sun, 14 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276518</guid>        </item>
        <item>
            <title>Proximity of Na(+)-Ca (2+)-exchanger and sarco/endoplasmic reticulum Ca(2+) pump in pig coronary artery smooth muscle: fluorescence microscopy.</title>
            <link>http://www.medworm.com/index.php?rid=3276517&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20155488%26dopt%3DAbstract</link>
            <description>Authors: Kuszczak I, Kuner R, Samson SE, Grover AK
    Pig coronary artery smooth muscle expresses the Na(+)-Ca(2+)-exchanger NCX1 and the sarco/endoplasmic reticulum (SER) Ca(2+) pump SERCA2. NCX has been proposed to play a role in refilling the SER Ca(2+) pool. Caveolae may also direct Ca(2+) traffic during cell signaling. Here, we use immunofluorescence microscopy to determine if there is proximity between NCX1, SERCA2, and the caveolar protein caveolin-1. Stacks of images of cell surface domains were analyzed. Image stacks for one protein were analyzed for overlap with another protein, with and without randomization or image shifting. Within the resolution of light microscopy, there is significant overlap in the distributions of NCX1, SERCA2, and caveolin-1 but the three proteins are n...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276517</comments>
            <pubDate>Sun, 14 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276517</guid>        </item>
        <item>
            <title>Mechanism for the regulation of mammalian cGMP phosphodiesterase6. 1: Identification of its inhibitory subunit complexes and their roles.</title>
            <link>http://www.medworm.com/index.php?rid=3267647&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20151179%26dopt%3DAbstract</link>
            <description>Authors: Yamazaki A, Bondarenko VA, Matsuura I, Tatsumi M, Kurono S, Komori N, Matsumoto H, Hayashi F, Yamazaki RK, Usukura J
    Cyclic GMP phosphodiesterase (PDE) in bovine rod photoreceptor outer segments (OS) comprises a catalytic subunit complex (Palphabeta) and two inhibitory subunits (Pgamma) and is regulated by the alpha subunit of transducin (Talpha). Here, we show an overall mechanism for PDE regulation by identifying Pgamma complexes in OS homogenates prepared with an isotonic buffer. Before Talpha activation, three Pgamma complexes exist in the soluble fraction. Complex a, a minor complex, contains Palphabeta, Talpha, and a protein named Pdelta. Complex b, Palphabetagammagamma( b ), has a PDE activity similar to that of membranous Palphabetagammagamma, Palphabetagammagamma( M )...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3267647</comments>
            <pubDate>Fri, 12 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3267647</guid>        </item>
        <item>
            <title>Fasting promotes the expression of SIRT1, an NAD(+)-dependent protein deacetylase, via activation of PPARalpha in mice.</title>
            <link>http://www.medworm.com/index.php?rid=3267651&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20148352%26dopt%3DAbstract</link>
            <description>In this study, we investigated how SIRT1 and PPARalpha correlate in the fasting-induced anti-aging pathways. A 24-h fasting in mice increased mRNA and protein expression of both SIRT1 and PPARalpha in the livers, where the NAD(+) levels increased with increasing nicotinamide phosphoribosyltransferase (NAMPT) activity in the NAD(+) salvage pathway. Treatment of Hepa1-6 cells in a low glucose medium conditions with NAD(+) or NADH showed that the mRNA expression of both SIRT1 and PPARalpha can be enhanced by addition of NAD(+), and decreased by increasing NADH levels. The cell experiments using SIRT1 antagonists and a PPARalpha agonist suggested that PPARalpha is a key molecule located upstream from SIRT1, and has a role in regulating SIRT1 gene expression in fasting-induced anti-aging pathwa...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3267651</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3267651</guid>        </item>
        <item>
            <title>Irradiation with heavy-ion particles changes the cellular distribution of human histone acetyltransferase HAT1.</title>
            <link>http://www.medworm.com/index.php?rid=3267650&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20148353%26dopt%3DAbstract</link>
            <description>In this report, it is shown for the first time that human Hat1 has two isoforms. Isoform a has 418 amino acids (aa) and is localized exclusively in the nuclear matrix of normal human keratinocytes (NHKs). Isoform b has 334 aa and is located in the cytoplasm, the nucleoplasm, attached to the chromatin and to the nuclear matrix. Immunohistochemical analyses revealed that the bulk of Hat1 is confined to the nucleus, with much lesser amounts in the cytoplasm. Cells undergoing mitotic division have an elevated amount of Hat1 compared to those that are non-mitotic. Senescent cells, however, exhibit a higher concentration of Hat1 in the cytoplasm compare to proliferating cells and the amount of Hat1 in the nucleus decreases with the progression of senescence. NHKs exposed to hydrogen peroxide (H(...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3267650</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3267650</guid>        </item>
        <item>
            <title>Suppression of the androgen receptor function by quercetin through protein-protein interactions of Sp1, c-Jun, and the androgen receptor in human prostate cancer cells.</title>
            <link>http://www.medworm.com/index.php?rid=3267649&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20148354%26dopt%3DAbstract</link>
            <description>Authors: Yuan H, Young CY, Tian Y, Liu Z, Zhang M, Lou H
    We have previously reported that the increase in c-Jun expression induced by quercetin inhibited androgen receptor (AR) transactivation, and Sp1 was involved in quercetin-mediated downregulation of AR activity. Transient transfection assays in this work revealed that co-expression of c-Jun quenched Sp1-induced production of luciferase activity driven by AR promoter or three copies of Sp1 binding elements in the AR promoter. Moreover, c-Jun repressed AR-mediated luciferase activity via androgen-response elements (AREs) of the hK2 gene, while this suppression could be restored partially by cotransfection of Sp1 expression plasmid. The physical associations of c-Jun, Sp1, and AR induced by quercetin were further demonstrated by co-i...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3267649</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3267649</guid>        </item>
        <item>
            <title>Angiostatic effects of K252a, a Trk inhibitor, in murine brain capillary endothelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=3267648&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20148355%26dopt%3DAbstract</link>
            <description>Authors: Lecht S, Arien-Zakay H, Kohan M, Lelkes PI, Lazarovici P
    Nerve growth factor (NGF) supports the survival and differentiation of sympathetic and sensory neurons and is also mitogenic for a variety of tumors. K252a, an antagonist of NGF receptor TrkA, was previously used as a pharmacological tool to study NGF actions and as a lead compound for developing anti-tumor drugs. Since recently, NGF was characterized as an angiogenic factor, we sought to investigate the angiostatic properties of K252a on endothelial cells (ECs). For this purpose, we used a murine brain microcapillary ECs model in which we found autocrine release of NGF in the culture medium and activation of TrkA receptor-induced downstream signaling molecules Erk1/2, Akt, and PLCgamma. In this model, we demonstrated th...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3267648</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3267648</guid>        </item>
        <item>
            <title>Characterization of zebrafish Esrom (Myc-binding protein 2) RCC1-like domain splice variants.</title>
            <link>http://www.medworm.com/index.php?rid=3260901&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20143133%26dopt%3DAbstract</link>
            <description>This study reports the identification and characterization of two novel Esrom splice variants, named splice variants 2 (splicing out 5' 24 bp of exon 17) and 3 (splicing out 5' 24 bp of exons 17 and 18). Polypeptides encoded by 5' 24 bp of exons 17 and 18 are part of basic amino-acid-rich region inside Esrom RCC1-like domain (RLD). These two splice variants maintain the whole protein reading frame and alternative exons usage patterns are conserved with mammal. At different developmental stages and adult zebrafish tissues, abundances of these splice variants are different. Importantly, by yeast two-hybrid screen and confocal colocalization analysis, it was found that alternative splicing of exon 18 regulates Esrom RLD interaction with kinesin family member 22 and G protein beta-subunit 1. T...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3260901</comments>
            <pubDate>Tue, 09 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3260901</guid>        </item>
        <item>
            <title>GST profile expression study in some selected plants: in silico approach.</title>
            <link>http://www.medworm.com/index.php?rid=3248807&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20135200%26dopt%3DAbstract</link>
            <description>This study aims to comprehend the relationship of GST gene family and plant oxidative stress with respect to certain specific conserved motifs, which may help in future studies for screening of biomodulators involved in plant stress metabolism.
    PMID: 20135200 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3248807</comments>
            <pubDate>Fri, 05 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3248807</guid>        </item>
        <item>
            <title>Effects of phenylalanine on the survival and neurite outgrowth of rat cortical neurons in primary cultures: possible involvement of brain-derived neurotrophic factor.</title>
            <link>http://www.medworm.com/index.php?rid=3211185&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20101519%26dopt%3DAbstract</link>
            <description>In this study, using a model system in which cultured cortical neurons were induced with Phe, we observed that Phe inhibited the longest neurite outgrowth and induced the neuronal death. We further demonstrated that the expression of BDNF mRNA and protein was significantly decreased by Phe, together with a decrease in extracellular signal-regulated kinase (ERK) and Akt phosphorylation activity. There was no change in expression of TrkB mRNA and protein. Considering the important role of BDNF in normal brain development and function, these L: -Phe-induced changes in BDNF in PKU brain may be a critical element of the neurological symptoms of PKU.
    PMID: 20101519 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3211185</comments>
            <pubDate>Wed, 27 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3211185</guid>        </item>
        <item>
            <title>ErbB4 signals Neuregulin1-stimulated cell proliferation and c-fos gene expression through phosphorylation of serum response factor by mitogen-activated protein kinase cascade.</title>
            <link>http://www.medworm.com/index.php?rid=3169677&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20066477%26dopt%3DAbstract</link>
            <description>Authors: Eto K, Hommyo A, Yonemitsu R, Abe SI
    The ErbB family of tyrosine kinase receptors mediates a variety of cellular responses to Neuregulin (NRG) 1; however, the intracellular signaling pathways downstream of ErbB4 and their functional outcomes remained to be elucidated. Here we show that NRG1 stimulated the proliferation of human HeLa cells expressing ErbB4, where the phosphorylation relay of extracellular signal-regulated kinase, a mitogen-activated protein kinase (MAPK), and serum response factor (SRF), a transcription factor, was induced, and the c-fos transcription was activated. By contrast, these all were attenuated in cells transfected with an ErbB4 mutant substituting the green fluorescence protein for the intracellular domain. We also demonstrated that a MAPK kinase inh...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3169677</comments>
            <pubDate>Tue, 12 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3169677</guid>        </item>
        <item>
            <title>Co-culture with cardiomyocytes enhanced the myogenic conversion of mesenchymal stromal cells in a dose-dependent manner.</title>
            <link>http://www.medworm.com/index.php?rid=3164015&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20063193%26dopt%3DAbstract</link>
            <description>Authors: He XQ, Chen MS, Li SH, Liu SM, Zhong Y, McDonald Kinkaid HY, Lu WY, Weisel RD, Li RK
    To increase the accessibility of myogenic cells for cell therapy in the infarcted heart, we identified conditions to improve the reproducible conversion of bone marrow mesenchymal stromal cells (BMSCs) into myogenic cells. Such cells may permit functional regeneration following a myocardial infarction. BMSCs derived from green fluorescent protein (GFP) transgenic rats were co-cultured with neonatal rat cardiomyocytes (1:1, 1:10, 1:20, and 1:40 ratios) for 7 days. Some BMSCs contracted synchronously with the neonatal cardiomyocytes, and exhibited action potentials that were confirmed with current clamp recordings. The myogenic phenotype of the BMSCs was confirmed by immunohistochemical staining...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164015</comments>
            <pubDate>Sun, 10 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164015</guid>        </item>
        <item>
            <title>Blockage of ceramide metabolism exacerbates palmitate inhibition of pro-insulin gene expression in pancreatic beta-cells.</title>
            <link>http://www.medworm.com/index.php?rid=3164016&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20063116%26dopt%3DAbstract</link>
            <description>This study was aimed at investigating whether this effect was exacerbated by the inhibition of ceramide degradation in pancreatic beta-cells and the molecular mechanism of intracellular ceramide-induced inhibition of proinsulin gene transcription in response to exposure to palmitate. We exposed insulin-secreting (INS-1) cells treated with low levels of palmitate to the ceramidase inhibitor n-oleoylethanolamine (NOE); this led to the generation of high levels of intracellular ceramide. We observed that the effects of ceramide accumulation in INS-1 cells were similar to the effects of the inhibition of this protein on proinsulin mRNA levels that are caused by the negative regulation of insulin promoter activity. In addition, we observed that ceramide accumulation induced by NOE leads to a si...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164016</comments>
            <pubDate>Sat, 09 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164016</guid>        </item>
        <item>
            <title>Protein domains, catalytic activity, and subcellular distribution of mouse NTE-related esterase.</title>
            <link>http://www.medworm.com/index.php?rid=3157778&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20058052%26dopt%3DAbstract</link>
            <description>Authors: Chang PA, Wang ZX, Long DX, Qin WZ, Wu YJ
    A mammalian family of lipid hydrolases, designated &quot;patatin-like phospholipase domain containing (PNPLA)&quot; recently has attracted attention. NTE-related esterase (NRE) as a member of PNPLA is an insulin-regulated lysophospholipase with homology to neuropathy target esterase (NTE). Mouse NRE (mNRE) has a predicted amino-terminal transmembrane region (TM), a putative regulatory (R) domain, and a hydrophobic catalytic (C) domain. In the current study, we described the expression of green fluorescent protein (GFP)-tagged constructs of mNRE and mutant proteins lacking the specific protein domains. Esterase assays indicated that neither the TM nor R-domain was essential for mNRE esterase activity, but the TM significantly contributed to its a...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157778</comments>
            <pubDate>Fri, 08 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3157778</guid>        </item>
        <item>
            <title>Persistent facial pain increases superoxide anion production in the spinal trigeminal nucleus.</title>
            <link>http://www.medworm.com/index.php?rid=3157777&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20058053%26dopt%3DAbstract</link>
            <description>This study demonstrated that there is an increased production of O(2) (-) in the second phase but not in the first phase of the formalin test; thus O(2) (-) is involved in pain induced by inflammation, but not in acute pain.
