<?xml version="1.0" encoding="iso-8859-1"?>
<!-- generator="FeedCreator 1.7.2" -->
<rss version="2.0">
    <channel>
        <title>Am J Physiol Cell Ph... 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 'Am J Physiol Cell Ph...' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Am+J+Physiol+Cell+Ph...&t=Am+J+Physiol+Cell+Ph...&s=Search&f=source]]></link>
        <lastBuildDate>Tue, 07 Feb 2012 08:48:49 +0100</lastBuildDate>
        <item>
            <title>Detailed examination of Mg2+ and pH sensitivity of human TRPM7 channels.</title>
            <link>http://www.medworm.com/index.php?rid=5659154&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22301056%26dopt%3DAbstract</link>
            <description>Authors: Chokshi R, Matsushita M, Kozak JA
    Abstract
    TRPM7 channel-kinase is a protein highly expressed in cells of hematopoietic lineage, such as lymphocytes. Studies performed in native and heterologous expression systems have shown that TRPM7 forms non-selective cation channels functional in the plasma membrane and activated upon depletion of cellular Mg(2+). In addition to internal Mg(2+), cytosolic pH and the phospholipid PI(4,5)P(2) are potent physiological regulators of this channel: protons inhibit, while PI(4,5)P(2) is required for TRPM7 channel activity. These channels are also inhibited from inside by other metal cations and polyamines. While the regulation of TRPM7 channels by internal metal ions, acidic pH and PI(4,5)P(2) is voltage-independent, extracellular metal cati...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659154</comments>
            <pubDate>Wed, 01 Feb 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5659154</guid>        </item>
        <item>
            <title>Abl regulates smooth muscle cell proliferation by modulating actin dynamics and ERK 1/2 activation.</title>
            <link>http://www.medworm.com/index.php?rid=5659153&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22301057%26dopt%3DAbstract</link>
            <description>In this study, treatment with endothelin-1 (ET-1) and platelet-derived growth factor (PDGF) increased Abl phosphorylation at Tyr-412 (an indication of Abl activation) in vascular smooth muscle cells. To assess the role of Abl in smooth muscle cell proliferation, we generated stable Abl knockdown cells by using lentivirus-mediated RNA interference. ET-1 and PDGF induced cell proliferation was attenuated in Abl knockdown cells compared to cells expressing control shRNA and uninfected cells. Abl silencing also arrested cell cycle progression from G(0)-G(1) to S phase. Furthermore, activation of smooth muscle cells with ET-1 and PDGF induced ERK1/2 phosphorylation and AKT phosphorylation. Abl knockdown attenuated ERK1/2 phosphorylation in smooth muscle cells stimulated with ET-1 and PDGF. Howe...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659153</comments>
            <pubDate>Wed, 01 Feb 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5659153</guid>        </item>
        <item>
            <title>Molecular Assembly and Dynamics of Fluorescent Protein-Tagged Single KCa1.1 Channel in Expression System and Vascular Smooth Muscle Cells.</title>
            <link>http://www.medworm.com/index.php?rid=5659152&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22301058%26dopt%3DAbstract</link>
            <description>Authors: Yamamura H, Ikeda C, Suzuki Y, Ohya S, Imaizumi Y
    Abstract
    The large-conductance Ca(2+)-activated K(+) (K(Ca)1.1, BK) channel has pivotal roles in the regulation of vascular tone. To clarify the molecular dynamics of BK channels and their functional-coupled protein on the membrane surface, we examined single-molecule imaging of fluorescent-labeled BK subunits in the plasma membrane using total internal reflection fluorescence (TIRF) microscopy. The dynamic mobility of YFP-tagged BK a-subunit (BKÎ±-YFP) expressed in human embryo kidney 293 (HEK) cells was detected in TIRF regions at the level of individual channels and their clusters on the plasma membrane with a diffusion coefficient of 6.7Ã—10(3) nm(2)/s. When BKa-YFP was co-expressed with CFP-tagged BKÎ²1 subunit (BKÎ²1-...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659152</comments>
            <pubDate>Wed, 01 Feb 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5659152</guid>        </item>
        <item>
            <title>Mouse SGLT3a generates proton activated currents, but does not transport sugar.</title>
            <link>http://www.medworm.com/index.php?rid=5659151&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22301059%26dopt%3DAbstract</link>
            <description>In this study, we cloned mouse SGLT3a (mSGLT3a) and characterized it by expressing it in Xenopus laevis oocytes and performing electrophysiology and sugar transport assays. mSGLT3a did not transport sugar, and sugars did not induce currents at pH 7.4, though acidic pH induced inward currents that increased in the presence of sugar. Moreover, mutation of residue 457 from glutamate to glutamine resulted in a Na(+)-dependent transport of sugar that was inhibited by phlorizin. To corroborate our results in oocytes, we expressed and characterized mSGLT3a in mammalian cells and confirmed our findings. In addition, we cloned, expressed, and characterized rat SGLT3a in oocytes and found characteristics similar to mSGLT3a. In summary, acidic pH induces currents in mSGLT3a, and sugar-induced current...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659151</comments>
            <pubDate>Wed, 01 Feb 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5659151</guid>        </item>
        <item>
            <title>Increased Na+-H+ Exchanger Activity on the Apical Surface of a Cilium-deficient Cortical Collecting Duct Principal Cell Model of Polycystic Kidney Disease.</title>
            <link>http://www.medworm.com/index.php?rid=5659150&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22301060%26dopt%3DAbstract</link>
            <description>This study provides the first description of altered NHE activity, and an associated acid-base anomaly in any form of PKD.
    PMID: 22301060 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659150</comments>
            <pubDate>Wed, 01 Feb 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5659150</guid>        </item>
        <item>
            <title>Caveolin-1 Regulates Mcl-1 Stability and Anoikis in Lung Carcinoma Cells.</title>
            <link>http://www.medworm.com/index.php?rid=5640332&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22277751%26dopt%3DAbstract</link>
            <description>Authors: Chunhacha P, Pongrakhananon V, Rojanasakul Y, Chanvorachote P
    Abstract
    Both Caveolin-1 (Cav-1) and Mcl-1 have been implicated in the regulation of cancer cell anoikis but their relationship and underlying mechanisms of regulation are not known. The present study demonstrated for the first time that Cav-1 regulates Mcl-1 through protein-protein interaction and inhibits its downregulation during cell anoikis in human lung cancer cells. Immunoprecipitation and immunocytochemistry studies showed that Cav-1 interacted with Mcl-1 and prevented it from degradation via the ubiquitin-proteasome pathway. Mcl-1 and Mcl-1-Cav-1 complex were highly elevated in Cav-1 overexpressing cells, but were greatly reduced in Cav-1 knockdown cells. Consistent with this finding, we found that Mcl-...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5640332</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5640332</guid>        </item>
        <item>
            <title>ENaCs and ASICs as Therapeutic Targets.</title>
            <link>http://www.medworm.com/index.php?rid=5640331&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22277752%26dopt%3DAbstract</link>
            <description>Authors: Qadri YJ, Rooj AK, Fuller CM
    Abstract
    The Epithelial Na(+) Channel (ENaC) and Acid-sensitive Ion Channel (ASIC) branches of the ENaC/Degenerin superfamily of cation channels have drawn increasing attention as potential therapeutic targets in a variety of diseases and conditions. Originally thought to be solely expressed in fluid absorptive epithelia and in neurons, it has become apparent that members of this family exhibit nearly ubiquitous expression. Therapeutic opportunities range from hypertension, due to the role of ENaC in maintaining whole body salt and water homeostasis, to anxiety disorders and pain associated with ASIC activity. As a physiologist intrigued by the fundamental mechanics of salt and water transport, it was natural that Dale Benos, to whom this serie...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5640331</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5640331</guid>        </item>
        <item>
            <title>Myostatin-Null Mice Exhibit Delayed Skin Wound Healing through The Blockade of Transforming Growth Factor-Î² Signaling by Decorin.</title>
            <link>http://www.medworm.com/index.php?rid=5640330&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22277753%26dopt%3DAbstract</link>
            <description>Authors: Zhang C, Tan CK, McFarlane C, Sharma M, Tan NS, Kambadur R
    Abstract
    Myostatin (Mstn) is a secreted growth and differentiation factor that belongs to the transforming growth factor-Î² (TGF-Î²) superfamily. Mstn has been well characterized as a regulator of myogenesis, and has been shown to play a critical role in postnatal muscle regeneration. Herein, we report for the first time that Mstn is expressed in both epidermis and dermis of murine and human skin and that Mstn-null mice exhibited delayed skin wound healing due to a combination of effects resulting from delayed epidermal re-epithelialization and dermal contraction. In epidermis, reduced keratinocyte migration and protracted keratinocyte proliferation were observed, which subsequently led to delayed recovery of epide...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5640330</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5640330</guid>        </item>
        <item>
            <title>Breast cancer cell-derived matrix supports vascular morphogenesis.</title>
            <link>http://www.medworm.com/index.php?rid=5640329&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22277754%26dopt%3DAbstract</link>
            <description>Authors: Cuddy AC, Qiu C, Gerecht S
    Abstract
    The extracellular matrix (ECM), important for maintaining tissue homeostasis, is abnormally expressed in mammary tumors and additionally plays a crucial role in angiogenesis. We hypothesize that breast cancer cells (BCC) deposit ECM that supports unique patterns of vascular morphogenesis of endothelial cells (ECs). Evaluation of ECM expression revealed that a non-tumorigenic cell line (MCF10A), a tumorigenic cell line (MCF7), and a metastatic cell line (MDA-MB-231) express collagens I and IV, fibronectin, and laminin with tenascin-C limited to MCF10A and MCF7. The amount of ECM deposited by BCCs was found to be higher in MCF10A compared to MCF7 and MDA231, with all ECM differing in their gross structure but similar in mean fiber diameter...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5640329</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5640329</guid>        </item>
        <item>
            <title>The Na,K-ATPase Î±1Î²1 heterodimer as a cell adhesion molecule in epithelia.</title>
            <link>http://www.medworm.com/index.php?rid=5640328&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22277755%26dopt%3DAbstract</link>
            <description>Authors: Vagin O, Dada LA, Tokhtaeva E, Sachs G
    Abstract
    The ion gradients generated by the Na,K-ATPase play a critical role in epithelia by driving transepithelial transport of various solutes. The efficiency of this Na,K-ATPase-driven vectorial transport depends on the integrity of epithelial junctions that maintain polar distribution of membrane transporters, including the basolateral sodium pump, and restrict paracellular diffusion of solutes. The review summarizes the data showing that, in addition to pumping ions, the Na,K-ATPase located at the sites of cell-cell junction acts as a cell adhesion molecule by interacting with the Na,K-ATPase of the adjacent cell in the intercellular space accompanied by anchoring to the cytoskeleton in the cytoplasm. The review also discusses t...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5640328</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5640328</guid>        </item>