    PMID: 20058053 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157777</comments>
            <pubDate>Fri, 08 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3157777</guid>        </item>
        <item>
            <title>Combination of chemokine and angiogenic factor genes and mesenchymal stem cells could enhance angiogenesis and improve cardiac function after acute myocardial infarction in rats.</title>
            <link>http://www.medworm.com/index.php?rid=3157776&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20058054%26dopt%3DAbstract</link>
            <description>Authors: Tang J, Wang J, Zheng F, Kong X, Guo L, Yang J, Zhang L, Huang Y
    Gene and stem-cell therapies hold promise for the treatment of ischemic cardiovascular disease. Combined stem cell, chemokine, and angiogenic growth factor gene therapy could augment angiogenesis, and better improve heart function in the infarcted myocardium. In order to prove this action, we established the animal model of myocardial infarction (MI) was by occlusion of the left anterior descending artery in rats. Seven days after surgery, 5.0 x 10(6) Ad-EGFP-MSC, 5.0 x 10(6) Ad-SDF-1-MSC, 5.0 x 10(6) Ad-VEGF-MSC, or 5.0 x 10(6) Ad-SDF-VEGF-MSC (Ad-SDF-1-VEGF-MSC) suspension in 0.2 ml of serum-free medium was injected into four sites in the infarcted hearts. Results showed that MSCs transfected with Ad-VEGF and A...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157776</comments>
            <pubDate>Fri, 08 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3157776</guid>        </item>
        <item>
            <title>Changes in E-NTPDase 3 expression and extracellular nucleotide hydrolysis during the myofibroblast/lipocyte differentiation.</title>
            <link>http://www.medworm.com/index.php?rid=3157775&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20058055%26dopt%3DAbstract</link>
            <description>Authors: Andrade CM, Wink MR, Margis R, Borojevic R, Battastini AM, Guma FC
    Hepatic stellate cells (HSC) play a critical role in the development and maintenance of liver fibrosis. HSC are lipocytes that displayed the capacity to develop into myofibroblast-like cells. Ecto-nucleoside triphosphate diphosphohydrolases (E-NTPDases) regulate the concentration of extracellular nucleotides, signaling molecules that play a role in the pathogenesis of hepatic fibrosis. In the present study, we identified and compared the expressions of E-NTPDase family members in two different phenotypes of the mouse hepatic stellate cell line (GRX) and evaluated the nucleotide hydrolysis by these cells. We show that both phenotypes of GRX cell line expressed NTPDase 3 and 5. However, only activated cells expre...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157775</comments>
            <pubDate>Fri, 08 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3157775</guid>        </item>
        <item>
            <title>Aggregation of spectrin and PKCtheta is an early hallmark of fludarabine/mitoxantrone/dexamethasone-induced apoptosis in Jurkat T and HL60 cells.</title>
            <link>http://www.medworm.com/index.php?rid=3157774&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20058056%26dopt%3DAbstract</link>
            <description>Authors: Dubielecka PM, Grzybek M, Kolondra A, Ja&amp;#x17A;wiec B, Draga A, Aleksandrowicz P, Ko&amp;#x142;odziejczyk M, Serwotka A, Doli&amp;#x144;ska-Krajewska B, Warcho&amp;#x142; J, Kuliczkowski K, Sikorski AF
    It has been shown that changes in spectrin distribution in early apoptosis preceded changes in membrane asymmetry and phosphatidylserine (PS) exposure. PKCtheta was associated with spectrin during these changes, suggesting a possible role of spectrin/PKCtheta aggregation in regulation of early apoptotic events. Here we dissect this hypothesis using Jurkat T and HL60 cell lines as model systems. Immunofluorescent analysis of alphaIIbetaII spectrin arrangement in Jurkat T and HL60 cell lines revealed the redistribution of spectrin and PKCtheta into a polar aggregate in early apoptosis induced...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157774</comments>
            <pubDate>Fri, 08 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3157774</guid>        </item>
        <item>
            <title>Regulating A549 cells growth by ASO inhibiting miRNA expression.</title>
            <link>http://www.medworm.com/index.php?rid=3146642&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20049626%26dopt%3DAbstract</link>
            <description>In conclusion, ASO (specific to oncogenic miRNAs) could induce A549 cells apoptosis by inhibiting oncogenic miRNAs, and could increase chemotherapy sensitivity of A549 cells to anti-cancer drug, which holds great promise to lung cancer therapy.
    PMID: 20049626 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3146642</comments>
            <pubDate>Tue, 05 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3146642</guid>        </item>
        <item>
            <title>Biochemical characterization of soluble nucleotide pyrophosphatase/phosphodiesterase activity in rat serum.</title>
            <link>http://www.medworm.com/index.php?rid=3146641&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20049627%26dopt%3DAbstract</link>
            <description>Authors: Laketa D, Bjelobaba I, Savic J, Lavrnja I, Stojiljkovic M, Rakic L, Nedeljkovic N
    Biochemical properties of nucleotide pyrophosphatase/phosphodiesterase (NPP) in rat serum have been described by assessing its nucleotide phosphodiesterase activity, using p-nitrophenyl-5'-thymidine monophosphate (p-Nph-5'-TMP) as a substrate. It was demonstrated that NPP activity shares some typical characteristics described for other soluble NPP, such as divalent cation dependence, strong alkaline pH optimum (pH 10.5), inhibition by glycosaminoglycans, and K (m) for p-Nph-5'-TMP hydrolysis of 61.8 +/- 5.2 muM. In order to characterize the relation between phosphodiesterase and pyrophosphatase activities of NPP, we have analyzed the effects of different natural nucleotides and nucleotide analogs...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3146641</comments>
            <pubDate>Tue, 05 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3146641</guid>        </item>
        <item>
            <title>Time-dependent alterations of cerebral proteins following short-term normobaric hyperoxia.</title>
            <link>http://www.medworm.com/index.php?rid=3146640&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20049628%26dopt%3DAbstract</link>
            <description>Authors: Hinkelbein J, Feldmann RE, Kalenka A
    Sufficient oxygenation is indispensable for cognitive performance in mammals. In order to assure adequate oxygenation and to prevent hypoxia in medicine or aviation, different approaches of oxygen delivery are realized. With regard to hyperoxia, it is well known that it increases the risk of tissue toxicity and inflammation by generating radical oxygen species. However, this impact of hyperoxia on the expression of specific brain proteins has not been evaluated in detail yet. The present study analyzes time-dependent changes in protein expression in rat brain after a short-term exposure to normobaric hyperoxia. Thirty-six Wistar rats were randomly assigned to six different groups, three normobaric hyperoxia (NH) groups or three normobaric n...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3146640</comments>
            <pubDate>Tue, 05 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3146640</guid>        </item>
        <item>
            <title>Analysis of GSTM1 and GSTT1 polymorphisms in circulating plasma DNA of lung cancer patients.</title>
            <link>http://www.medworm.com/index.php?rid=3146639&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20049629%26dopt%3DAbstract</link>
            <description>Authors: Cabral RE, Caldeira-de-Araujo A, Cabral-Neto JB, Costa Carvalho MD
    The concentration of free circulating plasma DNA and the genetic profile of patients suffering from various types of tumors were studied in an effort to increase the understanding of the biomarkers and genetic factors involved in predisposing an individual to lung cancer (LC). The polymorphic inheritance of glutathione S-transferases (GST), which modulate the effects of various genotoxic agents, especially those derived from benzo[a]pyrene, one of the main tobacco carcinogens, has been implicated in both cancer risk and prognostics. We investigated gene polymorphisms in the blood serum of patients previously diagnosed at the Pneumology Division of the Clementino Fraga Filho University Hospital of the Federal Un...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3146639</comments>
            <pubDate>Tue, 05 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3146639</guid>        </item>
        <item>
            <title>Carnosine supplementation protects rat brain tissue against ethanol-induced oxidative stress.</title>
            <link>http://www.medworm.com/index.php?rid=3146646&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20047045%26dopt%3DAbstract</link>
            <description>Authors: Ozel Turkcu U, Bilgihan A, Biberoglu G, Mertoglu Caglar O
    Ethanol causes oxidative stress and tissue damage. The aim of this study was to investigate the effect of antioxidant carnosine on the oxidative stress induced by ethanol in the rat brain tissue. Forty male rats were divided equally into four groups as control, carnosine (CAR), ethanol (EtOH), and ethanol plus carnosine (EtOH + CAR). Rats in the control group (n = 10) were injected intraperitoneally (i.p.) with 0.9% saline; EtOH group (n = 10) with 2 g/kg/day ethanol, CAR group (n = 10) received carnosine at a dose of 1 mg/kg/day and EtOH + CAR group (n = 10) received carnosine (orally) and ethanol (i.p.). All animals were sacrificed using ketamine and brain tissues were removed. Malondialdehyde (MDA), protein carbonyl ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3146646</comments>
            <pubDate>Sun, 03 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3146646</guid>        </item>
        <item>
            <title>Exogenously expressed human Ku70 stabilizes Ku80 in Xenopus oocytes and induces heterologous DNA-PK catalytic activity.</title>
            <link>http://www.medworm.com/index.php?rid=3146645&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20047046%26dopt%3DAbstract</link>
            <description>In this study, the two polypeptides (Ku80/Ku70) of the human Ku were expressed in Xenopus oocytes in order to investigate their over-expression, sub-cellular localization, and functional interaction with the Xenopus DNA-PK(cs). In vitro-transcribed mRNAs for Ku70 and Ku80 were obtained from the respective plasmid constructs. The exogenously expressed proteins from the injected mRNAs were immunoprecipitated using a specific anti-T7 Tag antibody. The T7 Tag epitope is present in the vector at the amino-terminus and is in-frame with the Ku cDNA sequences. While injected Ku70 mRNA translated to a full-length Ku70 polypeptide that translocated to the nucleus, injected Ku80 mRNA resulted in the expression of a truncated product that was retained in the cytoplasm. Although Ku80 mRNA was stable fo...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3146645</comments>
            <pubDate>Sun, 03 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3146645</guid>        </item>
        <item>
            <title>Ghrelin and obestatin expression in oral squamous cell carcinoma: an immunohistochemical and biochemical study.</title>
            <link>http://www.medworm.com/index.php?rid=3146644&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20047070%26dopt%3DAbstract</link>
            <description>Authors: Alnema MM, Aydin S, Ozkan Y, Dagli AF, Ozercan HI, Yildirim N, Sahin I, Karaoglu A, Kilic N, Yilmaz M, Ozercan MR, Donder E
    The underlying molecular mechanism of carcinogenesis in oral squamous cell carcinoma (OSCC) is poorly understood and appears to be controlled on many genetic, environmental, and hormonal factors. Obestatin and ghrelin, two recently discovered hormones, are co-expressed in endocrine cells. The purpose of this investigation was to examine the immunohistochemical features of OSCCs in relation to the tissue concentration of ghrelin and obestatin. The association between OSCC and Epstein Barr Virus (EBV) status was also explored. The expression of ghrelin and obestatin was examined by immunohistochemistry and immunoassay in oral biopsy specimens: 10 benign squ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3146644</comments>
            <pubDate>Sun, 03 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3146644</guid>        </item>
        <item>
            <title>Alterations in erythrocyte membrane fluidity and Na(+)/K (+)-ATPase activity in chronic alcoholics.</title>
            <link>http://www.medworm.com/index.php?rid=3146643&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20047071%26dopt%3DAbstract</link>
            <description>Authors: Maturu P, Vaddi DR, Pannuru P, Nallanchakravarthula V
    Ethanol disorders biological membranes causing perturbations in the bilayer and also by altering the physicochemical properties of membrane lipids. But, chronic alcohol consumption also increases nitric oxide (NO) production. There was no systemic study was done related to alcohol-induced production of NO and consequent formation of peroxynitrite mediated changes in biophysical and biochemical properties, structure, composition, integrity and function of erythrocyte membranes in chronic alcoholics. Hence, keeping all these conditions in mind the present study was undertaken to investigate the role of over produced nitric oxide on red cell membrane physicochemical properties in chronic alcoholics. Human male volunteers aged ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3146643</comments>
            <pubDate>Sun, 03 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3146643</guid>        </item>
        <item>
            <title>Overexpression of Trpp5 contributes to cell proliferation and apoptosis probably through involving calcium homeostasis.</title>
            <link>http://www.medworm.com/index.php?rid=3134878&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20043191%26dopt%3DAbstract</link>
            <description>Authors: Xiao Y, Lv X, Cao G, Bian G, Duan J, Ai J, Sun H, Li Q, Yang Q, Chen T, Zhao D, Tan R, Liu Y, Wang Y, Zhang Z, Yang Y, Wei Y, Zhou Q
    Trpp5 is one member of the polycystic kidney disease (PKD) family, which belongs to transient receptor potential (TRP) superfamily. Our previous study has shown that Trpp5 is developmentally expressed in mouse testis and overexpression of Trpp5 increases intracellular free calcium concentration in MDCK cells. However, the roles of this protein in cellular processes are largely unknown. Here, we demonstrated that Trpp5 resided in both cytoplasm and cell membrane of HEK293 cells. We found that overexpression of Trpp5 slightly increased the calcium current amplitude of HEK293 cells and shifted the reversal potential to a more negative value. Meanwhi...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3134878</comments>
            <pubDate>Thu, 31 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3134878</guid>        </item>
        <item>
            <title>Involvement of the residues of GSKIP, AxinGID, and FRATtide in their binding with GSK3beta to unravel a novel C-terminal scaffold-binding region.</title>
            <link>http://www.medworm.com/index.php?rid=3134877&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20043192%26dopt%3DAbstract</link>
            <description>Authors: Howng SL, Hwang CC, Hsu CY, Hsu MY, Teng CY, Chou CH, Lee MF, Wu CH, Chiou SJ, Lieu AS, Loh JK, Yang CN, Lin CS, Hong YR
    The specificity and regulation of GSK3beta are thought to involve in the docking interactions at core kinase domain because of the particular amino acid residues. Recent X-ray diffraction studies illuminated the relative binding residues on AxinGID and FRATtide for GSK3beta docking and appeared that GSK3beta Val267Gly (V267G) and Tyr288Phe (Y288F) could distinguish the direct interaction between AxinGID and FRATtide. In order to explore the mode that involved the binding of GSKIP to GSK3beta and compare it with that of AxinGID and FRATtide, we pinpointed the binding sites of GSKIP to GSK3beta through the single-point mutation of four corresponding sites with...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3134877</comments>
            <pubDate>Thu, 31 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3134877</guid>        </item>
        <item>
            <title>Propofol protects against hydrogen peroxide-induced oxidative stress and cell dysfunction in human umbilical vein endothelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=3129866&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20039104%26dopt%3DAbstract</link>
            <description>In this study, we studied hydrogen peroxide (H(2)O(2))-induced oxidative stress and cell dysfunction in human umbilical vein endothelial cells (HUVECs) and especially, their modulation by propofol. HUVECs were treated with different concentrations (0.1 and 0.5 mM) of H(2)O(2) for different times (1, 3, and 6 h). Then HUVECs were pretreated with different concentrations of propofol (10, 25, and 50 muM), followed by H(2)O(2) treatment (0.5 mM, 3 h). In another set of experiments, we pretreated cells with p38 mitogen-activated protein kinase (p38 MAPK) inhibitor SB203580, followed by H(2)O(2) treatment (0.5 mM, 3 h). After treatment, oxidative stress, p38 MAPK phosphorylation, transcription factor NF-kappaB activation, nitric oxide synthase (NOS) expression, nitric oxide (NO) production, and ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3129866</comments>
            <pubDate>Tue, 29 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3129866</guid>        </item>
        <item>
            <title>Role of nutritional zinc in the prevention of osteoporosis.</title>
            <link>http://www.medworm.com/index.php?rid=3122507&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20035439%26dopt%3DAbstract</link>
            <description>Authors: Yamaguchi M
    Zinc is known as an essential nutritional factor in the growth of the human and animals. Bone growth retardation is a common finding in various conditions associated with dietary zinc deficiency. Bone zinc content has been shown to decrease in aging, skeletal unloading, and postmenopausal conditions, suggesting its role in bone disorder. Zinc has been demonstrated to have a stimulatory effect on osteoblastic bone formation and mineralization; the metal directly activates aminoacyl-tRNA synthetase, a rate-limiting enzyme at translational process of protein synthesis, in the cells, and it stimulates cellular protein synthesis. Zinc has been shown to stimulate gene expression of the transcription factors runt-related transcription factor 2 (Runx2) that is related to d...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3122507</comments>
            <pubDate>Fri, 25 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3122507</guid>        </item>
        <item>
            <title>Suppression of tumor suppressor Tsc2 and DNA repair glycosylase Nth1 during spontaneous liver tumorigenesis in Long-Evans Cinnamon rats.</title>
            <link>http://www.medworm.com/index.php?rid=3122509&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20033472%26dopt%3DAbstract</link>
            <description>In this study, we examined the expression of Nth1 and Tsc2 genes during disease progression in the LEC rat liver. During the period of acute hepatitis (16-17 weeks), we observed decreased Nth1 and Tsc2 mRNA levels and a continued decrease of the Tsc2 gene in 24 weeks in LEC rats, while the effect was minimal in Long-Evans Agouti (LEA) rats. This reduction in the mRNA levels was due to the reduced binding of EBSs in the Nth1/Tsc2 promoter. Increase in protein oxidation (carbonyl content) during the same time period (16-24 weeks) may have an effect on the promoter binding of regulatory proteins and consequent decrease in Nth1 and Tsc2 gene expressions during tumorigenesis.