        <item>
            <title>ENDOTHELIAL Ca2+ WAVELETS AND THE INDUCTION OF MYOENDOTHELIAL FEEDBACK.</title>
            <link>http://www.medworm.com/index.php?rid=5640327&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22277756%26dopt%3DAbstract</link>
            <description>This study examined whether second messenger flux through myoendothelial gap junctions initiates a negative feedback response in hamster retractor muscle feed arteries. We specifically hypothesized that when agonists elicit depolarization and a rise in second messenger concentration, inositol trisphosphate (IP3) flux activates a discrete pool of IP3 receptors (IP3R), elicits localized endothelial Ca(2+) transients and activates downstream effectors to moderate constriction. Using integrated experimental techniques, this study provided three sets of supporting observations. Beginning at the functional level, we showed that blocking intermediate conductance Ca(2+) activated K(+) channels (IK) and Ca(2+) mobilization from the endoplasmic reticulum (ER), enhanced the contractile/electrical res...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5640327</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5640327</guid>        </item>
        <item>
            <title>ERK Acts in Parallel to PKC delta to Mediate the Connexin43-dependent Potentiation of Runx2 Activity by FGF2 in MC3T3 Osteoblasts.</title>
            <link>http://www.medworm.com/index.php?rid=5640326&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22277757%26dopt%3DAbstract</link>
            <description>Authors: Niger C, Buo AM, Hebert C, Duggan BT, Williams MS, Stains JP
    Abstract
    The gap junction protein, connexin43 (Cx43) plays an important role in skeletal biology. Previously, we have shown that Cx43 can enhance the signaling and transcriptional response to fibroblast growth factor 2 (FGF2) in osteoblasts by increasing protein kinase C delta (PKC delta) activation to affect Runx2 activity. In the present study, we show by luciferase reporter assays that the ERK signaling cascade acts in parallel to PKC delta to modulate Runx2 activity downstream of the Cx43-dependent amplification of FGF2 signaling. The PKC delta-independent activation of ERK by FGF2 was confirmed by western blotting, as was the Cx43-dependent enhancement of ERK activation. Consistent with our prior observation...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5640326</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5640326</guid>        </item>
        <item>
            <title>Differential determinants for coupling of distinct G proteins with the Class B secretin receptor.</title>
            <link>http://www.medworm.com/index.php?rid=5640325&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22277758%26dopt%3DAbstract</link>
            <description>Authors: Garcia GL, Dong M, Miller LJ
    Abstract
    The secretin receptor is a prototypic Class B G protein-coupled receptor that is activated by binding of its natural peptide ligand. The signaling effects of this receptor are mediated by coupling with Gs, which activates cAMP production, and Gq, which activates intracellular calcium mobilization. We have explored the molecular basis for the coupling of each of these G proteins to this receptor using systematic site-directed mutagenesis of key residues within each of the intracellular loop regions, and studying ligand binding and secretin-stimulated cAMP and calcium responses. Mutation of a conserved histidine in the first intracellular loop (H157A and H157R) markedly reduced cell surface expression and agonist-stimulated signaling. Mu...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5640325</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5640325</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +23 new citations</title>
            <link>http://www.medworm.com/index.php?rid=5623380&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222012%252F01%252F18%252010.00%2522%255BMHDA%255D%253A%25222012%252F01%252F24%252007.00%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222012%252F01%252F18%252010.00%2522%255BEDAT%255D%29%29</link>
            <description>23 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2012/01/24PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5623380</comments>
            <pubDate>Tue, 24 Jan 2012 12:00:03 +0100</pubDate>
            <guid isPermaLink="false">5623380</guid>        </item>
        <item>
            <title>From stress specificity to basal necessity: ATF6 UPRising.</title>
            <link>http://www.medworm.com/index.php?rid=5602494&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22237402%26dopt%3DAbstract</link>
            <description>Authors: Chevet E
    Abstract
    N/A.
    PMID: 22237402 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5602494</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5602494</guid>        </item>
        <item>
            <title>Regulation of Acid-Base Transporters by Reactive Oxygen Species Following Mitochondrial Fragmentation.</title>
            <link>http://www.medworm.com/index.php?rid=5602493&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22237403%26dopt%3DAbstract</link>
            <description>Authors: Johnson D, Allman E, Nehrke K
    Abstract
    Mitochondrial morphology is determined by the balance between the opposing processes of fission and fusion, each of which is regulated by a distinct set of proteins. Abnormalities in mitochondrial dynamics have been associated with a variety of diseases, including neurodegenerative conditions such as Alzheimers, Parkinson's disease, and dominant optic atrophy. While the genetic determinants of fission and fusion are well recognized, less is known about the mechanism(s) whereby altered morphology contributes to the underlying pathophysiology of these disease states. Previous work from our laboratory identified a role for mitochondrial dynamics in intracellular pH homeostasis in both mammalian cell culture and in the genetic model organ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5602493</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5602493</guid>        </item>
        <item>
            <title>The interplay of multiple molecular and cellular components is necessary for compartmentalization of cAMP.</title>
            <link>http://www.medworm.com/index.php?rid=5602492&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22237404%26dopt%3DAbstract</link>
            <description>Authors: Murray F
    Abstract
    NA.
    PMID: 22237404 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5602492</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5602492</guid>        </item>
        <item>
            <title>Lactic acid restores skeletal muscle force in an in-vitro fatigue model: are voltage-gated chloride channels involved?</title>
            <link>http://www.medworm.com/index.php?rid=5602491&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22237405%26dopt%3DAbstract</link>
            <description>Authors: Bandschapp O, Soule CL, Iaizzo PA
    Abstract
    High interstitial [K(+)] has been reported to impede normal propagation of electrical impulses along the muscle cell membrane (sarcolemma) and then also into the transverse tubule system; this is one considered underlying mechanism associated with the development of muscle fatigue. Interestingly, the extracellular build up of lactic acid, once considered an additional cause for muscle fatigue, has recently been shown to have force-restoring effects in such conditions. Specifically, it was proposed that elevated lactic acid (and intracellular acidosis) may lead to inhibition of voltage-gated chloride channels, thereby reestablishing better excitability of the muscle cell sarcolemma. In the present study, using an in-vitro muscle co...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5602491</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5602491</guid>        </item>
        <item>
            <title>Resolvin D1 prevents TNF-Î±-mediated disruption of salivary epithelial formation.</title>
            <link>http://www.medworm.com/index.php?rid=5602490&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22237406%26dopt%3DAbstract</link>
            <description>Authors: Odusanwo O, Chinthamani S, McCall A, Duffey ME, Baker OJ
    Abstract
    SjÃ¶gren's Syndrome (SS) is a chronic autoimmune disorder characterized by inflammation of salivary glands resulting in impaired secretory function. SS pathophysiology includes elevated levels of pro-inflammatory cytokines, such as tumor necrosis factor-Î± (TNF-Î±), interferon-Î³ (IFN-Î³), interleukin-1Î² (IL-1Î²), interleukin-6 (IL-6), interleukin-18 (IL-18) and interleukin-12 (IL-12). Our recent studies indicate that chronic exposure of salivary epithelium to TNF-Î± and/or IFN-Î³ alters tight junction (TJ) integrity, leading to secretory dysfunction. Resolvins of the D-series (RvD) are endogenous lipid mediators derived from DHA that regulate excessive inflammatory responses leading to resolution and tissu...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5602490</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5602490</guid>        </item>
        <item>
            <title>The role of calcium-independent phospholipase A2 gamma in modulation of aqueous humor drainage and Ca2+ sensitization of trabecular meshwork contraction.</title>
            <link>http://www.medworm.com/index.php?rid=5602489&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22237407%26dopt%3DAbstract</link>
            <description>This study investigates the role of calcium-independent phospholipase A(2) (iPLA(2)), which controls eicosanoid synthesis, in regulation of TM cell contraction and AH outflow using mechanism-based isoform specific inhibitors R-Bromoenol lactone (R-BEL, iPLA(2)Î³ specific) and S-Bromoenol lactone (S-BEL, iPLA(2)Î² specific). Immunohistochemical analysis revealed intense staining for both iPLA(2)Î² and Î³ isoforms throughout the TM, juxtacanalicular tissue and Schlemm's canal of human eye. Inhibition of iPLA(2)Î³ by R-BEL or siRNA-mediated silencing of iPLA(2)Î³ expression induced dramatic changes in TM cell morphology,and decreased actin stress fibers, focal adhesions and myosin light chain (MLC) phosphorylation. AH outflow facility increased progressively and significantly in enucleated po...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5602489</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5602489</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +25 new citations</title>
            <link>http://www.medworm.com/index.php?rid=5560718&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F12%252F29%252020.42%2522%255BMHDA%255D%253A%25222012%252F01%252F05%252010.18%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F12%252F29%252020.42%2522%255BEDAT%255D%29%29</link>
            <description>25 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2012/01/05PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5560718</comments>
            <pubDate>Thu, 05 Jan 2012 15:18:02 +0100</pubDate>
            <guid isPermaLink="false">5560718</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +30 new citations</title>
            <link>http://www.medworm.com/index.php?rid=5550451&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F12%252F23%252021.00%2522%255BMHDA%255D%253A%25222011%252F12%252F29%252020.42%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F12%252F23%252021.00%2522%255BEDAT%255D%29%29</link>
            <description>30 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/12/29PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5550451</comments>
            <pubDate>Fri, 30 Dec 2011 01:42:01 +0100</pubDate>
            <guid isPermaLink="false">5550451</guid>        </item>
        <item>
            <title>Effects of low glucose on carotid body chemoreceptor cells activity studied in cultures of intact organs and in dissociated cells.</title>
            <link>http://www.medworm.com/index.php?rid=5535378&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189552%26dopt%3DAbstract</link>
            <description>EFFECTS OF LOW GLUCOSE ON CAROTID BODY CHEMORECEPTOR CELLS ACTIVITY STUDIED IN CULTURES OF INTACT ORGANS AND IN DISSOCIATED CELLS.