    PMID: 20033472 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3122509</comments>
            <pubDate>Thu, 24 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3122509</guid>        </item>
        <item>
            <title>Cartilage oligomeric matrix protein promotes cell attachment via two independent mechanisms involving CD47 and alphaVbeta3 integrin.</title>
            <link>http://www.medworm.com/index.php?rid=3122508&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20033473%26dopt%3DAbstract</link>
            <description>In this study, the role of COMP in ligament was investigated with a series of cell attachment assays using ligament cells binding to COMP. A dose-dependent cell attachment activity was found, which was inhibited by a peptide containing the SFYVVMWK amino acid sequence derived from the globular C-terminal domain of COMP. This activity was independent of the recently described RGD-dependent attachment activity. Function-blocking antibodies to CD47 and alphaVbeta3 integrin reduced cell attachment to COMP, implicating the participation of these cell surface molecules in COMP cell binding. Immunofluorescence studies showed that cell attachment to COMP induced the formation of lamellae containing F-actin microspikes associated with fascin. We propose that COMP promotes cell attachment via two in...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3122508</comments>
            <pubDate>Thu, 24 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3122508</guid>        </item>
        <item>
            <title>Acute and/or chronic stress models modulate CuZnSOD and MnSOD protein expression in rat liver.</title>
            <link>http://www.medworm.com/index.php?rid=3104436&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20020182%26dopt%3DAbstract</link>
            <description>In this study, the protein levels of copper-zinc SOD (CuZnSOD) in the cytosolic and nuclear fraction, manganese SOD (MnSOD) in the mitochondrial, and cytosolic fraction and cytochrome c (cyt c) in the liver of male rats exposed to 2 h of acute immobilization (IM) or Cold stress, 21 days chronic isolation or their combinations (chronic/acute stress) were examined. The serum corticosterone (CORT) level was measured, as an indicator of stress stimuli. Both acute stressors with elevated CORT levels caused a decrease of mitochondrial MnSOD, while acute IM resulted in redistribution of the CuZnSOD protein level between the cytosolic and nuclear fraction. Chronic isolation, during which the CORT level was close to control value, resulted in an increase of cytosolic CuZnSOD, whereas a decrease of ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3104436</comments>
            <pubDate>Sat, 19 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3104436</guid>        </item>
        <item>
            <title>Selenium restores defective beta-adrenergic receptor response of thoracic aorta in diabetic rats.</title>
            <link>http://www.medworm.com/index.php?rid=3104441&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20016929%26dopt%3DAbstract</link>
            <description>Authors: Zeydanli EN, Bilginoglu A, Tanriverdi E, Gurdal H, Turan B
    Increased oxidative stress is one of the basic contributors to the development of the cardiovascular complications in diabetes. Both endothelial and vascular smooth muscle cell dysfunctions are the main sign involved in the pathogenesis of diabetic cardiovascular dysfunction. Matrix metalloproteinases (MMPs) are expressed in the vasculature, and participate in tissue remodeling under pathological conditions such as increased oxidative stress, whereas little is known about effect of hyperglycemia on regulation of MMPs in vascular system. Therefore, we aimed to evaluate the effect of an antioxidant, sodium selenate treatment (0.3 mg/kg for 4 weeks) on function of streptozotocin-diabetic rat aorta. Sodium selenate treatme...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3104441</comments>
            <pubDate>Fri, 18 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3104441</guid>        </item>
        <item>
            <title>Casein kinase 2 inhibition differentially modulates apoptotic effect of trichostatin A against epithelial ovarian carcinoma cell lines.</title>
            <link>http://www.medworm.com/index.php?rid=3104433&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20020183%26dopt%3DAbstract</link>
            <description>Authors: Lee CS, Jang ER, Kim YJ, Myung SC, Kim W
    Histone deacetylase inhibitors and casein kinase 2 inhibitors have been shown to induce apoptosis. However, the combined effect of casein kinase 2 inhibition on the apoptotic effect of histone deacetylase inhibitor is unknown. We assessed the effect of casein kinase 2 inhibition on the apoptotic effect of trichostatin A in human epithelial carcinoma cell lines with respect to cell death signaling pathways. At concentrations that did not induce cell death, the casein kinase 2 inhibitor 4,5,6,7-tetrabromobenzotriazole inhibited activation of apoptotic proteins and changes in mitochondrial membrane permeability induced by the histone deacetylase inhibitor trichostatin A. These results suggest that casein kinase 2 inhibition may reduce tric...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3104433</comments>
            <pubDate>Fri, 18 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3104433</guid>        </item>
        <item>
            <title>Sequence and expression of 11beta-hydroxysteroid dehydrogenase type 1 cDNA cloned from pig testis.</title>
            <link>http://www.medworm.com/index.php?rid=3104432&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20020184%26dopt%3DAbstract</link>
            <description>Authors: Ohno S, Ohta M, Honda Y, Nakajin S
    Pig 11beta-hydroxysteroid dehydrogenase (11beta-HSD) type 1 cDNA was cloned from neonatal pig testis, and 15 nucleotides were found to differ from the sequence in GenBank (Accession No. NM_214248). It was an exclusive clone obtained as pig 11beta-HSD type 1, and the sequence of 11beta-HSD type 1 cDNA cloned from pig liver was identical to that from testis. Amino acid sequence, deduced from cloned cDNA, also had a conserved triad of catalytically important Ser, Tyr and Lys residues for the short-chain dehydrogenase/reductase family, a membrane-spanning domain consisting of hydrophobic amino acid and a glycine motif in the cofactor binding region. The protein translated from this clone on expression in mammalian HEK293 cells exhibited oxo-reduc...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3104432</comments>
            <pubDate>Fri, 18 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3104432</guid>        </item>
        <item>
            <title>Evaluation of cell viability, DNA damage, and cell death in normal human dermal fibroblast cells induced by functionalized multiwalled carbon nanotube.</title>
            <link>http://www.medworm.com/index.php?rid=3104444&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20016928%26dopt%3DAbstract</link>
            <description>Authors: Patlolla A, Patlolla B, Tchounwou P
    Multiwalled carbon nanotubes (MWCNTs) are an example of a carbon-based nanomaterial that has won enormous popularity in nanotechnology. Due to their unusual one-dimensional hollow nanostructure and unique physicochemical properties, they are highly desirable for use within the commercial, environmental, and medical sectors. Despite their wide application, there is a lack of information concerning their impact on human health and the environment. While nanotechnology looms large with commercial promise and potential benefit, an equally large issue is the evaluation of potential effects on humans and other biological systems. Our research is focused on cellular response to purified functionalized MWCNT in normal human dermal fibroblast cells. ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3104444</comments>
            <pubDate>Thu, 17 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3104444</guid>        </item>
        <item>
            <title>Genetic polymorphisms of DNA repair gene XRCC1 and risk of uterine leiomyoma.</title>
            <link>http://www.medworm.com/index.php?rid=3104445&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20013148%26dopt%3DAbstract</link>
            <description>In conclusion, the results suggest that polymorphism of XRCC1 Arg280His was associated with the increased risk of uterine leiomyoma in a Chinese population.
    PMID: 20013148 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3104445</comments>
            <pubDate>Tue, 15 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3104445</guid>        </item>
        <item>
            <title>Intraocular penetration of pyruvate following its topical administration in mice.</title>
            <link>http://www.medworm.com/index.php?rid=3104449&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20012886%26dopt%3DAbstract</link>
            <description>Authors: Hegde KR, Kovtun S, Varma SD
    Previous studies from our laboratory have demonstrated that pyruvate, an endogenous alpha-keto acid metabolite, has a protective effect against oxidative stress induced damage to the ocular tissues including the lens, in which in addition to exerting its protective effect against tissue damage caused by oxyradicals generated under organ culture, it is also found effective in preventing actual cataract formation in vivo in animal models undergoing direct oxidative stress as well as in diabetes. In the latter studies, pyruvate was administered mixed with diet and drinking water. However, with the view of the desirability of treating eye diseases by topical administration of the pharmacological agents, the present studies were conducted to determine t...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3104449</comments>
            <pubDate>Sun, 13 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3104449</guid>        </item>
        <item>
            <title>Antitumor and antioxidant role of Chrysaora quinquecirrha (sea nettle) nematocyst venom peptide against ehrlich ascites carcinoma in Swiss Albino mice.</title>
            <link>http://www.medworm.com/index.php?rid=3104457&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20012161%26dopt%3DAbstract</link>
            <description>Authors: Balamurugan E, Reddy BV, Menon VP
    This investigation aims to evaluate the antitumor and antioxidant potential of Chrysaora quinquecirrha (sea nettle) nematocyst venom on Ehrlich ascites carcinoma (EAC) tumor model. Tumor was induced in mice by intraperitoneal injection of EAC cells. The antitumor effect of sea nettle nematocyst venom (SNV) peptide was evaluated by assessing in vitro cytotoxicity, survival time, hematological, and antioxidant parameters. Intraperitoneal injection of SNV peptide increased the survival time of the EAC-bearing mice. The SNV peptide brought back the altered levels of the hematological and antioxidant parameters in a dose dependent manner in EAC-bearing mice. The results were comparable to that of the result obtained from the animals treated with th...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3104457</comments>
            <pubDate>Fri, 11 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3104457</guid>        </item>
        <item>
            <title>Long-term metabolic effects of different doses of niacin-bound chromium on Sprague-Dawley rats.</title>
            <link>http://www.medworm.com/index.php?rid=3104454&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20012467%26dopt%3DAbstract</link>
            <description>We examined blood pressure, the renin-angiotensin system (RAS), nitric oxide (NO), and insulin systems and inflammatory parameters. Results in male and female SD rats were comparable. NBC lowered systolic blood pressure (SBP) in a dose-dependent fashion; however, after 200 days, the SBP of the low dose group (1X) began to rise and returned to baseline control. After raising the dose of NBC to 3X, the SBP in the 1X group decreased significantly once more. When half the test rats (3X and 10X) were deprived of NBC, SBP rose gradually to control levels after 2 to 3 months. However, the SBP decreased significantly once more when each satellite group returned to the 3X dose. Special testing suggests that NBC at adequate dosing increases insulin sensitivity, lowers HbA1C, decreases activity of th...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3104454</comments>
            <pubDate>Fri, 11 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3104454</guid>        </item>
        <item>
            <title>Preface.</title>
            <link>http://www.medworm.com/index.php?rid=3104453&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20012468%26dopt%3DAbstract</link>
            <description>Authors: Sharma RK, Duda T
    
    PMID: 20012468 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3104453</comments>
            <pubDate>Fri, 11 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3104453</guid>        </item>
        <item>
            <title>New insight into the functioning of nitric oxide-receptive guanylyl cyclase: physiological and pharmacological implications.</title>
            <link>http://www.medworm.com/index.php?rid=3104452&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20012469%26dopt%3DAbstract</link>
            <description>Authors: Garthwaite J
    The cellular counterpart of the &quot;soluble&quot; guanylyl cyclase found in tissue homogenates over 30 years ago is now recognized as the physiological receptor for nitric oxide (NO). The ligand-binding site is a prosthetic haem group that, when occupied by NO, induces a conformational change in the protein that propagates to the catalytic site, triggering conversion of GTP into cGMP. This review focuses on recent research that takes this basic information forward to the beginnings of a quantitative depiction of NO signal transduction, analogous to that achieved for other major transmitters. At its foundation is an explicit enzyme-linked receptor mechanism for NO-activated guanylyl cyclase that replicates all its main properties. In cells, NO signal transduction is subjec...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3104452</comments>
            <pubDate>Fri, 11 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3104452</guid>        </item>
        <item>
            <title>FOXO transcription factors and VEGF neutralizing antibody enhance antiangiogenic effects of resveratrol.</title>
            <link>http://www.medworm.com/index.php?rid=3104450&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20012470%26dopt%3DAbstract</link>
            <description>In conclusion, regulation of FOXO transcription factors by resveratrol may play an important role in angiogenesis which is critical for cancer, diabetic retinopathy, rheumatoid arthritis, psoriasis, and cardiovascular disorders.
    PMID: 20012470 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3104450</comments>
            <pubDate>Fri, 11 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3104450</guid>        </item>
        <item>
            <title>Novel functions of photoreceptor guanylate cyclases revealed by targeted deletion.</title>
            <link>http://www.medworm.com/index.php?rid=3104455&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20012162%26dopt%3DAbstract</link>
            <description>Authors: Karan S, Frederick JM, Baehr W
    Targeted deletion of membrane guanylate cyclases (GCs) has yielded new information concerning their function. Here, we summarize briefly recent results of laboratory generated non-photoreceptor GC knockouts characterized by complex phenotypes affecting the vasculature, heart, brain, kidney, and other tissues. The main emphasis of the review, however, addresses the two GCs expressed in retinal photoreceptors, termed GC-E and GC-F. Naturally occurring GC-E (GUCY2D) null alleles in human and chicken are associated with an early onset blinding disorder, termed &quot;Leber congenital amaurosis type 1&quot; (LCA-1), characterized by extinguished scotopic and photopic ERGs, and retina degeneration. In mouse, a GC-E null genotype produces a recessive cone dystroph...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3104455</comments>
            <pubDate>Wed, 09 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3104455</guid>        </item>
        <item>
            <title>Potential role of calcineurin in pathogenic conditions.</title>
            <link>http://www.medworm.com/index.php?rid=3063879&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19967549%26dopt%3DAbstract</link>
            <description>Authors: Kurji K, Sharma RK
    Since its initial discovery as Ca(2+)/calmodulin (CaM)-dependent serine/threonine protein phosphatase, calcineurin (CaN) has been extensively studied in many mammalian tissues. CaN has been shown to be involved in various biological and Ca(2+)-dependent signal transduction pathways. Over the last decade, our laboratory has been interested and has carried out numerous experiments on this specific protein phosphatase. While, a lot of research has been performed studying CaN's involvement in ischemia, the immune system, and various mammalian tissues, not much is known about the potential role of CaN in various eye diseases. This review focuses on the studies that have been carried out in our laboratory on CaN, and specifically CaN's involvement in the eye. We d...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3063879</comments>
            <pubDate>Sat, 05 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3063879</guid>        </item>
        <item>
            <title>High FFA-induced proliferation and apoptosis in human umbilical vein endothelial cell partly through Wnt/beta-catenin signal pathway.</title>
            <link>http://www.medworm.com/index.php?rid=3063878&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19967550%26dopt%3DAbstract</link>
            <description>Authors: Zhu P, Chen G, You T, Yao J, Jiang Q, Lin X, Shen X, Qiao Y, Lin L
    Free fatty acids (FFA)-induced proliferation and apoptosis was studied in human umbilical vein endothelial cells (HUVECs). A recombinant adenovirus containing a RNAi cassette targeting the GSK-3beta gene was produced and its silencing effect on GSK-3beta gene was detected by Western blot analysis and immunohistochemistry assay in HUVECs. The effect of the RNAi on the protein level of beta-catenin was explored by transfecting the RNAi adenovirus to inhibit the expression of GSK-3beta protein. The subsequent effect on the Wnt/GSK-3beta/beta-catenin signal pathway and on proliferation and apoptosis of HUVECs cultured with FFAs, was analyzed by BrdU assay, Annexin V-FITC/PI Apoptosis Detection Kit, and 4',6-diamidi...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3063878</comments>
            <pubDate>Sat, 05 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3063878</guid>        </item>
        <item>
            <title>Receptor guanylyl cyclase C (GC-C): regulation and signal transduction.</title>
            <link>http://www.medworm.com/index.php?rid=3061386&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19960363%26dopt%3DAbstract</link>
            <description>Authors: Basu N, Arshad N, Visweswariah SS
    Receptor guanylyl cyclase C (GC-C) is the target for the gastrointestinal hormones, guanylin, and uroguanylin as well as the bacterial heat-stable enterotoxins. The major site of expression of GC-C is in the gastrointestinal tract, although this receptor and its ligands play a role in ion secretion in other tissues as well. GC-C shares the domain organization seen in other members of the family of receptor guanylyl cyclases, though subtle differences highlight some of the unique features of GC-C. Gene knock outs in mice for GC-C or its ligands do not lead to embryonic lethality, but modulate responses of these mice to stable toxin peptides, dietary intake of salts, and development and differentiation of intestinal cells. It is clear that there...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3061386</comments>
            <pubDate>Fri, 04 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3061386</guid>        </item>
        <item>
            <title>Membrane guanylate cyclase is a beautiful signal transduction machine: overview.</title>
            <link>http://www.medworm.com/index.php?rid=3057049&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19957201%26dopt%3DAbstract</link>
            <description>This article is a sequel to the four earlier comprehensive reviews which covered the field of membrane guanylate cyclase from its origin to the year 2002 (Sharma in Mol Cell Biochem 230:3-30, 2002) and then to the year 2004 (Duda et al. in Peptides 26:969-984, 2005); and of the Ca(2+)-modulated membrane guanylate cyclase to the year 1997 (Pugh et al. in Biosci Rep 17:429-473, 1997) and then to 2004 (Sharma et al. in Curr Top Biochem Res 6:111-144, 2004). This article contains three parts. The first part is &quot;Historical&quot;; it is brief, general, and freely borrowed from the earlier reviews, covering the field from its origin to the year 2004 (Sharma in Mol Cell Biochem, 230:3-30, 2002; Duda et al. in Peptides 26:969-984, 2005). The second part focuses on the &quot;Ca(2+)-modulated ROS-GC membrane g...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3057049</comments>
            <pubDate>Thu, 03 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3057049</guid>        </item>
        <item>
            <title>ROS-GC subfamily membrane guanylate cyclase-linked transduction systems: taste, pineal gland and hippocampus.</title>
            <link>http://www.medworm.com/index.php?rid=3057051&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19953306%26dopt%3DAbstract</link>
            <description>Authors: Sharma RK, Duda T
    In the continuous efforts to test the validity of the theme that the Ca(2+)-modulated ROS-GC subfamily system is a universal transduction component of the sensory and sensory-linked network of neurons, this article focuses on the presence and variant biochemical forms of this transduction system in the gustatory epithelium, the site of gustatory transduction; in the pineal, a light-sensitive gland; and in the hippocampus neurons, linked with the perception of all SENSES.
    PMID: 19953306 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3057051</comments>
            <pubDate>Wed, 02 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3057051</guid>        </item>
        <item>
            <title>Mg(2+)/Ca (2+) cation binding cycle of guanylyl cyclase activating proteins (GCAPs): role in regulation of photoreceptor guanylyl cyclase.</title>
            <link>http://www.medworm.com/index.php?rid=3057050&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19953307%26dopt%3DAbstract</link>
            <description>Authors: Dizhoor AM, Olshevskaya EV, Peshenko IV
    Photon absorption by photoreceptors activates hydrolysis of cGMP, which shuts down cGMP-gated channels and decreases free Ca(2+) concentrations in outer segment. Suppression of Ca(2+) influx through the cGMP channel by light activates retinal guanylyl cyclase through guanylyl cyclase activating proteins (GCAPs) and thus expedites photoreceptors recovery from excitation and restores their light sensitivity. GCAP1 and GCAP2, two ubiquitous among vertebrate species isoforms of GCAPs that activate retGC during rod response to light, are myristoylated Ca(2+)/Mg(2+)-binding proteins of the EF-hand superfamily. They consist of one non-metal binding EF-hand-like domain and three other EF-hands, each capable of binding Ca(2+) and Mg(2+). In the m...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3057050</comments>
            <pubDate>Wed, 02 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3057050</guid>        </item>
        <item>
            <title>High glucose stimulates adipogenic and inhibits osteogenic differentiation in MG-63 cells through cAMP/protein kinase A/extracellular signal-regulated kinase pathway.</title>
            <link>http://www.medworm.com/index.php?rid=3048825&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19949837%26dopt%3DAbstract</link>
            <description>In this study, we investigated the effects of high glucose on differentiation of human osteoblastic MG-63 cells and involved intracellular signal transduction pathways. Here, we showed that high glucose suppressed the cell growth, mineralization, and expression of osteogenic markers including Runx2, collagen I, osteocalcin, osteonectin, but inversely promoted expression of adipogenic markers including PPARgamma, aP2, resistin, and adipsin. Moreover, high glucose significantly increased the intracellular cAMP level in a time-dependent manner and induced ERK1/2 activation. Meanwhile, supplementation of H89, a specific inhibitor of PKA, and PD98059, a specific inhibitor of MAPK/ERK kinase, reversed the cell growth inhibition, the down-regulation of osteogenic markers and the up-regulation of ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3048825</comments>
            <pubDate>Tue, 01 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3048825</guid>        </item>
        <item>
            <title>IL-1beta modulate the Ca(2+)-activated big-conductance K channels (BK) via reactive oxygen species in cultured rat aorta smooth muscle cells.</title>
            <link>http://www.medworm.com/index.php?rid=3048824&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19949838%26dopt%3DAbstract</link>
            <description>In this study, we investigated how IL-1beta modulates BK channel function in cultured arterial smooth muscle cells (ASMCs), and examined the role of H(2)O(2) in the process. We demonstrated that IL-1beta had biphasic effects on BK channel function and membrane potential of ASMCs, that is both concentration and time dependent. IL-1beta increased BK channel-dependent K(+) current and hyperpolarized ASMCs when applied for 30 min. While long-term (24-48 h) treatment of IL-1beta resulted in decreased expression of alpha-subunit of BK channel, suppressed BK channel activity, decreased BK channel-dependent K(+) current and depolarization of the cells. H(2)O(2) scavenger catalase completely abolished the early effect of IL-1beta, while it only partly diminished the long-term effect of IL-1beta. Th...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3048824</comments>
            <pubDate>Tue, 01 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3048824</guid>        </item>
        <item>
            <title>Overexpression of the NHE1 isoform of the Na(+)/H (+) exchanger causes elevated apoptosis in isolated cardiomyocytes after hypoxia/reoxygenation challenge.</title>
            <link>http://www.medworm.com/index.php?rid=3048823&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19949839%26dopt%3DAbstract</link>
            <description>In this study, we examined the effect of additional exogenous NHE1 expression on isolated cardiomyocytes susceptibility to ischemia/reperfusion damage. Exogenous NHE1 elevated Na(+)/H(+) exchanger expression and activity when introduced into isolated cardiomyocytes through an adenoviral system. Isolated cardiomyocytes were subjected to simulated ischemia and reperfusion after infection with either control or NHE1-containing adenovirus. Cells were placed into an anaerobic chamber and effects of NHE1 expression after hypoxia/reoxygenation were examined. Hypoxia/reoxygenation increased caspase-3-like activity in controls, and the effect was greatly magnified in cells expressing NHE1 protein. It also elevated the percentage of apoptotic cardiomyocytes, which was also aggravated by expression o...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3048823</comments>
            <pubDate>Tue, 01 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3048823</guid>        </item>
        <item>
            <title>Ca(2+)-modulated vision-linked ROS-GC guanylate cyclase transduction machinery.</title>
            <link>http://www.medworm.com/index.php?rid=3036337&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19943184%26dopt%3DAbstract</link>
            <description>Authors: Koch KW, Duda T, Sharma RK
    Vertebrate phototransduction depends on the reciprocal relationship between two-second messengers, cyclic GMP and Ca(2+). The concentration of both is reciprocally regulated including the dynamic synthesis of cyclic GMP by a membrane bound guanylate cyclase. Different from hormone receptor guanylate cyclases, the cyclases operating in phototransduction are regulated by the intracellular Ca(2+)-concentration via small Ca(2+)-binding proteins. Based on the site of their expression and their Ca(2+) modulation, this sub-branch of the cyclase family was named sensory guanylate cyclases, of which the retina specific forms are named ROS-GCs (rod outer segment guanylate cyclases). This review focuses on the structure and function of the ROS-GC subfamily pres...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3036337</comments>
            <pubDate>Fri, 27 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3036337</guid>        </item>
        <item>
            <title>cGMP production in bacteria.</title>
            <link>http://www.medworm.com/index.php?rid=3036336&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19943185%26dopt%3DAbstract</link>
            <description>Authors: Linder JU
    Production of cGMP in bacteria has been studied since the early 1970s. From the beginning on it proved to be a challenging topic. In Escherichia coli the cGMP levels were two orders of magnitude lower than the corresponding cAMP levels. Furthermore, no specific cGMP receptor protein was identified in the bacterium and a physiological role of cGMP in the bacterium was not substantiated. Consequently in 1977, compelling evidence was given that cGMP is a by-product of E. coli adenylate cyclase in vivo. This may be the reason why also work on cGMP in other bacteria like Bacillus licheniformis and Caulobacter crescentus was not pursued any further. However, recent study on cGMP and guanylate cyclase in the cyanobacterium Synechocysis PCC 6803 brought cGMP signaling in bac...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3036336</comments>
            <pubDate>Fri, 27 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3036336</guid>        </item>
        <item>
            <title>Atrial natriuretic factor-receptor guanylate cyclase signal transduction mechanism.</title>
            <link>http://www.medworm.com/index.php?rid=3036342&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19941036%26dopt%3DAbstract</link>
            <description>Authors: Duda T
    Atrial natriuretic factor (ANF) receptor guanylate cyclase (ANF-RGC), like the other members of the membrane guanylate cyclase family, is a single transmembrane-spanning protein. The transmembrane domain separates the protein into two regions, extracellular and intracellular. The extracellular region contains the ANF-binding domain and the intracellular region the catalytic domain located at the C-terminus of the protein. Preceding the catalytic domain, the intracellular region is comprised of the following functional domains: juxtaposed 40 amino acids to the transmembrane domain is the ATP-regulated module (ARM) domain [also termed the kinase homology domain (KHD)], and the putative dimerization domain. The ANF-RGC signaling is initiated by hormone, ANF, binding to its...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3036342</comments>
            <pubDate>Thu, 26 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3036342</guid>        </item>
        <item>
            <title>Ligand-mediated endocytosis and intracellular sequestration of guanylyl cyclase/natriuretic peptide receptors: role of GDAY motif.</title>
            <link>http://www.medworm.com/index.php?rid=3036341&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19941037%26dopt%3DAbstract</link>
            <description>Authors: Pandey KN
    The guanylyl cyclase/natriuretic peptide receptor-A (GC-A/NPRA), also referred to as GC-A, is a single polypeptide molecule having a critical function in blood pressure regulation and cardiovascular homeostasis. GC-A/NPRA, which resides in the plasma membrane, consists of an extracellular ligand-binding domain, a single transmembrane domain, and an intracellular cytoplasmic region containing a protein kinase-like homology domain (KHD) and a guanylyl cyclase (GC) catalytic domain. After binding with atrial and brain natriuretic peptides (ANP and BNP), GC-A/NPRA is internalized and sequestered into intracellular compartments. Therefore, GC-A/NPRA is a dynamic cellular macromolecule that traverses different subcellular compartments through its lifetime. This review desc...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3036341</comments>
            <pubDate>Thu, 26 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3036341</guid>        </item>
        <item>
            <title>Guanylate cyclases and associated activator proteins in retinal disease.</title>
            <link>http://www.medworm.com/index.php?rid=3036340&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19941038%26dopt%3DAbstract</link>
            <description>Authors: Hunt DM, Buch P, Michaelides M
    Two isoforms of guanylate cyclase, GC1 and GC2 encoded by GUCY2D and GUCY2F, are responsible for the replenishment of cGMP in photoreceptors after exposure to light. Both are required for the normal kinetics of photoreceptor sensitivity and recovery, although disease mutations are restricted to GUCY2D. Recessive mutations in this gene cause the severe early-onset blinding disorder Leber congenital amaurosis whereas dominant mutations result in a later onset less severe cone-rod dystrophy. Cyclase activity is regulated by Ca(2+) which binds to the GC-associated proteins, GCAP1 and GCAP2 encoded by GUCA1A and GUCA1B, respectively. No recessive mutations in either of these genes have been reported. Dominant missense mutations are largely confined to...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3036340</comments>
            <pubDate>Thu, 26 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3036340</guid>        </item>
        <item>
            <title>Receptor guanylyl cyclases in mammalian olfactory function.</title>
            <link>http://www.medworm.com/index.php?rid=3036339&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19941039%26dopt%3DAbstract</link>
            <description>Authors: Zufall F, Munger SD
    The contributions of guanylyl cyclases to sensory signaling in the olfactory system have been unclear. Recently, studies of a specialized subpopulation of olfactory sensory neurons (OSNs) located in the main olfactory epithelium have provided important insights into the neuronal function of one receptor guanylyl cyclase, GC-D. Mice expressing reporters such as beta-galactosidase and green fluorescent protein in OSNs that normally express GC-D have allowed investigators to identify these neurons in situ, facilitating anatomical and physiological studies of this sparse neuronal population. The specific perturbation of GC-D function in vivo has helped to resolve the role of this guanylyl cyclase in the transduction of olfactory stimuli. Similar approaches coul...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3036339</comments>