    Am J Physiol Cell Physiol. 2011 Dec 21;
    Authors: Gallego-Martin T, Fernandez-Martinez S, Rigual R, Obeso A, Gonzalez C
    Abstract
    The participation of the carotid body (CB) in glucose homeostasis and evidence obtained in simplified cultured CB slices or dissociated cells have led to propose that CB chemoreceptor cells are glucoreceptors. However, data generated in intact freshly excised organs deny CB chemoreceptor cells glucosensing properties. The physiological significance of the contention has prompted present study performed in a newly developed preparation of the intact CB organ in culture that maintains chemoreceptor cells' microenvironment...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535378</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535378</guid>        </item>
        <item>
            <title>Alterations of calcium channels and cell excitability in intracardiac ganglion neurons from type 2 diabetic rats.</title>
            <link>http://www.medworm.com/index.php?rid=5535377&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189553%26dopt%3DAbstract</link>
            <description>Authors: Liu J, Tu H, Zheng H, Zhang L, Tran TP, Muelleman RL, Li YL
    Abstract
    Clinical study has demonstrated that type 2 diabetic patients with attenuated arterial baroreflex have higher mortality rate compared to those without arterial baroreflex dysfunction. As a final pathway for the neural control of the cardiac function, functional changes of intracardiac ganglion (ICG) neurons might be involved in the attenuated arterial baroreflex in the type 2 diabetes mellitus (T2DM). Therefore, we measured the ICG neuron excitability and Ca(2+) channels in the sham and T2DM rats. T2DM was induced by a combination of both high-fat diet and low dose streptozotocin (STZ, 30 mg/kg, i.p.) injection. After 12-14 weeks of the above treatment, the T2DM rats presented hyperglycemia, hyperlipidemi...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535377</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535377</guid>        </item>
        <item>
            <title>Arrestins as signaling modulators: the plot thickens.</title>
            <link>http://www.medworm.com/index.php?rid=5535376&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189554%26dopt%3DAbstract</link>
            <description>Authors: Meier KE
    Abstract
    Editorial focus...no abstract required?
    PMID: 22189554 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535376</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535376</guid>        </item>
        <item>
            <title>PANCREATIC Î²-CELLS DEPEND ON BASAL EXPRESSION OF ACTIVE ATF6Î±-p50 FOR CELL SURVIVAL EVEN UNDER NON-STRESS CONDITIONS.</title>
            <link>http://www.medworm.com/index.php?rid=5535375&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189555%26dopt%3DAbstract</link>
            <description>Authors: Teodoro T, Odisho T, Sidorova E, Volchuk A
    Abstract
    ATF6 is one of three principle ER stress response proteins and becomes activated when ER homeostasis is perturbed. ATF6 functions to increase ER capacity by stimulating transcription of ER-resident chaperone genes such as GRP78. Using an antibody that recognizes active ATF6Î±-p50 we found that active ATF6Î± was detected in insulinoma cells and rodent islets even under basal conditions and the levels were further increased by ER stress. To examine the function of ATF6Î±-p50 we depleted endogenous ATF6Î±-p50 levels using siRNA in insulinoma cells. Knock-down of endogenous ATF6Î±-p50 levels by ~60% resulted in a reduction in the steady-state levels of GRP78 mRNA and protein levels in non-stressed cells. Furthermore, ATF6Î± k...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535375</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535375</guid>        </item>
        <item>
            <title>Opioid -induced hypernociception is associated with hyperexcitability and altered tetrodotoxin-resistant Na+ channel function of dorsal root ganglia.</title>
            <link>http://www.medworm.com/index.php?rid=5535374&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189556%26dopt%3DAbstract</link>
            <description>In conclusion, chronic morphine -induced hypernociception is associated with hyperexcitability and functional remodeling of TTX-R Na(+) - and TRPV1- channels of sensory neurons.
    PMID: 22189556 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535374</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535374</guid>        </item>
        <item>
            <title>Eryptotic Red Blood Cell Adhesion to Vascular Endothelium: CXCL16/SR-PSOX, a Pathophysiological Amplifier.</title>
            <link>http://www.medworm.com/index.php?rid=5535373&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189557%26dopt%3DAbstract</link>
            <description>Authors: Lauf PK
    Abstract
    NA.
    PMID: 22189557 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535373</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535373</guid>        </item>
        <item>
            <title>Calmodulin kinase II and protein kinase C mediate the effect of increased intracellular calcium to augment late sodium current in rabbit ventricular myocytes.</title>
            <link>http://www.medworm.com/index.php?rid=5535372&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189558%26dopt%3DAbstract</link>
            <description>This study test the hypothesis that both Ca(2+)-calmodulin-dependent protein kinase II (CaMKII) and protein kinase C (PKC) mediate the effect of increased [Ca(2+)](i) to increase I(Na.L). Whole-cell and open cell-attached patch clamp techniques were used to record I(Na.L) in rabbit ventricular myocytes dialyzed with solutions containing various concentrations of [Ca(2+)](i). Dialysis of cells with [Ca(2+)](i) from 0.1 to 0.3, 0.6 and 1.0 Î¼M increased I(Na.L) in a concentration-dependent manner from 0.221 Â± 0.038 to 0.554 Â± 0.045 pA/pF (n = 10, P &amp;lt; 0.01), and was associated with an increase in mean Na(+) channel open probability and prolongation of channel mean open-time (n = 7, P &amp;lt; 0.01). In the presence of 0.6 Î¼M [Ca(2+)](i), KN-93 (10 Î¼M) and bisindolylmaleimide (BIM, 2 Î¼M) d...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535372</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535372</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +20 new citations</title>
            <link>http://www.medworm.com/index.php?rid=5513821&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F11%252F30%252013.36%2522%255BMHDA%255D%253A%25222011%252F12%252F17%252023.12%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F11%252F30%252013.36%2522%255BEDAT%255D%29%29</link>
            <description>20 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/12/17PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5513821</comments>
            <pubDate>Sun, 18 Dec 2011 04:12:00 +0100</pubDate>
            <guid isPermaLink="false">5513821</guid>        </item>
        <item>
            <title>L-mimosine blocks cell proliferation via upregulation of B-cell translocation gene 2 and N-myc downstream regulated gene 1 in prostate carcinoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=5456442&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22116304%26dopt%3DAbstract</link>
            <description>Authors: Chung LC, Tsui KH, Feng TH, Lee SL, Chang PL, Juang HH
    Abstract
    L-mimosine, an iron chelator and a prolyl 4-hydroxylase inhibitor, blocks many cancer cells at the late G1 phase. B-cell translocation gene 2 (Btg2) regulates the G1/S transition phases of the cell cycle. N-myc downstream-regulated gene 1 (Ndrg1) is a differentiation-inducing gene upregulated by hypoxia. We evaluated the molecular mechanisms of L-mimosine on cell cycle modulation in PC-3 and LNCaP prostate carcinoma cells. The effect of L-mimosine on cell proliferation of prostate carcinoma cells was determined by the (3)H-thymidine incorporation and flow cytometry assays. L-mimosine arrested the cell cycle at the G1 phase in PC-3 cells and at S phase in LNCaP cells, thus attenuating cell proliferation. Immuno...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5456442</comments>
            <pubDate>Wed, 23 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5456442</guid>        </item>
        <item>
            <title>Molecular Mechanism of Interleukin-2-induced Mucosal Homeostasis.</title>
            <link>http://www.medworm.com/index.php?rid=5456441&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22116305%26dopt%3DAbstract</link>
            <description>In this report we demonstrate that IL-2 also plays a role in IEC homeostasis through concentration-dependent regulation of IEC proliferation and cell-death. At lower concentrations (â‰¤ 50U/ml) IL-2 promoted proliferation, while at higher concentrations (100 U/ml), it promoted apoptosis. Activation by IL-2 led to tyrosine phosphorylation-dependent interactions between Jak3 and p52ShcA only at lower concentrations. Phosphatase SHP1 dephosphorylated IL-2-induced phosphorylated p52ShcA. Higher concentrations of IL-2 decreased the phosphorylation of Jak3 and p52ShcA, disrupted their interactions, redistributed Jak3 to the nucleus, and induced apoptosis in IEC. IL-2 also induced dose dependent up-regulation of p52shcA, and down-regulation of jak3-mRNA. Constitutive over-expression and mir-shRNA...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5456441</comments>
            <pubDate>Wed, 23 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5456441</guid>        </item>
        <item>
            <title>Assessment of cellular mechanisms contributing to cAMP compartmentalization in pulmonary microvascular endothelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=5456440&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22116306%26dopt%3DAbstract</link>
            <description>Authors: Feinstein WP, Zhu B, Leavesley SJ, Sayner SL, Rich TC
    Abstract
    Cyclic AMP signals encode information required to differentially regulate a wide variety of cellular responses; yet it is not well understood how information is encrypted within these signals. An emerging concept is that compartmentalization underlies specificity within the cAMP signaling pathway. This concept is based upon a series of observations indicating that cAMP levels are distinct in different regions of the cell. One such observation is that cAMP production at the plasma membrane increases pulmonary microvascular endothelial barrier integrity, whereas cAMP production in the cytosol disrupts barrier integrity. To better understand how cAMP signals might be compartmentalized, we have developed mathematic...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5456440</comments>
            <pubDate>Wed, 23 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5456440</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +29 new citations</title>
            <link>http://www.medworm.com/index.php?rid=5421770&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F11%252F06%252018.15%2522%255BMHDA%255D%253A%25222011%252F11%252F18%252021.00%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F11%252F06%252018.15%2522%255BEDAT%255D%29%29</link>
            <description>29 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/11/18PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5421770</comments>
            <pubDate>Sat, 19 Nov 2011 02:00:01 +0100</pubDate>
            <guid isPermaLink="false">5421770</guid>        </item>
        <item>
            <title>Kinase activation of ClC-3 accelerates cytoplasmic condensation during mitotic cell rounding.</title>
            <link>http://www.medworm.com/index.php?rid=5380184&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22049206%26dopt%3DAbstract</link>
            <description>Authors: Cuddapah VA, Habela CW, Watkins S, Moore LS, Barclay TT, Sontheimer H
    Abstract
    &quot;Mitotic cell rounding&quot; describes the rounding of mammalian cells before dividing into 2 daughter cells. This shape change requires coordinated cytoskeletal contraction and changes in osmotic pressure. While considerable research has been devoted to understanding mechanisms underlying cytoskeletal contraction, little is known about how osmotic gradients are involved in cell division. Here we describe cytoplasmic condensation preceding cell division, termed &quot;premitotic condensation&quot; (PMC), which involves cells extruding osmotically-active Cl(-) via ClC-3, a voltage-gated channel/transporter. This leads to a decrease in cytoplasmic volume during mitotic cell rounding and cell division. Using a com...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380184</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380184</guid>        </item>
        <item>
            <title>This, too, shall pass - like a kidney stone: a possible path to prophylaxis of nephrolithiasis?</title>
            <link>http://www.medworm.com/index.php?rid=5380182&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22049207%26dopt%3DAbstract</link>
            <description>Authors: Heneghan JF, Alper SL
    Abstract
    Editorial Focus.