            <pubDate>Thu, 26 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3036339</guid>        </item>
        <item>
            <title>Involvement of rhodopsin and ATP in the activation of membranous guanylate cyclase in retinal photoreceptor outer segments (ROS-GC) by GC-activating proteins (GCAPs): a new model for ROS-GC activation and its link to retinal diseases.</title>
            <link>http://www.medworm.com/index.php?rid=3036338&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19941040%26dopt%3DAbstract</link>
            <description>Authors: Bondarenko VA, Hayashi F, Usukura J, Yamazaki A
    Membranous guanylate cyclase in retinal photoreceptor outer segments (ROS-GC), a key enzyme for the recovery of photoreceptors to the dark state, has a topology identical to and cytoplasmic domains homologous to those of peptide-regulated GCs. However, under the prevailing concept, its activation mechanism is significantly different from those of peptide-regulated GCs: GC-activating proteins (GCAPs) function as the sole activator of ROS-GC in a Ca(2+)-sensitive manner, and neither reception of an outside signal by the extracellular domain (ECD) nor ATP binding to the kinase homology domain (KHD) is required for its activation. We have recently shown that ATP pre-binding to the KHD in ROS-GC drastically enhances its GCAP-stimulate...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3036338</comments>
            <pubDate>Thu, 26 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3036338</guid>        </item>
        <item>
            <title>Central role of guanylyl cyclase in natriuretic peptide signaling in hypertension and metabolic syndrome.</title>
            <link>http://www.medworm.com/index.php?rid=3031128&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19937369%26dopt%3DAbstract</link>
            <description>Authors: Martel G, Hamet P, Tremblay J
    Studied for nearly 30 years for its ability to control many parameters, such as vascular smooth muscle cell relaxation, heart fibrosis, and kidney function, the natriuretic peptide (NP) system is now considered to be a key element in several other major metabolic pathways. After stimulation by NPs, natriuretic peptide receptors (NPR) convert GTP to the second messenger cGMP. In addition to its vasodilatory effects and natriuretic and diuretic functions, cGMP has been positively associated with fat cell function, apoptosis, and NPR expression/activity modulation. The NP system is also closely linked to metabolic syndrome (MetS) progression and obesity control. A new era is now on its way targeting the NP system to not only treat high blood pressure...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3031128</comments>
            <pubDate>Wed, 25 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3031128</guid>        </item>
        <item>
            <title>Odorant-linked ROS-GC subfamily membrane guanylate cyclase transduction system.</title>
            <link>http://www.medworm.com/index.php?rid=3031131&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19937091%26dopt%3DAbstract</link>
            <description>Authors: Sharma RK, Duda T
    This review focuses on the principles of the Ca(2+)-modulated ROS-GC subfamily transduction system linked with the mammalian olfactory transduction field, its historical development, and the present day status on its constitution and operational mechanisms controlling the process of olfactory-transduction. Beginning parts of this article are freely borrowed from the earlier reviews of the authors (Sharma RK, Duda T, Venkataraman V, Koch KW, Curr Topics Biochem Res 6:111-144, 2004; Duda T, Venkataraman V, Sharma RK, Neuronal calcium sensor proteins, pp 91-113, Nova Science Publishers, Inc., 2007).
    PMID: 19937091 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3031131</comments>
            <pubDate>Tue, 24 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3031131</guid>        </item>
        <item>
            <title>A new Rac/PAK/GC/cGMP signaling pathway.</title>
            <link>http://www.medworm.com/index.php?rid=3031130&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19937092%26dopt%3DAbstract</link>
            <description>Authors: Guo D, Zhang JJ, Huang XY
    Guanosine 3',5'-cyclic monophosphate (cGMP) and small GTPase Rac are critical regulators of cell functions. Recently, Rac has been shown to use its downstream effector p21-activated kinase (PAK) to directly activate transmembrane guanylyl cyclases (GCs). This novel Rac/PAK/GC/cGMP signaling pathway bridges Rac and cGMP, and provides a general molecular mechanism for diverse receptors to regulate physiological functions such as cell migration through elevating the cellular cGMP level.
    PMID: 19937092 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3031130</comments>
            <pubDate>Tue, 24 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3031130</guid>        </item>
        <item>
            <title>Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination and degradation.</title>
            <link>http://www.medworm.com/index.php?rid=3031129&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19937093%26dopt%3DAbstract</link>
            <description>Authors: Li S, Lu K, Wang J, An L, Yang G, Chen H, Cui Y, Yin X, Xie P, Xing G, He F, Zhang L
    The HECT-type E3 Smad ubiquitination regulation factor 1 (Smurf1) functions in regulation of cell polarity and bone homeostasis by targeting Smads, Runx2, RhoA and MEKK2 for ubiquitination and degradation. In a yeast two-hybrid screening, we identified TNF receptor-associated factor 4 (TRAF4) as a candidate substrate and was further validated. The PY motifs of TRAF4 mediated the interaction with the second WW domain of Smurf1. Overexpression of Smurf1 reduced the protein levels of TRAF4 dependent of its E3 activity and the proteasome. Further, we showed that all six members of TRAF family could be ubiquitinated by Smurf1. Consequently, Smurf1 interfered with the functions of TRAFs in NF-kappaB...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3031129</comments>
            <pubDate>Tue, 24 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3031129</guid>        </item>
        <item>
            <title>Polymorphisms of IL-6 174 G/C, IL-10 -592 C/A and risk of HIV/AIDS among North Indian population.</title>
            <link>http://www.medworm.com/index.php?rid=3031132&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19936625%26dopt%3DAbstract</link>
            <description>Authors: Sobti RC, Berhane N, Mahedi SA, Kler R, Hosseini SA, Kuttiat V, Wanchu A
    A growing body of evidence suggests that host genetic factors play an important role both in susceptibility to HIV infection and progression to AIDS. The present study aimed at evaluating the role of IL-6 and IL-10 gene polymorphisms on the risk of HIV susceptibility and disease progression among North Indian patients. The polymerase chain reaction (PCR) and restriction fragment length polymorphism (RFLP) techniques were applied to genotype IL-6 and IL-10. 300 seropositive and an equal number of age- and sex-matched seronegative control subjects were recruited for this study. There was statistically no significant variation in the frequencies of IL-6 and IL-10 genotypes among cases and controls. However, ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3031132</comments>
            <pubDate>Fri, 20 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3031132</guid>        </item>
        <item>
            <title>FEZ1 interacts with CLASP2 and NEK1 through coiled-coil regions and their cellular colocalization suggests centrosomal functions and regulation by PKC.</title>
            <link>http://www.medworm.com/index.php?rid=3015576&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19924516%26dopt%3DAbstract</link>
            <description>Authors: Lanza DC, Meirelles GV, Alborghetti MR, Abrile CH, Lenz G, Kobarg J
    FEZ1 was initially described as a neuronal protein that influences axonal development and cell polarization. CLASP2 and NEK1 proteins are present in a centrosomal complex and participate in cell cycle and cell division mechanisms, but their functions were always described individually. Here, we report that NEK1 and CLASP2 colocalize with FEZ1 in a perinuclear region in mammalian cells, and observed that coiled-coil interactions occur between FEZ1/CLASP2 and FEZ1/NEK1 in vitro. These three proteins colocalize and interact with endogenous gamma-tubulin. Furthermore, we found that CLASP2 is phosphorylated and interacts with active PKC isoforms, and that FEZ1/CLASP2 colocalization is inhibited by PMA treatment. Ou...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3015576</comments>
            <pubDate>Thu, 19 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3015576</guid>        </item>
        <item>
            <title>Impact of template overhang-binding region of HIV-1 RT on the binding and orientation of the duplex region of the template-primer.</title>
            <link>http://www.medworm.com/index.php?rid=3008817&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19921401%26dopt%3DAbstract</link>
            <description>Authors: Upadhyay AK, Talele TT, Pandey VN
    Fingers domain of HIV-1 RT is one of the constituents of the dNTP-binding pocket that is involved in binding of both dNTP and the template-primer. In the ternary complex of HIV-1 RT, two residues Trp-24 and Phe-61 located on the beta1 and beta3, respectively, are seen interacting with N + 1 to N + 3 nucleotides in the template overhang. We generated nonconservative and conservative mutant derivatives of these residues and examined their impact on the template-primer binding and polymerase function of the enzyme. We noted that W24A, F61A, and F61Y and the double mutant (W24A/F61A) were significantly affected in their ability to bind template-primer and also to catalyze the polymerase reaction while W24F remained unaffected. Using a specially de...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3008817</comments>
            <pubDate>Tue, 17 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3008817</guid>        </item>
        <item>
            <title>Ca(2+)-modulated membrane guanylate cyclase in the testes.</title>
            <link>http://www.medworm.com/index.php?rid=3000415&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19915996%26dopt%3DAbstract</link>
            <description>Authors: Jankowska A, Warchol JB
    To date, the calcium-regulated membrane guanylate cyclase Rod Outer Segment Guanylate Cyclase type 1 (ROS-GC1) transduction system in addition to photoreceptors is known to be expressed in three other types of neuronal cells: in the pinealocytes, mitral cells of the olfactory bulb and the gustatory epithelium of tongue. Very recent studies from our laboratory show that expression of ROS-GC1 is not restricted to the neuronal cells; the male gonads and the spermatozoa also express ROS-GC1. In this presentation, the authors review the existing information on the localization and function of guanylate cyclase with special emphasis on Ca(2+)-modulated membrane guanylate cyclase, ROS-GC1, in the testes. The role of ROS-GC1 and its Ca(2+)-sensing modulators in...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000415</comments>
            <pubDate>Sun, 15 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000415</guid>        </item>
        <item>
            <title>Diversity of sensory guanylate cyclases in teleost fishes.</title>
            <link>http://www.medworm.com/index.php?rid=3000418&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19915958%26dopt%3DAbstract</link>
            <description>Authors: R&amp;#xE4;tscho N, Scholten A, Koch KW
    Teleost fishes like medaka fish (Oryzias latipes), zebrafish (Danio rerio), and pufferfish (Fugu rubripes) contain in their genomes a larger number of guanylate cyclases and guanylate cyclase-activating proteins than mammals. Based on amino acid sequence alignments a group of transmembrane sensory guanylate cyclases can be identified, which are mainly if not exclusively expressed in sensory organs like the retina and olfactory tissue. Retina specific guanylate cyclases and guanylate cyclase-activating proteins in the zebrafish show dynamic changes in their spatial-temporal expression patterns and transcripts of the corresponding genes appear coincidently with the beginning of cone cell maturation at 3 days post-fertilization. Expression patt...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000418</comments>
            <pubDate>Sat, 14 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000418</guid>        </item>
        <item>
            <title>Adaptive immune responses during Shigella dysenteriae type 1 infection: an in vitro stimulation with 57 kDa major antigenic OMP in the presence of anti-CD3 antibody.</title>
            <link>http://www.medworm.com/index.php?rid=3000417&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19915959%26dopt%3DAbstract</link>
            <description>Authors: Bagchi AK, Sinha AK, Adhikari R, Mukherjee J
    An effort was made to understand the role of the 57 kDa major antigenic fraction of Shigella outer membrane protein (OMP) in the presence of T-cell antigen receptor in activation of adaptive immune responses of the cell mediated immune (CMI) restored patients. The expression of HLA-DR/CD4 out of CD3(+) T-cells was significantly dominant over the HLA-DR/CD8 and comparable to unstimulated cells of infected or healthy controls. CD4(+) T-cell activation together with HLA-DR is associated with the expression of CD25(+) (IL2Ralpha) for IL-2 growth factors with decreased IL-4 levels, required for maintaining the homeostasis of CD4(+) T cell. Furthermore, the positive expression of the CD45 antigen is possibly required for acquiring the mem...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000417</comments>
            <pubDate>Sat, 14 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000417</guid>        </item>
        <item>
            <title>Dietary fat and apolipoprotein genotypes modulate plasma lipoprotein levels in Brazilian elderly women.</title>
            <link>http://www.medworm.com/index.php?rid=3000416&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19915960%26dopt%3DAbstract</link>
            <description>This study aimed to investigate the impact of apolipoprotein E, A5, and B genotypes and dietary intake on lipid profile in a sample of elderly women in Brazil. Two hundred and fifty-two women (60 years or older) living in the outskirts of the Brazilian Federal District underwent clinical and laboratory assessments to characterize glycemic and lipidemic variables, and also to exclude confounding factors (smoking, drinking, hormone replacement, cognitive impairment, physical activity). Three-day food records were used to determine usual dietary intake, whereas genotypic evaluations were in accordance to established methodologies. Genotype frequencies were consistent with the Hardy-Weinberg equilibrium. Prior to adjustment, individuals carrying the epsilon2 allele showed higher serum levels o...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000416</comments>
            <pubDate>Sat, 14 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000416</guid>        </item>
        <item>
            <title>Identification of novel PTEN-binding partners: PTEN interaction with fatty acid binding protein FABP4.</title>
            <link>http://www.medworm.com/index.php?rid=3000421&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19911253%26dopt%3DAbstract</link>
            <description>Authors: Gorbenko O, Panayotou G, Zhyvoloup A, Volkova D, Gout I, Filonenko V
    PTEN is a tumor suppressor with dual protein and lipid-phosphatase activity, which is frequently deleted or mutated in many human advanced cancers. Recent studies have also demonstrated that PTEN is a promising target in type II diabetes and obesity treatment. Using C-terminal PTEN sequence in pEG202-NLS as bait, yeast two-hybrid screening on Mouse Embryo, Colon Cancer, and HeLa cDNA libraries was carried out. Isolated positive clones were validated by mating assay and identified through automated DNA sequencing and BLAST database searches. Sequence analysis revealed a number of PTEN-binding proteins linking this phosphatase to a number of different signaling cascades, suggesting that PTEN may perform other f...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000421</comments>
            <pubDate>Fri, 13 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000421</guid>        </item>
        <item>
            <title>MS80, a novel sulfated polysaccharide, inhibits CD40-NF-kappaB pathway via targeting RIP2.</title>
            <link>http://www.medworm.com/index.php?rid=3000420&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19911254%26dopt%3DAbstract</link>
            <description>Authors: Du X, Jiang S, Liu H, Xin X, Li J, Geng M, Jiang H
    In the previous studies, MS80 was found to be able to inhibit the pulmonary fibrosis. However, the target of MS80 remains unclear. To determine the target and the anti-fibrosis mechanisms of MS80, affinity column, MALDI-TOF-MS/MS, co-immunoprecipitation, and co-localization were used. The results showed that MS80 targeting protein was receptor interacting protein 2 (RIP2), which was further confirmed by co-immunoprecipitation and co-localization. Moreover, MS80 inhibited the CD40 ligation-induced NF-kappaB activation, and subsequently inflammatory cytokines secretion, the collagen synthesis, and the excessive proliferation of fibroblasts. Thus the detailed molecular machinery was ascribed to the involvement of MS80 in targetin...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000420</comments>
            <pubDate>Fri, 13 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000420</guid>        </item>
        <item>
            <title>Hepsin activates prostasin and cleaves the extracellular domain of the epidermal growth factor receptor.</title>
            <link>http://www.medworm.com/index.php?rid=3000419&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19911255%26dopt%3DAbstract</link>
            <description>Authors: Chen M, Chen LM, Lin CY, Chai KX
    The epithelial extracellular serine protease activation cascade involves matriptase (PRSS14) and prostasin (PRSS8), capable of modulating epidermal growth factor receptor (EGFR) signaling. Matriptase activates prostasin by cleaving in the amino-terminal pro-peptide region of prostasin, presumably at the Arg residue of position 44 (R44) of the full-length human prostasin. Using an Arg-to-Ala mutant (R44A) human prostasin, we showed in this report that the cleavage of prostasin by matriptase is at Arg44. This prostasin proteolytic activation site is also cleaved by hepsin (TMPRSS1) to produce active prostasin capable of forming a covalent complex with protease nexin 1 (PN-1). An amino-terminal truncation of EGFR in the extracellular domain (ECD) ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000419</comments>
            <pubDate>Fri, 13 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000419</guid>        </item>
        <item>
            <title>A common polymorphism in the promoter of UCP2 is associated with obesity and hyperinsulenemia in northern Indians.</title>
            <link>http://www.medworm.com/index.php?rid=2990024&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19908126%26dopt%3DAbstract</link>
            <description>In conclusion, our results suggest that the -866 AA genotype and A allele of the UCP2 gene is associated with obesity and A allele associated with hyperinsulinemia in obese subjects.
    PMID: 19908126 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2990024</comments>
            <pubDate>Thu, 12 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2990024</guid>        </item>
        <item>
            <title>Localization of erythropoietin in and around growing cartilage.</title>
            <link>http://www.medworm.com/index.php?rid=2990023&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19908127%26dopt%3DAbstract</link>
            <description>Authors: De Spiegelaere W, Cornillie P, Van den Broeck W
    Erythropoietin (EPO) is known to be a hematopoietic growth factor and a regulator of red blood cell production. Recently, EPO has also been reported to function as a tissue-protective cytokine and as an angiogenesis promoting factor. EPO is mainly regulated by hypoxia through the action of hypoxia inducible factors (HIF-1alpha and HIF-2alpha). The localization of the EPO protein and the HIF-2alpha protein were immunohistochemically analyzed in developing porcine embryos. Both proteins were localized in developing cartilage tissue. HIF-2alpha and EPO protein were expressed in the peripheral chondrocytes of cartilage anlagen, in the perichondrium and in the cell condensations that will eventually differentiate into cartilage tissue...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2990023</comments>
            <pubDate>Thu, 12 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2990023</guid>        </item>
        <item>
            <title>Role of genetic polymorphism of estrogen receptor-alpha gene and risk of prostate cancer in north Indian population.</title>
            <link>http://www.medworm.com/index.php?rid=2982957&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19904497%26dopt%3DAbstract</link>
            <description>Authors: Gupta L, Thakur H, Sobti RC, Seth A, Singh SK
    Present study depicted the role of polymorphisms in estrogen receptor-alpha gene in association with prostate cancer in north Indian population. The study was performed on 157 cases of prostate cancer, 170 cases of BPH, and 170 healthy Indian males diagnosed with prostate cancer and benign prostatic hyperplasia (BPH) and healthy males as controls. Determination of polymorphism in the ER-alpha gene was done by polymerase chain reaction followed by restriction fragment length polymorphism (RFLP) analysis with PvuII and XbaI enzymes. An association was observed between PvuII polymorphism of ER-alpha gene and that of prostate cancer. However, there was no such association with XbaI polymorphism in ER-alpha gene.
    PMID: 19904497 [Pub...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2982957</comments>
            <pubDate>Wed, 11 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2982957</guid>        </item>
        <item>
            <title>The male-determining gene SRY is a hybrid of DGCR8 and SOX3, and is regulated by the transcription factor CP2.</title>
            <link>http://www.medworm.com/index.php?rid=2982958&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19902333%26dopt%3DAbstract</link>
            <description>Authors: Sato Y, Shinka T, Sakamoto K, Ewis AA, Nakahori Y
    In mammals, sex is determined by the presence or absence of the Y chromosome that bears a male-dominant sex-determining gene SRY, which switches the differentiation of gonads into male testes. The molecular signaling mechanism turning on the switch, however, has remained unclear for 18 years since the identification of the gene. Here, we describe how this gene emerged and started to work. From amino acid homology, we realized that SRY is a hybrid gene between a portion of the first exon of DiGeorge syndrome critical region gene 8 (DGCR8) and the high-mobility group (HMG) box of SRY box-3 (SOX3) gene. We identified the regulatory sequence in the SRY promotor region by searching for a common motif shared with DGCR8 mRNA. From the...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2982958</comments>
            <pubDate>Tue, 10 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2982958</guid>        </item>
        <item>
            <title>Novel function of RECS1 as a negative regulator of TNF-alpha-induced NF-kappaB activation.</title>
            <link>http://www.medworm.com/index.php?rid=2977645&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19898777%26dopt%3DAbstract</link>
            <description>Authors: Liao Z, Wu M, Chen X
    Shear stress plays a significant role in vascular remodeling, in which process tumor necrosis factor-alpha (TNF-alpha)-induced activation of NF-kappaB is generally considered to be involved. RECS1 (responsive to centrifugal force and shear stress gene 1) was first reported to be a shear stress responsive gene and RECS1 knockout mice at old age were prone to cystic medium degeneration (CMD) and aortic dilation, accompanied by enhanced expression of matrix metalloproteinase 9 (MMP-9). RECS1 was here identified as an interacting protein of tumor necrosis factor receptor 1 (TNFR1) and negatively regulated TNF-alpha-induced NF-kappaB activation. Knockdown of RECS1 by RNA interference in human umbilical vein endothelial cells (HUVECs) prolonged TNF-alpha-induced...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2977645</comments>
            <pubDate>Sun, 08 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2977645</guid>        </item>
        <item>
            <title>Study of possible interactions of tubulin, microtubular network, and STOP protein with mitochondria in muscle cells.</title>
            <link>http://www.medworm.com/index.php?rid=2967962&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19888554%26dopt%3DAbstract</link>
            <description>Authors: Guerrero K, Monge C, Br&amp;#xFC;ckner A, Puurand U, Kadaja L, K&amp;#xE4;&amp;#xE4;mbre T, Seppet E, Saks V
    We studied possible connections of tubulin, microtubular system, and microtubular network stabilizing STOP protein with mitochondria in rat and mouse cardiac and skeletal muscles by confocal microscopy and oxygraphy. Intracellular localization and content of tubulin was found to be muscle type-specific, with high amounts in oxidative muscles, and much lower in glycolytic skeletal muscle. STOP protein localization and content in muscle cells was also muscle type-specific. In isolated heart mitochondria, addition of 1 muM tubulin heterodimer increased apparent K (m) for ADP significantly. Dissociation of microtubular system into free tubulin by colchicine treatment only slightly decr...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2967962</comments>
            <pubDate>Wed, 04 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2967962</guid>        </item>
        <item>
            <title>Inhibition of neuronal cell death after retinoic acid-induced down-regulation of P2X(7) nucleotide receptor expression.</title>
            <link>http://www.medworm.com/index.php?rid=2959703&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19882109%26dopt%3DAbstract</link>
            <description>Authors: Orellano EA, Rivera OJ, Chevres M, Chorna NE, Gonz&amp;#xE1;lez FA
    Apoptosis is a major mechanism for cell death in the nervous system during development. P2X(7) nucleotide receptors are ionotropic ATP receptors that mediate cell death under pathological conditions. We developed an in vitro protocol to investigate the expression and functional responses of P2X(7) nucleotide receptors during retinoic acid (RA)-induced neuronal differentiation of human SH-SY5Y neuroblastoma cells. Neuronal differentiation was examined measuring cellular growth arrest and neuritic processes elongation. We found that SH-SY5Y cells treated for 5 days with RA under low serum content exhibited a neuron-like phenotype with neurites extending more than twice the length of the cell body and cell growth arre...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2959703</comments>
            <pubDate>Sun, 01 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2959703</guid>        </item>
        <item>
            <title>The expression of HMGB1 protein and its receptor RAGE in human malignant tumors.</title>
            <link>http://www.medworm.com/index.php?rid=2947746&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19876719%26dopt%3DAbstract</link>
            <description>Authors: Kostova N, Zlateva S, Ugrinova I, Pasheva E
    High Mobility Group Box 1 (HMGB1) is a nuclear non-histone protein discovered to be released in the extracellular medium as a response to various stimuli and implicated in cancerogenesis. High HMGB1 levels are reported in a variety of tumor types, but there are few data relating HMGB1 to the histological grade or to a particular cell type and cellular localization. We studied the expression of HMGB1 protein in malignant human tumors of different differentiation level and in tumor metastasis. In all tumor tissues, the protein level is elevated. In moderately differentiated carcinomas, the localization of the protein is perinuclear, while in the low differentiated; there is a tendency for non-specific nuclear localization. HMGB1 protei...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2947746</comments>
            <pubDate>Fri, 30 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2947746</guid>        </item>
        <item>
            <title>Functional effects of protein kinases and peroxynitrite on cardiac carnitine palmitoyltransferase-1 in isolated mitochondria.</title>
            <link>http://www.medworm.com/index.php?rid=2942388&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19862603%26dopt%3DAbstract</link>
            <description>Authors: Sharma V, Abraham T, So A, Allard MF, McNeill JH
    We have previously shown that metoprolol can inhibit carnitine palmitoyltransferase-1 catalytic activity and decrease its malonyl CoA sensitivity within 30 min, suggesting the importance of a covalent modification. The aim of this study was to characterize the effects of PTMs on CPT-1 in the heart. Mitochondria were isolated from the hearts of male Wistar rats and incubated with kinases of interest (protein kinase A, CAMK-II, p38 MAPK, Akt) or with peroxynitrite and sodium nitroprusside. PKA decreased CPT-1 malonyl CoA sensitivity, associated with phosphorylation of CPT-1A, whereas CAMK-II increased malonyl CoA sensitivity by phosphorylating CPT-1B. p38 bound to CPT-1B and stimulated CPT-1 activity. The association of CPT-1 with...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2942388</comments>
            <pubDate>Wed, 28 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2942388</guid>        </item>
        <item>
            <title>Use of pifithrin to inhibit p53-mediated signalling of TNF in dystrophic muscles of mdx mice.</title>
            <link>http://www.medworm.com/index.php?rid=2935153&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19859789%26dopt%3DAbstract</link>
            <description>This study investigates the role that p53 plays in TNF-mediated necrosis of dystrophic myofibres by inhibiting p53 using pifithrin-alpha and three pifithrin-beta analogues. Tissue culture studies using C2C12 myoblasts established that pifithrin-alpha was toxic to differentiating myoblasts at concentrations greater than 10 muM. While non-toxic concentrations of pifithrin-alpha did not prevent the TNF-mediated inhibition of myoblast differentiation, Western blots indicated that nuclear levels of p53 were higher in TNF-treated myoblasts indicating that TNF does elevate p53. In contrast, in vivo studies in adult mdx mice showed that pifithrin-alpha significantly reduced myofibre necrosis that resulted from voluntary wheel running over 48 h. These results support the hypothesis that p53 plays s...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935153</comments>
            <pubDate>Tue, 27 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2935153</guid>        </item>
        <item>
            <title>c-Jun-NH(2) terminal kinase (JNK)-mediates AP-1 activation by thioredoxin: phosphorylation of cJun, JunB, and Fra-1.</title>
            <link>http://www.medworm.com/index.php?rid=2935152&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19859790%26dopt%3DAbstract</link>
            <description>Authors: Das KC, Muniyappa H
    Thioredoxin (Trx) is a small ubiquitous protein, which has been shown to be involved in redox-dependent cellular functions. In this article, we demonstrate that the increased level of Trx induces AP-1 DNA binding in a redox-dependent manner by activating JNK subgroup of MAPKs. The majority of AP-1 DNA binding complex was found to be composed of cJun, JunB, and Fra-1. Increased expression of Trx resulted in phosphorylation of cJun, Jun B, and Fra-1. Further, increased expression of Trx induced the phosphorylation of MKK4 and MKK7 which are upstream kinases of the JNK signaling cascade. In co-transfection studies, AP-1-dependent luciferase reporter vector and pcDNA3-Trx increased luciferase activity demonstrating that increased expression of Trx increases AP-...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935152</comments>
            <pubDate>Tue, 27 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2935152</guid>        </item>
        <item>
            <title>Phospholipase D modulation by ceramide in senescence.</title>
            <link>http://www.medworm.com/index.php?rid=2935154&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19856145%26dopt%3DAbstract</link>
            <description>We examined the source of changes in PLD activity in senescent human umbilical vein endothelial cells and in human diploid fibroblasts. Using fractionated cell components we found that the cytosolic components were necessary for maximum PLD activation. In comparison to low-passage cells, senescent cells showed a profound lack of PLD activatability. By recombining fractionated components from senescent and low-passage cells, we found that in senescence the membrane component is defective in activating PLD implicating either the PLD enzyme itself or its interaction with PKC and/or ARF. The sphingolipid ceramide has been implicated in mediating senescence. Treatment with ceramide resulted in a decrease in PLD activity, implicating ceramide as the mediator of the inhibition.