    PMID: 22049207 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380182</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380182</guid>        </item>
        <item>
            <title>THE NA+,K+-ATPase AS SELF ADHESION MOLECULE AND HORMONE RECEPTOR.</title>
            <link>http://www.medworm.com/index.php?rid=5380181&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22049208%26dopt%3DAbstract</link>
            <description>Authors: Cereijido M, Contreras RG, Shoshani L, Larre I
    Abstract
    Thanks to the homeostasis of the internal milieu, metazoan cells can enormously simplify their housekeeping efforts, and engage instead in differentiation and multiple forms of organization (tissues, organs, systems) that enable them produce an astonishing diversity of mammals. The stability of the internal milieu in spite of drastic variations of the external environment (air, fresh or sea water, gastrointestinal fluids, glomerular filtrate, bile) is due to transporting epithelia that can adjust their specific permeability to H(2)O, H(+), Na(+), K(+), Ca(2+), Cl(-) over several orders of magnitude, and exchange substances with the outer milieu with an exquisite precision. This exchange is due to the polarized express...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380181</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380181</guid>        </item>
        <item>
            <title>Ischemia-induced stimulation of cerebral microvascular endothelial cell Na-K-Cl cotransport involves p38 and JNK MAP kinases.</title>
            <link>http://www.medworm.com/index.php?rid=5380180&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22049209%26dopt%3DAbstract</link>
            <description>Authors: Wallace BK, Jelks KA, O'Donnell ME
    Abstract
    Previous studies have provided evidence that in the early hours of ischemic stroke a luminal membrane blood-brain barrier (BBB) Na-K-Cl cotransporter (NKCC) participates in ischemia-induced cerebral edema formation. Inhibition of BBB NKCC activity by intravenous bumetanide significantly reduces edema and infarct in the rat permanent middle cerebral artery occlusion (MCAO) model of ischemic stroke. We have demonstrated previously that the BBB cotransporter is stimulated by hypoxia, aglycemia and arginine vasopressin (AVP), factors present during cerebral ischemia. However, the underlying mechanisms have not been known. Ischemic conditions have been shown to activate p38 and JNK MAP kinases (MAPKs) in brain and the p38 and JNK inhi...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380180</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380180</guid>        </item>
        <item>
            <title>T-type Ca2+ channels in mouse embryonic stem cells: modulation during cell cycle and contribution to self-renewal.</title>
            <link>http://www.medworm.com/index.php?rid=5380178&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22049210%26dopt%3DAbstract</link>
            <description>Authors: Rodriguez-Gomez JA, Levitsky KL, Lopez-Barneo J
    Abstract
    Ion channels participate in cell homeostasis and are involved in the regulation of proliferation and differentiation in several cell types, however their presence and function in embryonic stem (ES) cells are poorly studied. We have investigated the existence of voltage-dependent inward currents in mouse ES cells and their ability to modulate proliferation and self-renewal. Patch clamped ES cells had inactivating tetrodotoxin (TTX)-sensitive Na+ currents as well as transient Ca(2+) currents abolished by the external application of Ni(2+). Biophysical and pharmacological data indicated that the Ca(2+) current is predominantly mediated by T-type (Ca(v)3.2) channels. The number of cells expressing T-type channels and Ca...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380178</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380178</guid>        </item>
        <item>
            <title>Calsequestrin (casq1) rescues function and structure of calcium release units in skeletal muscles of casq1-null mice.</title>
            <link>http://www.medworm.com/index.php?rid=5380177&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22049211%26dopt%3DAbstract</link>
            <description>CALSEQUESTRIN (CASQ1) RESCUES FUNCTION AND STRUCTURE OF CALCIUM RELEASE UNITS IN SKELETAL MUSCLES OF CASQ1-NULL MICE.
    Am J Physiol Cell Physiol. 2011 Nov 2;
    Authors: Tomasi M, Canato M, Paolini C, Dainese M, Reggiani C, Volpe P, Protasi F, Nori A
    Abstract
    Amplitude of Ca(2+) transients, ultrastructure of Ca(2+) release units and molecular composition of sarcoplasmic reticulum (SR) are altered in fast-twitch skeletal muscles of calsequestrin-1 (CASQ1)-null mice. To determine whether such changes are directly caused by CASQ1 ablation or are instead the result of adaptive mechanisms, here we assessed ability of CASQ1 in rescuing the null phenotype. In vivo re-introduction of CASQ1 was carried out by cDNA electro transfer in flexor digitorum brevis muscle of the mouse. Exogenou...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380177</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380177</guid>        </item>
        <item>
            <title>Integrin Î±6Î²4 cooperates with LPA signaling to stimulate Rac through AKAP-Lbc-mediated RhoA activation.</title>
            <link>http://www.medworm.com/index.php?rid=5380176&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22049212%26dopt%3DAbstract</link>
            <description>In this study, we explore how the Î±6Î²4 integrin cooperates with lysophosphatidic acid (LPA) to activate Rho and Rac small GTPases. Through the use of dominant negative Rho constructs, C3 exotransferase and Rho kinase inhibitor, we find that Rho is critical for LPA-dependent chemotaxis and lamellae formation. However, utilization of specific Rho isoforms depends on integrin Î±6Î²4 expression status. Integrin Î±6Î²4-negative MDA-MB-435 cells utilize only RhoC for motility, whereas integrin Î±6Î²4-expressing cells utilize RhoC, but additionally activate and utilize RhoA for LPA-dependent cell motility and lamellae formation. Notably, the activation of RhoA by cooperative LPA and integrin Î±6Î²4 signaling requires the Rho guanine nucleotide exchange factor AKAP-Lbc. We also determine that in...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380176</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380176</guid>        </item>
        <item>
            <title>Functional role of NHE4 as a pH regulator in rat and human colonic crypts.</title>
            <link>http://www.medworm.com/index.php?rid=5380171&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22049213%26dopt%3DAbstract</link>
            <description>In this study we examined the role of NHE4 in rat and human colonic crypts, determined the effect of aldosterone on NHE4 specifically, and explored the intracellular pathways leading to activation. Colonic samples were dissected from Sprague Dawley rats. Human specimens were obtained from patients undergoing elective colon resections. Crypts were isolated using ethylenediaminetetraacetic acid and intracellular pH (pH(i)) changes were monitored using BCECF. Crypts were exposed to EIPA 7Î¼M or amiloride 400Î¼M, doses previously shown to inhibit NHE1 and NHE3 but allow NHE4 to remain active. Functional NHE4 activity was demonstrated in both rat and human colonic crypts. NHE4 activity was increased in the presence of aldosterone 1Î¼M. In the rat model, crypts were exposed to IBMX 100Î¼M/ forsk...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380171</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380171</guid>        </item>
        <item>
            <title>Toll-Like Receptor Deficiency Worsens Inflammation and Lymphedema after Lymphatic Injury.</title>
            <link>http://www.medworm.com/index.php?rid=5380168&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22049214%26dopt%3DAbstract</link>
            <description>In conclusion, TLR deficiency worsens tissue responses to lymphatic fluid stasis and is associated with decreased lymphangiogenesis, increased fibrosis, and reduced macrophage infiltration. These findings suggest a role for innate immune responses including TLR signaling in lymphatic repair and lymphedema pathogenesis.
    PMID: 22049214 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380168</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380168</guid>        </item>
        <item>
            <title>Ligand-induced internalization of the type 1 cholecystokinin receptor independent of recognized signaling activity.</title>
            <link>http://www.medworm.com/index.php?rid=5380167&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22049215%26dopt%3DAbstract</link>
            <description>Authors: Cawston EE, Harikumar KG, Miller LJ
    Abstract
    Receptor ligands identified as antagonists based on absence of stimulation of signaling can rarely stimulate receptor internalization. D-Tyr-Gly-[(Nle(28,31),D-Trp(30))CCK-26-32]-2-phenylethyl ester (D-Trp-OPE) is such a ligand that binds to the cholecystokinin (CCK) receptor and stimulates internalization. Here, the molecular basis of this trafficking event is explored, assuming ligand binding initiates conformational change exposing an epitope to direct endocytosis. Ligand-stimulated internalization was studied morphologically using fluorescent CCK and D-Trp-OPE. D-Trp-OPE occupation of CHO cell receptors stimulated internalization into the same region as CCK. Arrestin-biased action was ruled out using morphologic translocatio...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380167</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380167</guid>        </item>
        <item>
            <title>PDGF enhances store-operated Ca2+ entry by upregulating STIM1/Orai1 via activation of Akt/mTOR in human pulmonary arterial smooth muscle cells.</title>
            <link>http://www.medworm.com/index.php?rid=5361410&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22031597%26dopt%3DAbstract</link>
            <description>In this study, we investigated the role of PDGF-mediated activation of Akt signaling in the regulation of cytosolic Ca(2+) concentration ([Ca(2+)](cyt)) and cell proliferation. PDGF activated the Akt/mTOR pathway and, subsequently, enhanced store-operated Ca(2+) entry (SOCE) and cell proliferation in human PASMC. Inhibition of Akt attenuated both the increase in [Ca(2+)](cyt) due to SOCE and PASMC proliferation. This effect correlated with a significant downregulation of STIM and Orai, proposed molecular correlates for SOCE in many cell types. The data from this study present a novel pathway for the regulation of Ca(2+) signaling and PASMC proliferation involving activation of Akt in response to upregulated expression of PDGF. Targeting this pathway, may lead to development of a novel ther...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361410</comments>
            <pubDate>Wed, 26 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361410</guid>        </item>
        <item>
            <title>Mechanisms for the control of matriptase activity in the absence of sufficient HAI-1.</title>
            <link>http://www.medworm.com/index.php?rid=5361409&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22031598%26dopt%3DAbstract</link>
            <description>Authors: Xu H, Xu Z, Tseng IC, Chou FP, Chen YW, Wang JK, Johnson MD, Kataoka H, Lin CY
    Abstract
    Matriptase proteolytic activity must be tightly controlled for normal placental development, epidermal function, and epithelial integrity. Although HAI-1 represents the predominant endogenous inhibitor for matriptase and the protein molar ratio of HAI-1 to matriptase is determined to be higher than 10 in epithelial cells and the majority of carcinoma cells, an inverse HAI-1:matriptase ratio is seen in some ovarian and hematopoietic cancer cells. In the current study, cells with insufficient HAI-1 are investigated for the mechanisms through which the activity of matriptase is regulated. When matriptase activation is robustly induced in these cells, activated matriptase rapidly forms two ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361409</comments>
            <pubDate>Wed, 26 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361409</guid>        </item>
        <item>
            <title>The Role of Autophagy in Angiogenesis in Aortic Endothelial Cells.</title>