    PMID: 19856145...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935154</comments>
            <pubDate>Sun, 25 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2935154</guid>        </item>
        <item>
            <title>Erratum to: Reduced endoplasmic reticulum luminal calcium links saturated fatty acid-mediated endoplasmic reticulum stress and cell death in liver cells.</title>
            <link>http://www.medworm.com/index.php?rid=2935158&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19856078%26dopt%3DAbstract</link>
            <description>Authors: Wei Y, Wang D, Gentile CL, Pagliassotti MJ
    
    PMID: 19856078 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935158</comments>
            <pubDate>Sat, 24 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2935158</guid>        </item>
        <item>
            <title>Distinct expression patterns of hedgehog ligands between cultured and primary colorectal cancers are associated with aberrant methylation of their promoters.</title>
            <link>http://www.medworm.com/index.php?rid=2935157&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19856079%26dopt%3DAbstract</link>
            <description>In conclusion, ligand dependent activity of Hh pathway is inactive in cultured colon cancer cells correlating to ligands hypermethylation. In contrast, SHH overexpression, possible consequence of promoter hypomethylation, could play a role in the carcinogenesis of primary CRCs.
    PMID: 19856079 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935157</comments>
            <pubDate>Sat, 24 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2935157</guid>        </item>
        <item>
            <title>Phospholipase Cbeta(4) isozyme is expressed in human, rat, and murine heart left ventricles and in HL-1 cardiomyocytes.</title>
            <link>http://www.medworm.com/index.php?rid=2935156&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19856080%26dopt%3DAbstract</link>
            <description>In this study, PLCbeta((1-4)) isozymes mRNA relative expression was studied by real-time PCR (RT-PCR) in human, rat, and murine left ventricle and the presence of PLCbeta(4) isozyme at the protein level was confirmed by Western blotting in all species studied. Confocal microscopy experiments carried out in HL-1 cardiomyocytes revealed a sarcoplasmic subcellular distribution of PLCbeta(4). Although there were unexpected significant interspecies differences in the PLCbeta((1-4)) mRNA expression, PLCbeta(4) mRNA was the main transcript expressed in all left ventricles studied. Thus, whereas in human and rat left ventricles PLCbeta(4) &amp;gt; PLCbeta(3) &amp;gt; PLCbeta(2) &amp;gt; PLCbeta(1) mRNA pattern of expression was found, in murine left ventricle the pattern of expression was different, i.e., PLC...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935156</comments>
            <pubDate>Sat, 24 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2935156</guid>        </item>
        <item>
            <title>The interaction between interferon-induced protein with tetratricopeptide repeats-1 and eukaryotic elongation factor-1A.</title>
            <link>http://www.medworm.com/index.php?rid=2935155&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19856081%26dopt%3DAbstract</link>
            <description>Authors: Li HT, Su YP, Cheng TM, Xu JM, Liao J, Chen JC, Ji CY, Ai GP, Wang JP
    It has been shown previously that in mammalian cells, interferon-induced protein with tetratricopeptide repeats-1(IFIT1) is rapidly synthesized in response to viral infection, functions as an inhibitor of translation by binding to the eukaryotic initiation factor-3, and consequently assigns resistive activity against viral invasion to cells. It has also been reported that IFIT1 is rapidly produced in response to other cell stress agents with no direct relation to virus such as bacterial lipopolysaccharide and interleukin-1, but its function under these non-viral infection cell stress conditions has yet to be elucidated. Here, we demonstrate an interaction between IFIT1 and eukaryotic elongation factor-1A (eE...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935155</comments>
            <pubDate>Sat, 24 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2935155</guid>        </item>
        <item>
            <title>Effect of adjuvants on immune response and protective immunity elicited by recombinant Hsp60 (GroEL) of Salmonella typhi against S. typhi infection.</title>
            <link>http://www.medworm.com/index.php?rid=2923890&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19851830%26dopt%3DAbstract</link>
            <description>Authors: Bansal A, Paliwal PK, Sagi SS, Sairam M
    Heat shock proteins (Hsps) have been reported to be dominant antigens for the host immune response to various pathogens and thus, have great potential for use in vaccination. In the present study, we evaluated the immunogenicity and protective efficacy of GroEL of Salmonella enterica serovar Typhi against lethal infection by S. typhi Ty2 in mice with or without adjuvants. Anti GroEL-IgG titers were significantly higher in mice immunized with either GroEL-alone or in combination with alum/Complete Freund's adjuvant (CFA) as compared to the control. Analysis of antibody isotypes suggested predominance of Th2 type immune response in GroEL + alum immunized animals as revealed by higher IgG1/IgG2a ratio. Whereas, immunization of animals with ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2923890</comments>
            <pubDate>Fri, 23 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2923890</guid>        </item>
        <item>
            <title>Adipophilin affects the expression of TNF-alpha, MCP-1, and IL-6 in THP-1 macrophages.</title>
            <link>http://www.medworm.com/index.php?rid=2923889&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19851831%26dopt%3DAbstract</link>
            <description>In this study, we observe the effect of adipophilin on proinflammatory cytokine expression and secretion in THP-1 macrophages. SiRNA and adipophilin gene overexpression mediated by an pEGFP-C3 vector were used to observe the effect of adipophilin on proinflammatory cytokines in THP-1 macrophages in vitro. Realtime PCR and enzyme-linked immunosorbent assay (ELISA) were applied to detect the production of tumor necrosis factor alpha (TNF-alpha), monocyte chemoattractant protein 1 (MCP-1), and interleukin-6 (IL-6). It was found that acetylated low-density lipoprotein (AcLDL), pioglitazone [a peroxisome proliferator-activated receptor gamma (PPARgamma) agonist] increased adipophilin expression in macrophages, while glucose had no such affect. It was also shown that adipophilin augments TNF-alp...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2923889</comments>
            <pubDate>Fri, 23 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2923889</guid>        </item>
        <item>
            <title>Downregulation of CREB-binding protein expression sensitizes endothelial cells to serum-deprived apoptosis: important role of nitric oxide.</title>
            <link>http://www.medworm.com/index.php?rid=2923888&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19851832%26dopt%3DAbstract</link>
            <description>In this study, we found that when CBP expression was silenced by RNA interference, ECs were more prone to apoptosis under serum deprivation, whereas the apoptosis was not significantly induced in the serum-containing condition. The increased apoptosis is paralleled by a reduction of NO, and the apoptosis was reversed by NO donors, suggesting an important role of NO. Furthermore, CBP silencing decreased NO production by downregulating the endothelial NO synthase (eNOS) expression in a dose-dependent manner. These results indicated that CBP silencing is associated with decreased eNOS expression and NO production, and therefore concomitantly increased the sensitivity of ECs toward apoptosis.
    PMID: 19851832 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2923888</comments>
            <pubDate>Fri, 23 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2923888</guid>        </item>
        <item>
            <title>Ectopic expression of hC/EBPs in breast tumor cells induces apoptosis.</title>
            <link>http://www.medworm.com/index.php?rid=2923887&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19851833%26dopt%3DAbstract</link>
            <description>Authors: Pal P, Lochab S, Kanaujiya J, Sanyal S, Trivedi AK
    CCAAT/enhancer binding proteins (C/EBPs) are a group of transcription factors which have been implicated in cellular proliferation, terminal differentiation, and apoptosis in a variety of tissues including mammary gland. Owing to its role in various cellular functions, inactivation of C/EBP proteins is central to the pathogenesis of many disorders. Recent reports suggest that expression as well as function of C/EBP proteins is deregulated in breast tumors. Although, role of C/EBPs in growth arrest in mammary tissues has been studied in much detail; their role in apoptosis is relatively less explored. In the present study, we have assessed if breast tumors evade apoptosis and grow faster by down regulating and inhibiting the C/...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2923887</comments>
            <pubDate>Fri, 23 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2923887</guid>        </item>
        <item>
            <title>Histamine stimulates human lung fibroblast migration.</title>
            <link>http://www.medworm.com/index.php?rid=2923886&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19851834%26dopt%3DAbstract</link>
            <description>This study demonstrated that histamine has the potential to stimulate human lung fibroblast migration, and thus may contribute to regulation of wound healing and the development of fibrotic disorders of the lung.
    PMID: 19851834 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2923886</comments>
            <pubDate>Fri, 23 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2923886</guid>        </item>
        <item>
            <title>Opening of the mitoK(ATP) channel and decoupling of mitochondrial complex II and III contribute to the suppression of myocardial reperfusion hyperoxygenation.</title>
            <link>http://www.medworm.com/index.php?rid=2923885&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19851835%26dopt%3DAbstract</link>
            <description>In conclusion, our results demonstrated that diazoxide suppressed the in vivo post-ischemic myocardial hyperoxygenation through opening the mitoK(ATP) channel and ubisemiquinone-dependent O(2) (-*) generation via inhibiting mitochondrial complex II-dependent respiration.
    PMID: 19851835 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2923885</comments>
            <pubDate>Fri, 23 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2923885</guid>        </item>
        <item>
            <title>Expression and distribution of CYP3A genes, CYP2B22, and MDR1, MRP1, MRP2, LRP efflux transporters in brain of control and rifampicin-treated pigs.</title>
            <link>http://www.medworm.com/index.php?rid=2916914&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19844775%26dopt%3DAbstract</link>
            <description>Authors: Nannelli A, Rossignolo F, Tolando R, Rossato P, Pellegatti M, Longo V, Giovanni Gervasi P
    The in vivo effect of rifampicin, a potent ligand of PXR, on gene expression of CYP2B22, 3A22, 3A29, 3A46, CAR, PXR and MDR1, MRP1, MRP2, LRP transporters in liver and cortex, cerebellum, midbrain, hippocampus, meninges and brain capillaries of pig was investigated. Animals were treated i.p. with four daily doses of rifampicin (40 mg/kg). The basal mRNA expressions of the individual CYP3As, CYP2B22, CAR, and PXR in various brain regions, except meninges, were about or below 10% of the corresponding hepatic mRNA values, whereas the mRNAs of brain transporters were closer or comparable to those in liver. After pig treatment with rifampicin, the mRNA expression of CYPs and transporters from ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2916914</comments>
            <pubDate>Wed, 21 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2916914</guid>        </item>
        <item>
            <title>Chitosan prevents oxidative stress-induced amyloid beta formation and cytotoxicity in NT2 neurons: involvement of transcription factors Nrf2 and NF-kappaB.</title>
            <link>http://www.medworm.com/index.php?rid=2916913&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19844776%26dopt%3DAbstract</link>
            <description>Authors: Khodagholi F, Eftekharzadeh B, Maghsoudi N, Rezaei PF
    Increased oxidative stress is a widely accepted factor in the development and progression of Alzheimer's disease. Here, we introduce chitosan, an antioxidant oligosaccharide, as a protective agent against H(2)O(2)/FeSO(4)-induced cell death in the NT2 neural cell line. Chitosan not only protects the neurons against cell death, as measured by MTT and caspase-3 activity, but also decreases amyloid beta formation. NT2 neurons can be used to elucidate the relationship between oxidative stress and Abeta formation. We induced Abeta formation through oxidative stress in NT2 neurons and studied the effect of chitosan. We demonstrate that chitosan can be neuroprotective by suppressing Abeta formation. We further show that chitosan e...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2916913</comments>
            <pubDate>Tue, 20 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2916913</guid>        </item>
        <item>
            <title>Changes in the level of apoptosis-related proteins in Jurkat cells infected with HIV-1 versus HIV-2.</title>
            <link>http://www.medworm.com/index.php?rid=2916916&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19841866%26dopt%3DAbstract</link>
            <description>Authors: Wang X, Viswanath R, Zhao J, Tang S, Hewlett I
    Human immunodeficiency virus (HIV) infection-induced apoptosis of infected CD4 T cells as well as uninfected (bystander) CD4 T cells and other types of cells is a major factor in the pathogenesis of AIDS. Clinically, HIV-2 patients have a higher CD4 cell count at the time of an AIDS diagnosis, and generally have longer survival after development of symptoms. The mortality after an AIDS diagnosis has been reported to be more influenced by CD4 cell count than HIV type. Previous studies have shown significant variations in cytopathic effects following in vitro infection with primary isolates of HIV-1 or HIV-2 subtypes; however, the relative contributions of HIV-1 and HIV-2 infection leading to cell death remain unclear. Using a human...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2916916</comments>
            <pubDate>Mon, 19 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2916916</guid>        </item>
        <item>
            <title>MUC5AC production is downregulated in NCI-H292 lung cancer cells cultured on type-IV collagen.</title>
            <link>http://www.medworm.com/index.php?rid=2916915&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19841867%26dopt%3DAbstract</link>
            <description>In this study, we investigated whether the signals from ECM regulate MUC5AC production in the human lung epithelial cell line NCI-H292. We found that MUC5AC production is downregulated in NCI-H292 cells cultured on type-IV collagen, a major component of ECM, but shows no obvious changes when cultured on type-I collagen or fibronectin. In contrast, MUC5AC production was upregulated on laminin and on reconstituted basement membrane (Matrigel), a complex of ECM components. Antibody-mediated inhibition of integrin beta1-subunit, a major receptor involved in the adherence of cells to type-IV collagen, upregulated the MUC5AC production in NCI-H292 cells, and also in the cells cultured on type-IV collagen. Although the major signaling pathway from integrins is via Src kinase activation, treatment...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2916915</comments>
            <pubDate>Thu, 15 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2916915</guid>        </item>
        <item>
            <title>GST profile expression study in some selected plants: in silico approach.</title>
            <link>http://www.medworm.com/index.php?rid=2909507&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19838771%26dopt%3DAbstract</link>
            <description>This study aims to comprehend the relationship of GST gene family and plant oxidative stress with respect to certain specific conserved motifs, which may help in future studies for screening of biomodulators involved in plant stress metabolism.
    PMID: 19838771 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2909507</comments>
            <pubDate>Wed, 14 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2909507</guid>        </item>
        <item>
            <title>Preface to the International Symposium on &quot;Perspectives of cell signaling and molecular medicine&quot;</title>
            <link>http://www.medworm.com/index.php?rid=2901975&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19830526%26dopt%3DAbstract</link>
            <description>Authors: Sen PC
    
    PMID: 19830526 [PubMed - as supplied by publisher] (Source: Molecular and Cellular Biochemistry)</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2901975</comments>
            <pubDate>Wed, 14 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2901975</guid>        </item>
        <item>
            <title>Multifocal signal modulation therapy of cancer: ancient weapon, modern targets.</title>
            <link>http://www.medworm.com/index.php?rid=2895028&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19826768%26dopt%3DAbstract</link>
            <description>Authors: Das T, Sa G, Saha B, Das K
    Although safe in most cases, ancient treatments are ignored because neither their active components nor their molecular targets are well defined. This is not the case, however, with curcumin, a yellow-pigment substance and component of turmeric (Curcuma longa), which was identified more than a century ago. Recently, extensive research has addressed the chemotherapeutic potential of this relatively nontoxic-plant-derived polyphenol. Because most cancers are caused by deregulation of as many as 500 different genes, agents that target multiple gene products are needed for prevention and treatment of cancer. In this regard, curcumin has been reported to have immense potentiality for being used in cancer chemotherapy because of its control over the machin...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2895028</comments>
            <pubDate>Tue, 13 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2895028</guid>        </item>
        <item>
            <title>Insulin resistance due to lipid-induced signaling defects could be prevented by mahanine.</title>
            <link>http://www.medworm.com/index.php?rid=2895027&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19826769%26dopt%3DAbstract</link>
            <description>Authors: Biswas A, Bhattacharya S, Dasgupta S, Kundu R, Roy SS, Pal BC, Bhattacharya S
    It is well known that free fatty acids (FFAs) play a key role in implementing insulin resistance and type 2 diabetes. Resources of chemical compounds that intervene the derogatory effect of FFAs are indeed very limited. We have isolated mahanine, a carbazole alkaloid, from the leaves of Murraya koenegii that prevented palmitate-induced inhibition of insulin-stimulated phosphorylation of IRbeta, PI3K, PDK1, and Akt in L6 myotubes. This was also reflected in the palmitate-induced inhibition of insulin-stimulated [(3)H] 2-DOG uptake by L6 myotubes, where palmitate adverse effect was significantly blocked by mahanine. Previous reports indicated that one of the major targets of lipid-induced damage in ins...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2895027</comments>
            <pubDate>Tue, 13 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2895027</guid>        </item>
        <item>
            <title>Genetic polymorphism of CYP3A5 in Indian chronic myeloid leukemia patients.</title>
            <link>http://www.medworm.com/index.php?rid=2895030&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19823770%26dopt%3DAbstract</link>
            <description>Authors: Bajpai P, Tripathi AK, Agrawal D
    CYP3A5 is an important genetic contributor to inter-individual differences in CYP3A-dependent clinically important drugs of metabolism and also of various endogenous compounds and environmental contaminants. The CYP3A5*3 allele results in a truncated protein with loss of CYP3A5 expression and CYP3A5*6 is associated with lower CYP3A5 catalytic activity. The polymorphism analysis was performed by PCR-RFLP and some representative cases by direct sequencing. Our case control study involved 183 consecutive North Indian CML patients in chronic phase of disease and 208 geographically and racially matched healthy controls. PCR-RFLP was carried out to determine the frequency of CYP3A5*3 and CYP3A5*6 genotypes. The relationship between these allelic vari...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2895030</comments>
            <pubDate>Mon, 12 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2895030</guid>        </item>
        <item>
            <title>Mechanism of noradrenaline-induced stimulation of Na-K ATPase activity in the rat brain: implications on REM sleep deprivation-induced increase in brain excitability.</title>
            <link>http://www.medworm.com/index.php?rid=2895029&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19823772%26dopt%3DAbstract</link>
            <description>Authors: Mallick BN, Singh S, Singh A
    Rapid eye movement (REM) sleep is a unique phenomenon expressed in all higher forms of animals. Its quantity varies in different species and with ageing; it is also affected in several psycho-somatic disorders. Several lines of studies showed that after REM sleep loss, the levels of noradrenaline (NA) increase in the brain. The NA in the brain modulates neuronal Na-K ATPase activity, which helps maintaining the brain excitability status. The detailed mechanism of increase in NA level after REM sleep loss and the effect of NA on stimulation of Na-K ATPase in the neurons have been discussed. The findings have been reviewed and discussed with an aim to understand the role of REM sleep in maintaining brain excitability status.
    PMID: 19823772 [PubMe...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2895029</comments>
            <pubDate>Mon, 12 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2895029</guid>        </item>
        <item>
            <title>Telomerase activity and hepatic functions of rat embryonic liver progenitor cell in nanoscaffold-coated model bioreactor.</title>
            <link>http://www.medworm.com/index.php?rid=2881451&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19816756%26dopt%3DAbstract</link>
            <description>Authors: Giri S, Nieber K, Acikg&amp;#xF6;z A, Pavlica S, Keller M, Bader A
    Presently, there is growing interest on telomerase activity in all cells (somatic cells, stem cells, cancerous cells and others) since this activity is associated with cellular changes such as proliferation, differentiation, immortalization, cell injury and ageing. Telomerase activity is absent in most of the somatic cells but present in over 90% of cancerous cells and other immortalized cell lines. In our present study, we cultured a rat embryonal liver progenitor cell line RLC-18 in a self-assembly nanostructured scaffold-coated bioreactor (NCB), collagen-coated plates (CCP) and uncoated plates (UP), and evaluated changes of telomerase activity by non radioactive techniques (Telo TAGGG Telomerase PCR ELISA, cell ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2881451</comments>
            <pubDate>Thu, 08 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2881451</guid>        </item>
        <item>
            <title>Fibronectin-integrin mediated signaling in human cervical cancer cells (SiHa).</title>
            <link>http://www.medworm.com/index.php?rid=2881450&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19816757%26dopt%3DAbstract</link>
            <description>Authors: Maity G, Fahreen S, Banerji A, Roy Choudhury P, Sen T, Dutta A, Chatterjee A
    Interaction between cell surface integrin receptors and extracellular matrix (ECM) components plays an important role in cell survival, proliferation, and migration, including tumor development and invasion of tumor cells. Matrix metalloproteinases (MMPs) are a family of metalloproteinases capable of digesting ECM components and are important molecules for cell migration. Binding of ECM to integrins initiates cascades of cell signaling events modulating expression and activity of different MMPs. The aim of this study is to investigate fibronectin-integrin-mediated signaling and modulation of MMPs. Our findings indicated that culture of human cervical cancer cell (SiHa) on fibronectin-coated surface pe...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2881450</comments>
            <pubDate>Thu, 08 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2881450</guid>        </item>
        <item>
            <title>Evaluation of inhibitory activities of plant extracts on production of LPS-stimulated pro-inflammatory mediators in J774 murine macrophages.</title>
            <link>http://www.medworm.com/index.php?rid=2876990&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19813079%26dopt%3DAbstract</link>
            <description>Authors: Verma N, Tripathi SK, Sahu D, Das HR, Das RH
    Whole plant methanolic extracts of 14 traditionally used medicinal herbs were evaluated for their anti-inflammatory activity. Extracts of Grindelia robusta, Salix nigra, Arnica montana, and Quassia amara showed up to 4.5-fold inhibition of nitric oxide (NO) production in the J774 murine macrophage cells challenged with LPS without cytotoxicity. These four selected extracts significantly reduced the protein levels of inducible NO synthase (iNOS) and the cyclooxygenase-2 (COX-2) as observed by Western blot analysis. Culture supernatants from cells treated with these extracts indicated 3-5-fold reduction of tumor necrosis factor-alpha (TNF-alpha). However, only G. robusta and Q. amara extracts significantly inhibited (by 50%) IL-1beta ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2876990</comments>
            <pubDate>Wed, 07 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2876990</guid>        </item>
        <item>
            <title>Enhanced death signaling in ozone-exposed ischemic-reperfused hearts.</title>
            <link>http://www.medworm.com/index.php?rid=2876991&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19809794%26dopt%3DAbstract</link>
            <description>Authors: Perepu RS, Garcia C, Dostal D, Sethi R
    Although numerous advancements made in the field of human health have resulted in reduced deaths due to cardiovascular diseases (CVD), many patients with cardiac disease show no established risk. Therefore, other unknown factors may be responsible for the pathophysiology of CVD. Out of 350,000 sudden cardiac deaths each year in the United States, 60,000 deaths have been related to air pollution, suggesting a detrimental role of environmental pollutants in the development of CVD. The present study tested our hypothesis that chronic ozone exposure enhances the sensitivity to ischemia-reperfusion (I/R) injury in isolated perfused hearts. Sprague-Dawley rats were continuously exposed for 8 h/day for 28 and 56 days to filtered air or 0.8 ppm o...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2876991</comments>
            <pubDate>Fri, 02 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2876991</guid>        </item>
        <item>
            <title>Modulation of chromatin by MARs and MAR binding oncogenic transcription factor SMAR1.</title>
            <link>http://www.medworm.com/index.php?rid=2863037&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19802523%26dopt%3DAbstract</link>
            <description>Authors: Nakka KK, Chattopadhyay S
    The orchestration of the events in the cell during the progression of the cell cycle is modulated by various phenomenon which are regulated by structural modules of the cell. The nucleus is a major hub for all these regulatory units which harbour the nuclear matrix, matrix proteins and chromatin. The histone modifications etch a complex code on the chromatin and the matrix proteins in consort with the histone code regulate the gene expression. SMAR1 is a matrix attachment region binding protein that interacts with chromatin modulators like HDAC1, Sin3A and causes chromatin condensation. SMAR1 modulates the chromatin at the Vbeta locus and plays a prominent role in V(D)J recombination. Such indispensable function of SMAR1 by the modulation of chromatin...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2863037</comments>
            <pubDate>Fri, 02 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2863037</guid>        </item>
        <item>
            <title>Regulation of tyrosine kinase activity during capacitation in goat sperm.</title>
            <link>http://www.medworm.com/index.php?rid=2863036&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19802524%26dopt%3DAbstract</link>
            <description>Authors: Chatterjee M, Nandi P, Ghosh S, Sen PC
    Protein tyrosine phosphorylation is a key event accompanying sperm capacitation. Although this signaling cascade generates an array of tyrosine-phosphorylated polypeptides, their molecular characterization is still limited. It is necessary to differentiate the localization of the tyrosine-phosphorylated proteins in spermatozoa to understand the link between the different phosphorylated proteins and the corresponding regulated sperm function. cAMP plays a pivotal role in the regulation of tyrosine phosphorylation. The intracellular cAMP levels were raised in goat spermatozoa by the addition of the phosphodiesterase inhibitor, IBMX in conjugation with caffeine. Tyrosine phosphorylation was significantly up-regulated following treatment with...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2863036</comments>
            <pubDate>Fri, 02 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2863036</guid>        </item>
        <item>
            <title>TNF-alpha modulates iNOS expression in an experimental rat model of indomethacin-induced jejunoileitis.</title>
            <link>http://www.medworm.com/index.php?rid=2863035&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19802525%26dopt%3DAbstract</link>
            <description>Authors: Nandi J, Saud B, Zinkievich JM, Yang ZJ, Levine RA
    Multiple mucosal immune factors, such as TNF-alpha and IL-1beta, are thought to be key mediators involved in inflammatory bowel disease. We evaluated the role of the pro-inflammatory cytokine TNF-alpha on nitric oxide synthase (NOS) expression in indomethacin-induced jejunoileitis in rats. Jejunoileitis was induced in rats with subcutaneous injections of indomethacin (7.5 mg/kg) 24 h apart for two consecutive days, and animals were randomized into four groups. Group 1 received only indomethacin. Group 2 was treated with a daily dose of phosphodiesterase (PDE) inhibitor (theophylline or pentoxifylline) by oral gavage for 2 days before and 4 days after indomethacin. Group 3 received a single dose of anti-TNF-alpha monoclonal ant...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2863035</comments>
            <pubDate>Fri, 02 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2863035</guid>        </item>
        <item>
            <title>Activation of RhoA and FAK induces ERK-mediated osteopontin expression in mechanical force-subjected periodontal ligament fibroblasts.</title>
            <link>http://www.medworm.com/index.php?rid=2858067&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19798549%26dopt%3DAbstract</link>
            <description>Authors: Hong SY, Jeon YM, Lee HJ, Kim JG, Baek JA, Lee JC
    The precise mechanism by which Rho kinase translates the mechanical signals into OPN up-regulation in force-exposed fibroblasts has not been elucidated. Human periodontal ligament fibroblasts (hPLFs) were exposed to mechanical force by centrifuging the culture plates at a magnitude of 50 g/cm(2) for 60 min. At various times of the force application, they were processed for analyzing cell viability, trypan blue exclusion, and OPN expression at protein and RNA levels. Cellular mechanism(s) of the force-induced OPN up-regulation was also examined using various kinase inhibitors or antisense oligonucleotides specific to mechanosensitive factors. Centrifugal force up-regulated OPN expression and induced a rapid and transient increas...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2858067</comments>
            <pubDate>Thu, 01 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2858067</guid>        </item>
        <item>
            <title>Antihyperlipidemic effect of bis-1,7-(2-hydroxyphenyl)-hepta-1,6-diene-3,5-dione, a curcumin analog, on nicotine and streptozotocin treated rats.</title>
            <link>http://www.medworm.com/index.php?rid=2855066&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19789843%26dopt%3DAbstract</link>
            <description>Authors: Reddy BV, Sivagama Sundari J, Balamurugan E, Menon VP
    Diabetes and smoking have been considered as major health problems individually and their seriousness related to health hazard has been well reported. Data regarding the possible contribution of cigarette smoking to the development of diabetes are scarce and inconclusive. The aim was to investigate the effect of nicotine on diabetes and to analyze the effect of bis demethoxy curcumin analog (BDMCA) in streptozotocin (STZ) and nicotine-induced toxicity. The tissue lipids were extracted according to the method of Folch et al. Plasma and tissue cholesterol was estimated by the method of Allain et al. using reagent kit. Triglycerides were estimated by the method of Foster and Dunn. Free fatty acids were estimated by the method ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2855066</comments>
            <pubDate>Tue, 29 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2855066</guid>        </item>
        <item>
            <title>Homocysteine modulates the proteolytic potential of human arterial smooth muscle cells through a reactive oxygen species dependant mechanism.</title>
            <link>http://www.medworm.com/index.php?rid=2846829&amp;cid=s_37698_60_f&amp;fid=37698&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19787299%26dopt%3DAbstract</link>
            <description>Authors: Ke XD, Foucault-Bertaud A, Genovesio C, Dignat-George F, Lamy E, Charpiot P
    Pathological levels of homocysteine induce a dramatic degradation of arterial elastic structures. This severe metalloproteinase-dependant elastolysis affects elastic structures all over the media suggesting that smooth muscle cells (SMC) may participate to this process induced by homocysteine. Therefore, we investigated the effect of physiological (10 muM) and pathological (50, 100, and 500 muM) concentrations of homocysteine on the metalloproteinase-dependant proteolytic potential of human arterial SMC in culture. Pathological levels of homocysteine increased concomitantly the secretion of latent MMP-2 and TIMP-2 while the secretion of other elastolytic matrix metalloproteinases (MMPs) and expression ...</description>
            <author>Molecular and Cellular Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2846829</comments>
            <pubDate>Mon, 28 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2846829</guid>        </item>
    </channel>
</rss>