            <link>http://www.medworm.com/index.php?rid=5361408&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22031599%26dopt%3DAbstract</link>
            <description>Authors: Du J, Teng RJ, Guan T, Eis A, Kaul S, Konduri GG, Shi Y
    Abstract
    Angiogenesis plays critical roles in the recovery phase of ischemic heart disease and peripheral vascular disease. An increase in autophagy is protective under hypoxic and chronic ischemic conditions. In the present study we determined the role of autophagy in angiogenesis. 3-Methyladenine (3-MA) and siRNA against ATG5 were used to inhibit autophagy induced by nutrient-deprivation of cultured bovine aortic endothelial cells (BAECs). Assays of BAECs tube formation and cell migration, revealed that inhibition of autophagy by 3-MA or siRNA against ATG5 reduced angiogenesis. In contrast, induction of autophagy by overexpression of ATG5 increased BAECs tube formation and migration. Additionally, inhibiting autopha...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361408</comments>
            <pubDate>Wed, 26 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361408</guid>        </item>
        <item>
            <title>Nox4-Derived Reactive Oxygen Species Mediate Cardiomyocyte Injury In Early Type 1 Diabetes.</title>
            <link>http://www.medworm.com/index.php?rid=5361407&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22031600%26dopt%3DAbstract</link>
            <description>This study explored the role of the NADPH oxidase Nox4 as a source of reactive oxygen species (ROS) involved in the development of diabetic cardiomyopathy. Phosphorothioated antisense (AS) or sense (S) oligonucleotides for Nox4 were administered for 2 weeks to rats made diabetic by streptozotocin. NADPH-oxidase activity, ROS generation and the expression of Nox4, but Nox1 or Nox2, were increased in left ventricular tissue of the diabetic rats. Molecular markers of hypertrophy and myofibrosis including fibronectin, collagen, Î±-smooth muscle actin and Î²-myosin heavy chain were also increased. These parameters were attenuated by the administration of AS but not S Nox4. Moreover, the impairment of contractility observed in diabetic rats was prevented in AS- but not S-treated animals. Exposur...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361407</comments>
            <pubDate>Wed, 26 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361407</guid>        </item>
        <item>
            <title>A Dynamic Model of Calcific Nodule Destabilization in Response to Monocytes- and Oxidized Lipids-Induced Matrix Metalloproteinases.</title>
            <link>http://www.medworm.com/index.php?rid=5361406&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22031601%26dopt%3DAbstract</link>
            <description>Authors: Li R, Mittelstein D, Lee J, Fang K, Majumdar R, Tintut Y, Demer LL, Hsiai T
    Abstract
    Vulnerable plaque remains clinically undetectable, and there is no accepted in vitro model. We characterize the calcific nodules produced by calcifying vascular cells (CVC) in ApoE-null mice, demonstrating increased destabilization of cultured nodules in the presence of oxidized low density lipoprotein (oxLDL) and monocytes under pulsatile shear stress (PSS). CVC implanted in the subcutaneous space of hyperlipidemic mice produced nodules revealing features of calcific atherosclerotic plaque including a fibrous cap, cholesterol clefts, thin shoulder, lipids and calcium mineral deposits. CVC nodules seeded in the pulsatile flow channel (Ï„(avg) = 23 dyneâ€¢cm-2, âˆ‚Ï„/âˆ‚Ï„ = 71 dyneâ€¢cm(-2...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361406</comments>
            <pubDate>Wed, 26 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361406</guid>        </item>
        <item>
            <title>Mitochondrial Functional Specialization in Glycolytic and Oxidative Muscle Fibers: Tailoring the Organelle for Optimal Function.</title>
            <link>http://www.medworm.com/index.php?rid=5361405&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22031602%26dopt%3DAbstract</link>
            <description>Authors: Picard M, Hepple RT, Burelle Y
    Abstract
    In skeletal muscle two major types of muscle fibers exist: slow-twitch oxidative (Type I) fibers designed for low-intensity long-lasting contractions; and fast-twitch glycolytic (Type II) designed for high-intensity short-duration contractions. Such a wide range of capabilities has emerged through the selection across fiber types of a narrow set of molecular characteristics suitable to achieve a specific contractile phenotype. In this article we review evidence supporting the existence of distinct functional phenotypes in mitochondria from slow and fast fibers that may be required to ensure optimal muscle function. This includes differences with respect to energy substrate preferences, regulation of oxidative phosphorylation, dynamic...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361405</comments>
            <pubDate>Wed, 26 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361405</guid>        </item>
        <item>
            <title>The human gene SLC41A1 encodes for the Na+/Mg2+ exchanger.</title>
            <link>http://www.medworm.com/index.php?rid=5361404&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22031603%26dopt%3DAbstract</link>
            <description>Authors: Kolisek M, Nestler A, Vormann J, Schweigel-RÃ¶ntgen M
    Abstract
    Magnesium (Mg(2+)), the second most abundant divalent intracellular cation, is involved in the vast majority of intracellular processes, including the synthesis of nucleic acids and proteins and energy metabolism. The concentration of intracellular free Mg(2+) ([Mg(2+)](i)) in mammalian cells is therefore tightly regulated to its optimum, mainly by an exchange of intracellular Mg(2+) for extracellular Na(+). Despite the importance of this process for cellular Mg(2+) homeostasis, the gene(s) encoding for the functional Na(+)/Mg(2+) exchanger is (are) still unknown. Here, using the fluorescent probe mag-fura 2 to measure [Mg(2+)](i) changes, we examine Mg(2+) extrusion from hSLC41A1-overexpressing HEK-293 cells. ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361404</comments>
            <pubDate>Wed, 26 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361404</guid>        </item>
        <item>
            <title>Endogenous ouabain regulates cell viability.</title>
            <link>http://www.medworm.com/index.php?rid=5361403&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22031604%26dopt%3DAbstract</link>
            <description>In this study we show that EO is present in mammalian sera and CSF, as well as in commercial bovine and horse sera. The lowering of serum EO concentration by the addition of specific anti-ouabain antibodies caused a decrease in the viability of several cultured cell lines. Among these, neuronal NT2 cells were mostly affected, whereas no reduction in viability was seen in rat neuroendocrine PC12 and monkey kidney COS-7 cells. The anti-ouabain antibody-induced reduction in NT2 cell viability was significantly attenuated by the addition of ouabain and was not observed in cells growing in serum-free media. Furthermore, the addition to the medium of low concentrations (nM) of the cardenolide ouabain, but not of the bufadienolide bufalin, increased NT2 and PC12 cell viability and proliferation. ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361403</comments>
            <pubDate>Wed, 26 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361403</guid>        </item>
        <item>
            <title>The human RhAG ammonia channel is impaired by the Phe65Ser mutation in overhydrated stomatocytic red cells.</title>
            <link>http://www.medworm.com/index.php?rid=5361416&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22012326%26dopt%3DAbstract</link>
            <description>Authors: Genetet S, Ripoche P, Picot J, Bigot S, Delaunay J, Armari-Alla C, Colin Y, Mouro-Chanteloup I
    Abstract
    In red cells, Rh-Associated Glycoprotein (RhAG) acts as an ammonia channel, as demonstrated by stopped-flow analysis of ghost intracellular pH (pHi) changes. Recently, overhydrated hereditary stomatocytosis (OHSt), a rare dominantly-inherited haemolytic anemia, was found to be associated with a mutation (Phe65Ser or Ile61Arg) in RHAG. Ghosts from the erythrocytes of four of the OHSt patients with a Phe65Ser mutation were resealed with a pH-sensitive probe and submitted to ammonium gradients. Alkalinization rate constants, reflecting NH3 transport through the channel and NH3 diffusion unmediated by RhAG, were deduced from time courses of fluorescence changes. After subtra...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361416</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361416</guid>        </item>
        <item>
            <title>Strong glucose dependence of electron current in human monocytes.</title>
            <link>http://www.medworm.com/index.php?rid=5361415&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22012327%26dopt%3DAbstract</link>
            <description>We describe changes in the proton and electron current produced by PMA, the NADPH oxidase inhibitor diphenylene iodonium (DPI), and the PKC inhibitor GF109203X (GFX). To characterize glucose dependence of PBM further, NADPH oxidase activity was assessed as hydrogen peroxide (H(2)O(2)) production and was recorded fluorometrically. H(2)O(2) production exhibited similar glucose dependence as did electron current. We show fundamentally differences in the glucose dependence of ROS in human monocytes compared to human neutrophils.
    PMID: 22012327 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361415</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361415</guid>        </item>
        <item>
            <title>Static Mechanical Stretching Accelerates Lipid Production in 3T3-L1 Adipocytes by Activating the MEK Signaling Pathway.</title>
            <link>http://www.medworm.com/index.php?rid=5361414&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22012328%26dopt%3DAbstract</link>
            <description>Authors: Shoham N, Gottlieb R, Shaharabani-Yosef O, Zaretsky U, Benayahu D, Gefen A
    Abstract
    Understanding mechanotransduction in adipocytes is important for research of obesity and related diseases. We cultured 3T3-L1 preadipocytes on elastic substrata and applied static tensile strains of 12% to the substrata while inducing differentiation. Using an image processing method we monitored lipid production for a period of 3-4 weeks. The ratio of %-lipid area per field of view (FOV) in the stretched over non-stretched cultures was significantly greater than unity (p&amp;lt;0.05), reaching ~1.8 on average starting from experimental day ~10. The superior coverage of the FOV by lipids in the stretched cultures was due to significantly greater sizes of lipid droplets (LDs) with respect to non...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361414</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361414</guid>        </item>
        <item>
            <title>Angiotensin II increases the permeability and PV-1 expression of endothelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=5361413&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22012329%26dopt%3DAbstract</link>
            <description>In conclusion, we have demonstrated that angiotensin II plays a role in regulation of permeability and formation of cell surface openings through AT1 receptor and PV-1 protein synthesis in a p38 MAP kinase dependent manner in endothelial cells. The surface openings which increase in parallel with permeability may represent trans-cellular channels, caveolae or both. These morphological and permeability changes may be involved in (patho-) physiological effects of angiotensin II.
    PMID: 22012329 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361413</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361413</guid>        </item>
        <item>
            <title>Differential activation of rage by hmgb1 modulates neutrophil associated nadph oxidase activity and bacterial killing.</title>
            <link>http://www.medworm.com/index.php?rid=5361412&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22012330%26dopt%3DAbstract</link>
            <description>DIFFERENTIAL ACTIVATION OF RAGE BY HMGB1 MODULATES NEUTROPHIL ASSOCIATED NADPH OXIDASE ACTIVITY AND BACTERIAL KILLING.
    Am J Physiol Cell Physiol. 2011 Oct 19;
    Authors: TadiÃ© JM, Bae HB, Banerjee S, Zmijewski JW, Abraham E
    Abstract
    The Receptor for Advanced Glycation Endproducts (RAGE) plays an important role in host defense against bacterial infection. In the present experiments, we investigated the mechanisms by which RAGE contributes to the ability of neutrophils to eradicate bacteria. Wild type (RAGE(+/+)) neutrophils demonstrated significantly greater ability to kill E. colias compared to RAGE(-/-) neutrophils. After intraperitoneal injection of E. coli, increased numbers of bacteria were found in peritoneal fluid from RAGE(-/-) as compared to RAGE(+/+) mice. Exposure ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361412</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361412</guid>        </item>
        <item>
            <title>Relief of Autoinhibition of the Electrogenic Na/HCO3 Cotransporter NBCe1-B: Role of IRBIT versus Amino-Terminal Truncation.</title>
            <link>http://www.medworm.com/index.php?rid=5361411&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22012331%26dopt%3DAbstract</link>
            <description>Authors: Lee SK, Boron WF, Parker MD
    Abstract
    Two maneuvers known to stimulate NBCe1 activity are [1] deletion from the cytosolic amino-terminus (Nt) of NBCe1-C of an 87 amino acid sequence that contains an autoinhibitory domain (AID) and [2] binding of the protein IRBIT to elements within the same 87 aa module in a different variant, NBCe1-B. Helpful to understanding the relationship between these two phenomena would be an appreciation of the relative magnitude of stimulation caused by each maneuver for the same NBCe1 variant. In the present study, we performed two-electrode voltage-clamp on Xenopus oocytes expressing human NBCe1-B constructs with and without human IRBIT constructs. We find that removal of the AID stimulates NBCe1-B to the same extent as co-expression of wild-type...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361411</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361411</guid>        </item>
        <item>
            <title>TRPM5 is critical for linoleic acid-induced CCK secretion from the enteroendocrine cell line, STC-1.</title>
            <link>http://www.medworm.com/index.php?rid=5329319&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21998136%26dopt%3DAbstract</link>
            <description>Authors: Shah BP, Liu P, Yu T, Hansen DR, Gilbertson TA
    Abstract
    Fatty acid-induced stimulation of enteroendocrine cells leads to release of the hormones such as cholecystokinin (CCK) that contribute to satiety. Recently, the fatty acid activated G-protein-coupled receptor, GPR120, has been shown to mediate long chain unsaturated free fatty acid(FFA)-induced CCK release from the enteroendocrine cell line, STC-1, yet the downstream signaling pathway remains unclear. Here we show that linoleic acid (LA) elicits membrane depolarization and an intracellular calcium rise in STC-1 cells and these responses are significantly reduced when activity of G proteins or phospholipase C (PLC) is blocked. LA leads to activation of monovalent cation-specific transient receptor potential channel typ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5329319</comments>
            <pubDate>Wed, 12 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5329319</guid>        </item>
        <item>
            <title>KV2.1 and electrically silent KV channel subunits control excitability and contractility of Guinea pig detrusor smooth muscle.</title>
            <link>http://www.medworm.com/index.php?rid=5329318&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21998137%26dopt%3DAbstract</link>
            <description>Authors: Hristov KL, Chen M, Soder RP, Parajuli SP, Cheng Q, Kellett WF, Petkov GV
    Abstract
    Voltage-gated K(+) (K(V)) channels are implicated in detrusor smooth muscle (DSM) function. However, little is known about the functional role of the heterotetrameric K(V) channels in DSM. Here, we provide molecular, electrophysiological, and functional evidence for the presence of K(V)2.1 and electrically silent K(V) channel subunits in Guinea pig DSM. Stromatoxin-1 (ScTx1), a selective inhibitor of the homotetrameric K(V)2.1, K(V)2.2, and K(V)4.2 as well as the heterotetrameric K(V)2.1/6.3 and K(V)2.1/9.3 channels, was used to examine the role of these K(V) channels in DSM function. RT-PCR indicated mRNA expression of K(V)2.1, K(V)6.2-6.3, K(V)8.2, K(V)9.1-K(V)9.3 subunits in isolated DSM ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5329318</comments>
            <pubDate>Wed, 12 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5329318</guid>        </item>
        <item>
            <title>Hydrogen sulfide, renin, and regulating the second messenger cAMP.</title>
            <link>http://www.medworm.com/index.php?rid=5329317&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21998138%26dopt%3DAbstract</link>
            <description>Authors: Beierwaltes WH
    Abstract
    I have not included an abstact for an editorial focus article.
    PMID: 21998138 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5329317</comments>
            <pubDate>Wed, 12 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5329317</guid>        </item>
        <item>
            <title>FUNCTIONAL ANALYSIS OF THE HUMAN CONCENTRATIVE NUCLEOSIDE TRANSPORTER-1 VARIANT hCNT1S546P PROVIDES INSIGHT INTO THE SODIUM-BINDING POCKET.</title>
            <link>http://www.medworm.com/index.php?rid=5329316&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21998139%26dopt%3DAbstract</link>
            <description>In this study we have characterized the molecular mechanisms responsible for this apparent loss of function. The hCNT1S546P variant showed an appropriate ER export and insertion into the plasma membrane, whereas loss of nucleoside translocation ability affected all tested nucleoside and nucleoside-derived drugs. Site-directed mutagenesis analysis revealed that it is the lack of the serine residue itself responsible for the loss of hCNT1 function. This serine residue is highly conserved and mutation of the analogous serine in hCNT2 (Ser541) and hCNT3 (Ser568) resulted in total and partial loss of function, respectively. Moreover, hCNT3, the only member which shows a 2Na(+)/1 nucleoside stoichiometry, showed altered Na+ binding properties, associated with a shift in the Hill coefficient, con...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5329316</comments>
            <pubDate>Wed, 12 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5329316</guid>        </item>
        <item>
            <title>Tonicity-independent regulation of the osmosensitive transcription factor TonEBP (NFAT5).</title>
            <link>http://www.medworm.com/index.php?rid=5329315&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21998140%26dopt%3DAbstract</link>
            <description>Authors: Halterman JA, Kwon HM, Wamhoff BR
    Abstract
    Tonicity-responsive enhancer binding protein (TonEBP/nuclear factor of activated T-cells 5 [NFAT5]) is a Rel homology transcription factor classically known for its osmosensitive role in regulating cellular homeostasis during states of hypo- and hypertonic stress. A recently growing body of research indicates that TonEBP is not solely regulated by tonicity, but that it can be stimulated by various tonicity-independent mechanisms in both hypertonic and isotonic tissues. Physiological and pathophysiological stimuli such as cytokines, growth factors, receptor and integrin activation, contractile agonists, ions, and reactive oxygen species have been implicated in the positive regulation of TonEBP expression and activity in diverse cel...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5329315</comments>
            <pubDate>Wed, 12 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5329315</guid>        </item>
        <item>
            <title>Role of thromboxane A2-activated nonselective cation channels in hypoxic pulmonary vasoconstriction of rat.</title>
            <link>http://www.medworm.com/index.php?rid=5329314&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21998141%26dopt%3DAbstract</link>
            <description>Authors: Yoo HY, Park SJ, Seo EY, Park KS, Han JA, Kim KS, Shin DH, Earm YE, Zhang YH, Kim SJ
    Abstract
    HHypoxia-induced pulmonary vasoconstriction (HPV) is critical for matching of ventilation/perfusion in lungs. Although hypoxic inhibition of K(+) channels has been a leading hypothesis for depolarization of pulmonary arterial smooth muscle cells (PASMCs) under hypoxia, pharmacological inhibition of K(+) channels do not induce significant contraction in rat pulmonary arteries. Because a partial contraction by thromboxane A2 (TXA(2)) is required for induction of HPV, we hypothesize that TXA2 receptor (TP) stimulation might activate depolarizing nonselective cation channels (NSCs). Consistently, we found that 5-10 nM U46619, a stable agonist for TP, was indispensible for contraction ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5329314</comments>
            <pubDate>Wed, 12 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5329314</guid>        </item>
        <item>
            <title>CFTR channel pharmacology: insight from a flock of clones.</title>
            <link>http://www.medworm.com/index.php?rid=5329313&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21998142%26dopt%3DAbstract</link>
            <description>Authors: Sheppard DN
    Abstract
    Not Applicable for an Editorial Focus.
    PMID: 21998142 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5329313</comments>
            <pubDate>Wed, 12 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5329313</guid>        </item>
        <item>
            <title>Force produced by isolated sarcomeres and half-sarcomeres after an imposed stretch.</title>
            <link>http://www.medworm.com/index.php?rid=5329312&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21998143%26dopt%3DAbstract</link>
            <description>Authors: Rassier DE, Pavlov I
    Abstract
    When a stretch is imposed to activated muscles, there is a residual force enhancement that persists after the stretch; the force is higher than that produced during an isometric contraction in the corresponding length. The mechanisms behind the force enhancement remain elusive, and there is disagreement if it represents a sarcomeric property, or if it is associated with length non-uniformities among sarcomeres and half-sarcomeres. The purpose of this study was to investigate the effects of stretch on single sarcomeres and myofibrils with pre-determined numbers of sarcomeres (n = 2, 3... 8) isolated from the rabbit psoas muscle. Sarcomeres were attached between two pre-calibrated micro-needles for force measurements, and images of the preparati...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5329312</comments>
            <pubDate>Wed, 12 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5329312</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +47 new citations</title>
            <link>http://www.medworm.com/index.php?rid=5298148&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F10%252F04%252004.39%2522%255BMHDA%255D%253A%25222011%252F10%252F09%252007.55%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F10%252F04%252004.39%2522%255BEDAT%255D%29%29</link>
            <description>47 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/10/09PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5298148</comments>
            <pubDate>Sun, 09 Oct 2011 11:55:00 +0100</pubDate>
            <guid isPermaLink="false">5298148</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +30 new citations</title>
            <link>http://www.medworm.com/index.php?rid=5281425&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F09%252F29%252002.21%2522%255BMHDA%255D%253A%25222011%252F10%252F04%252004.39%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F09%252F29%252002.21%2522%255BEDAT%255D%29%29</link>
            <description>30 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/10/04PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5281425</comments>
            <pubDate>Tue, 04 Oct 2011 08:39:51 +0100</pubDate>
            <guid isPermaLink="false">5281425</guid>        </item>
        <item>
            <title>Hydrogen sulfide regulates cAMP homeostasis and renin degranulation in As4.1 and rat renin-rich kidney cells.</title>
            <link>http://www.medworm.com/index.php?rid=5261343&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21940660%26dopt%3DAbstract</link>
            <description>In conclusion, H(2)S regulates cAMP homeostasis via inhibition of adenylate cyclase and stimulation of phosphodiesterase. Our findings suggest that H(2)S plays a critical role in regulation of renin degranulation in As4.1 and rat renin-rich kidney cells.
    PMID: 21940660 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5261343</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5261343</guid>        </item>
        <item>
            <title>Divergent CFTR orthologs respond differently to the channel inhibitors CFTRinh-172, Glibenclamide, and GlyH-101.</title>
            <link>http://www.medworm.com/index.php?rid=5261342&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21940661%26dopt%3DAbstract</link>
            <description>Authors: Stahl M, Stahl K, Brubacher MB, Forrest JN
    Abstract
    Comparison of diverse orthologs is a powerful tool to study the structure and function of channel proteins. We investigated the response of human, killifish, pig, and shark cystic fibrosis transmembrane conductance regulator (CFTR) to specific inhibitors of the channel: CFTR(inh)-172, glibenclamide, and GlyH-101. In three systems, including organ perfusion of the shark rectal gland, primary cultures of shark rectal gland tubules, and expression studies of each ortholog in cRNA microinjected Xenopus laevis oocytes, we observed fundamental differences in the sensitivity to inhibition by these channel blockers. In organ perfusion studies, shark CFTR was insensitive to inhibition by CFTR(inh)-172. This insensitivity was also ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5261342</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5261342</guid>        </item>
        <item>
            <title>Lymphatic function is regulated by a coordinated expression of lymphangiogenic and anti-lymphangiogenic cytokines.</title>
            <link>http://www.medworm.com/index.php?rid=5261341&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21940662%26dopt%3DAbstract</link>
            <description>In conclusion, we show that gradients of lymphatic fluid stasis regulate not only the expression of pro-lymphangiogenic cytokines but also potent suppressors of lymphangiogenesis as a consequence of T-cell inflammation and that modulation of the balance between these stimuli can regulate lymphatic function.
    PMID: 21940662 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5261341</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5261341</guid>        </item>
        <item>
            <title>Enhanced Store-Operated Ca2+ Entry and TRPC channel Expression in Pulmonary Arteries of Monocrotaline-Induced Pulmonary Hypertensive Rats.</title>
            <link>http://www.medworm.com/index.php?rid=5261340&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21940663%26dopt%3DAbstract</link>
            <description>Authors: Liu XR, Zhang MF, Yang N, Liu Q, Wang RX, Cao YN, Yang XR, Sham JS, Lin MJ
    Abstract
    Pulmonary hypertension (PH) is associated with profound vascular remodeling and alterations in Ca(2+) homeostasis in pulmonary arterial smooth muscle cells (PASMCs). Previous studies show that canonical transient receptor potential (TRPC) genes are upregulated and store-operated Ca(2+) entry (SOCE) is augmented in PASMCs of chronic hypoxic rats and patients of pulmonary arterial hypertension (PAH). Here we further examine the involvement of TRPC and SOCE in PH with a widely used rat model of monocrotaline (MCT)-induced PAH. Rats developed severe PAH, right ventricular hypertrophy, and significant increase in store-operated TRPC1 and TRPC4 mRNA and protein in endothelium-denuded pulmonary ar...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5261340</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5261340</guid>        </item>
        <item>
            <title>Structural Selectivity of Human SGLT Inhibitors.</title>
            <link>http://www.medworm.com/index.php?rid=5261339&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21940664%26dopt%3DAbstract</link>
            <description>Authors: Hummel CS, Lu C, Liu J, Ghezzi C, Hirayama BA, Loo DD, Kepe V, Barrio JR, Wright EM
    Abstract
    Human SGLT2 inhibitors constitute the newest class of type 2 diabetes drugs, blocking up to 50% of renal glucose reabsorption in vivo. These drugs have potential for use in the diabetes epidemic, but how they work at a molecular level is poorly understood. We use electrophysiological methods to assess how these inhibitors block SGLT1 and SGLT2 co-transporters expressed in HEK293T cells, and compared them to the classic SGLT inhibitor phlorizin. Dapagliflozin ((1S)-1,5, 5-anhydro-1-C-{4-chloro-3-[(4-ethoxyphenyl)methyl]phenyl}-D-glucitol), two structural analogs, and the aglycones of phlorizin and dapagliflozin were investigated in detail. Dapagliflozin and fluoro-dapagliflozin ((1S...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5261339</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5261339</guid>        </item>
        <item>
            <title>Angiotensin II-NADPH oxidase-derived superoxide mediates diabetes-attenuated cell excitability of aortic baroreceptor neurons.</title>
            <link>http://www.medworm.com/index.php?rid=5261338&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21940665%26dopt%3DAbstract</link>
            <description>Authors: Li YL, Zheng H
    Abstract
    Overactivation of hyperpolarization-activated cyclic nucleotide-gated (HCN) channels is involved in diabetes-depressed excitability of aortic baroreceptor neurons in nodose ganglia. This involvement links to the autonomic dysfunction associated with high morbidity and mortality in diabetic patients. The present study examined the effects of an angiotensin II type I receptor (AT(1)R) antagonist (losartan), a NADPH oxidase inhibitor (apocynin), and a superoxide dismutase mimetic (tempol) on the enhanced HCN currents and attenuated cell excitability in diabetic nodose neurons. In sham and streptozotocin-induced type 1 diabetic rats, HCN currents and cell excitability of aortic baroreceptor neurons were recorded by the whole cell patch-clamp technique. ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5261338</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5261338</guid>        </item>
        <item>
            <title>Large-Scale Phosphotyrosine Proteomic Profiling of Rat Renal Collecting Duct Epithelium Reveals Predominance of Proteins Involved in Cell Polarity Determination.</title>
            <link>http://www.medworm.com/index.php?rid=5261337&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21940666%26dopt%3DAbstract</link>
            <description>Authors: Zhao B, Knepper MA, Chou CL, Pisitkun T
    Abstract
    Although extensive phosphoproteomic information is available for renal epithelial cells, previous emphasis has been on phosphorylation of serines and threonines with little focus on tyrosine phosphorylation. Here we have carried out large-scale identification of phosphotyrosine sites in pervanadate-treated native inner medullary collecting ducts of rat, with a view towards identification of physiological processes in epithelial cells that are potentially regulated by tyrosine phosphorylation. The method combined antibody-based affinity purification of tyrosine phosphorylated peptides coupled with immobilized metal ion chromatography to enrich tyrosine phosphopeptides, which were identified by LC-MS/MS. A total of 418 unique ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5261337</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5261337</guid>        </item>
        <item>
            <title>Ion Channels in Control of Cancer and Cell Apoptosis.</title>
            <link>http://www.medworm.com/index.php?rid=5261336&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21940667%26dopt%3DAbstract</link>
            <description>Authors: Lehen'kyi V, Shapovalov G, Skryma R, Prevarskaya N
    Abstract
    Ion channels contribute to virtually all basic cellular processes, including such crucial ones for maintaining tissue homeostasis as proliferation, differentiation, and apoptosis. The involvement of ion channels in regulation of programmed cell death, or apoptosis, has been known for at least three decades, based on observation that classical blockers of ion channels can influence cell death rates, prolonging or shortening cell survival. Identification of the central role of these channels in regulation of cell cycle and apoptosis as well as the recent discovery that the expression of ion channels is not limited solely to the plasma membrane, but may also include membranes of internal compartments has led research...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5261336</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5261336</guid>        </item>
        <item>
            <title>Doxorubicin acts via mitochondrial ROS to stimulate catabolism in C2C12 myotubes.</title>
            <link>http://www.medworm.com/index.php?rid=5261335&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21940668%26dopt%3DAbstract</link>
            <description>Authors: Gilliam LA, Moylan JS, Patterson EW, Smith JD, Wilson AS, Rabbani Z, Reid MB
    Abstract
    Doxorubicin, a commonly prescribed chemotherapeutic agent, causes skeletal muscle wasting in cancer patients undergoing treatment and increases mitochondrial reactive oxygen species (ROS) production. ROS stimulate protein degradation in muscle by activating proteolytic systems that include caspase-3 and the ubiquitin-proteasome pathway. We hypothesized that doxorubicin causes skeletal muscle catabolism through ROS, causing upregulation of E3 ubiquitin ligases and caspase-3. We tested this hypothesis by exposing differentiated C2C12 myotubes to doxorubicin (0.2 Î¼M). Doxorubicin decreased myotube width 48 hrs following exposure, along with a 40-50% reduction in myosin and sarcomeric actin....</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5261335</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5261335</guid>        </item>
        <item>
            <title>Uncovering the pathway of sepsis-induced renal tubular dysfunction.</title>
            <link>http://www.medworm.com/index.php?rid=5261334&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21940669%26dopt%3DAbstract</link>
            <description>Authors: Di Sole F, Girardi AC
    Abstract
    No abstract available.
    PMID: 21940669 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5261334</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5261334</guid>        </item>
        <item>
            <title>Chronic AMPK stimulation attenuates adaptive signaling in dystrophic skeletal muscle.</title>
            <link>http://www.medworm.com/index.php?rid=5261333&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21940670%26dopt%3DAbstract</link>
            <description>Authors: Ljubicic V, Khogali S, Renaud JM, Jasmin BJ
    Abstract
    In the present study, we evaluated how a pharmacologically-induced phenotype shift in dystrophic skeletal muscle would affect subsequent intracellular signaling in response to a complementary, adaptive physiological stimulus. mdx mice were treated with the AMP-activated protein kinase (AMPK) activator AICAR (500 mg/kg/day) for 30 days, and then half of the animals were subjected to a bout of treadmill running to induce acute AMPK and p38 MAPK signaling. The mRNA levels of phenotypic modifiers, including PPARÎ´, PGC-1Î±, RIP 140 and SIRT1 were assessed in skeletal muscle, as well as the expression of PRMT1 and CARM1. We found unique AMPK and p38 phosphorylation and expression signatures between dystrophic and healthy musc...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5261333</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5261333</guid>        </item>
        <item>
            <title>Extracellular chloride regulation of Kv2.1, contributor to the major outward Kv current in mammalian outer hair cells.</title>
            <link>http://www.medworm.com/index.php?rid=5261332&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21940671%26dopt%3DAbstract</link>
            <description>Authors: Li X, Surguchev A, Bian S, Navaratnam D, Santos-Sacchi J
    Abstract
    Outer hair cells (OHC) function as both receptors and effectors in providing a boost to auditory reception. Amplification is driven by the motor protein prestin, which is under anionic control. Interestingly, we now find that the major, 4-AP sensitive, outward K current of the OHC (I(K)) is also sensitive to chloride, though, in contrast to prestin, extracellularly. I(K) is inhibited by reducing extracellular Cl(-) levels, with a linear dependence of 0.4%/mM. Other Kv channel conductances in supporting cells, such as Hensen and Deiters' cells, are not affected by reduced extracellular chloride. To elucidate the molecular basis of this Cl(-) sensitive I(K), we looked at potential molecular candidates based on...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5261332</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5261332</guid>        </item>
        <item>
            <title>IGF-1 increases the expression of fibronectin by Nox4-dependent Akt phosphorylation in renal tubular epithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=5261331&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21940672%26dopt%3DAbstract</link>
            <description>Authors: New D, Block K, Bandhari B, Gorin YC, Abboud HE
    Abstract
    Extracellular matrix accumulation contributes to the progression of chronic kidney disease. Many growth factors including insulin-like growth factor-1 (IGF-1) enhance matrix protein accumulation. Proximal tubular epithelial cells (PTCs) synthesize matrix proteins. NADPH oxidases are major sources of reactive oxygen species (ROS), important signaling molecules that mediate biological responses in a variety of cells and tissue. We investigated the mechanism by which IGF-1 regulates fibronectin accumulation in PTCs and the role of a potential redox-dependant signaling pathway. IGF-1 induces an increase in NADPH-dependent superoxide generation, enhances the release of hydrogen peroxide and increases the expression of Nox...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5261331</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5261331</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +33 new citations</title>
            <link>http://www.medworm.com/index.php?rid=5219266&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F09%252F04%252023.52%2522%255BMHDA%255D%253A%25222011%252F09%252F14%252022.51%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F09%252F04%252023.52%2522%255BEDAT%255D%29%29</link>
            <description>33 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/09/14PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5219266</comments>
            <pubDate>Thu, 15 Sep 2011 02:51:55 +0100</pubDate>
            <guid isPermaLink="false">5219266</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +47 new citations</title>
            <link>http://www.medworm.com/index.php?rid=5193065&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F08%252F19%252020.22%2522%255BMHDA%255D%253A%25222011%252F09%252F04%252023.52%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F08%252F19%252020.22%2522%255BEDAT%255D%29%29</link>
            <description>47 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/09/04PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5193065</comments>
            <pubDate>Mon, 05 Sep 2011 03:52:02 +0100</pubDate>
            <guid isPermaLink="false">5193065</guid>        </item>
        <item>
            <title>Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S.</title>
            <link>http://www.medworm.com/index.php?rid=5141644&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21849667%26dopt%3DAbstract</link>
            <description>Authors: Stewart AK, Shmukler BE, Vandorpe DH, Rivera A, Heneghan JF, Li X, Hsu A, Karpatkin M, O'Neill AF, Bauer DE, Heeney MM, John K, Kuypers FA, Gallagher PG, Lux SE, Brugnara C, Westhoff CM, Alper SL
    Abstract
    Four patients with overhydrated cation leak stomatocytosis (OHSt) exhibited the heterozygous RhAG missense mutation F65S. OHSt erythrocytes were osmotically fragile, with elevated Na and decreased K contents and increased cation channel-like activity. Xenopus oocytes expressing wildtype RhAG and RhAG F65S exhibited increased ouabain and bumetanide-resistant uptake of Li(+) and (86)Rb(+), with secondarily increased (86)Rb(+) influx sensitive to ouabain and to bumetanide. Increased RhAG-associated (14)C-methylammonium (MA) influx was severely reduced in RhAG F65S-expressing...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141644</comments>
            <pubDate>Tue, 16 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141644</guid>        </item>
        <item>
            <title>Bioactive phospholipids signaling influences NHE3-dependent intestinal Na+ and fluid absorption: a macromolecular complex perspective.</title>
            <link>http://www.medworm.com/index.php?rid=5141643&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21849668%26dopt%3DAbstract</link>
            <description>Authors: Zhang W, Naren AP
    Abstract
    Malabsorption of solutes and water in the small intestine may result in large amounts of fluid entering the colon which will overwhelm its absorptive capacity and cause diarrhea. The intestinal epithelial cells drive the fluid movement through active transport of Na(+) and Cl(-) or HCO(3)(-). Electroneutral NaCl absorption is mediated by the coupled function of apical Na(+)/H(+) exchangers (NHEs) and Cl(-)/HCO(3)(-) exchangers. NHE3 (Slc9a3) is the dominant NHE in the small intestine and plays important roles in maintaining normal GI physiology. Previously, lysophosphatidic acid (LPA)has been found to acutely stimulate Na+ and fluid absorption in human intestinal epithelial cells and in mouse intestine by activating NHE3 through an LPA5-mediated ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141643</comments>
            <pubDate>Tue, 16 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141643</guid>        </item>
        <item>
            <title>Role of RhoA, ROCK and mDia1 in modulation the deformation-induced FAK,ERK,P38 and MLC motogenic signals in human Caco-2 intestinal epithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=5141642&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21849669%26dopt%3DAbstract</link>
            <description>Authors: Chaturvedi LS, Marsh HM, Basson MD
    Abstract
    Repetitive deformation enhances intestinal epithelial migration across tissue fibronectin. We evaluated the contribution of RhoA and its effectors Rho-associated kinase (ROK/ROCK) and mammalian diaphanous formins (mDia1) to deformation-induced intestinal epithelial motility across fibronectin, and the responsible FAK, ERK, p38 and MLC signaling. We reduced RhoA, ROCK1, ROCK2, and mDia1 by siRNA and pharmacologically inhibited RhoA, ROCK and FAK in human Caco-2 intestinal epithelial monolayers on fibronectin-coated membranes subjected to 10% repetitive deformation at 10 cycles/minute. Migration was measured by wound closure. Stimulation of migration by deformation was prevented by exoenzyme C3, Y27632 or selective RhoA, ROCK1and R...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141642</comments>
            <pubDate>Tue, 16 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141642</guid>        </item>
        <item>
            <title>Differential Impact of Mitochondrial Positioning on Mitochondrial Ca2+ Uptake and Ca2+ Spark Suppression in Skeletal Muscle.</title>
            <link>http://www.medworm.com/index.php?rid=5141641&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21849670%26dopt%3DAbstract</link>
            <description>Authors: Rossi AE, Boncompagni S, Wei L, Protasi F, Dirksen RT
    Abstract
    Muscle contraction requires ATP and Ca(2+), and thus, is under direct control of both mitochondria and the sarcoplasmic reticulum. During postnatal skeletal muscle maturation, the mitochondrial network exhibits a shift from a longitudinal (&quot;longitudinal mitochondria&quot;) to a mostly transversal orientation as a result of a progressive increase in mitochondrial association with Ca(2+) release units (CRUs) or triads (&quot;triadic mitochondria&quot;). To determine the physiological implications of this shift in mitochondrial disposition, we monitored activity-dependent changes in myoplasmic (Fluo-4) and mitochondrial Ca(2+) (Rhod-2) with confocal microscopy in single flexor digitorum brevis (FDB) fibers from 1- to 4-month-old...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141641</comments>
            <pubDate>Tue, 16 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141641</guid>        </item>
        <item>
            <title>Vascularizing the tumor: trp channels as molecular targets.</title>
            <link>http://www.medworm.com/index.php?rid=5141655&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21832241%26dopt%3DAbstract</link>
            <description>VASCULARIZING THE TUMOR: TRP CHANNELS AS MOLECULAR TARGETS.
    Am J Physiol Cell Physiol. 2011 Aug 10;
    Authors: Pla AF, Avanzato D, Munaron L, Ambudkar IS
    Abstract
    Tumor vascularization is a critical process that determines tumor growth and metastasis. In the last decade new experimental evidence obtained from in vitro and in vivo studies have challenged the classical angiogenesis model forcing us to consider new scenarios for tumor neovascularization. In particular the genetic stability of tumor-derived endothelial cells (TEC) has been recently questioned in several studies which show that tumor-derived endothelial cells (TECs), as well as pericytes, differ significantly from their normal counterparts at genetic and functional levels. In addition to such an epigenetic action ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141655</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141655</guid>        </item>
        <item>
            <title>Lysophosphatidic acid 5 receptor induces activation of Na+/H+ exchanger 3 via apical epidermal growth factor receptor in intestinal epithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=5141654&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21832242%26dopt%3DAbstract</link>
            <description>Authors: Yoo BK, He P, Lee SJ, Yun CC
    Abstract
    Na+ absorption is a vital process present in all living organisms. We have reported previously that lysophosphatidic acid (LPA) acutely stimulates Na+ and fluid absorption in human intestinal epithelial cells and mouse intestine by stimulation of Na(+)/H(+) exchanger 3 (NHE3) via LPA5 receptor. In the current study, we investigated the mechanism of NHE3 activation by LPA5 in Caco-2bbe cells. LPA5-dependent activation of NHE3 was blocked by mitogen-activated protein kinase kinase (MEK) inhibitor PD98059 and U0126, but not by phosphatidylinositol 3-kinase inhibitor LY294002 or phospholipase C-Î² inhibitor U73122. We found that LPA5 transactivated the epidermal growth factor receptor (EGFR) and inhibition of EGFR blocked LPA5-dependent ac...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141654</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141654</guid>        </item>
        <item>
            <title>Caveolin-2 is a negative regulator of anti-proliferative function and signaling of transforming growth factor beta in endothelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=5141653&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21832243%26dopt%3DAbstract</link>
            <description>Authors: Xie L, Vo-Ransdell C, Abel B, Willoughby C, Jang S, Sowa G
    Abstract
    Using a combination of wild type (WT) and caveolin-2 (Cav-2) knockout along with retroviral re-expression approaches, we provide the evidence for the negative role of Cav-2 in regulating anti-proliferative function and signaling of transforming growth factor beta (TGF-beta) in endothelial cells (ECs). Although, TGF-beta had a modest inhibitory effect on WT ECs, it profoundly inhibited proliferation of Cav-2 knockout ECs. To confirm the specificity of the observed difference in response to TGF-beta, we have stably re-expressed Cav-2 in Cav-2 knockout ECs using a retroviral approach. Similar to WT ECs, the anti-proliferative effect of TGF-beta was dramatically reduced in the Cav-2 re-expressing ECs. The redu...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141653</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141653</guid>        </item>
        <item>
            <title>A novel facet to consider for the effects of butyrate on its target cells: Focus on &quot;The short chain fatty acid butyrate is a substrate of BCRP&quot;</title>
            <link>http://www.medworm.com/index.php?rid=5141652&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21832244%26dopt%3DAbstract</link>
            <description>A novel facet to consider for the effects of butyrate on its target cells: Focus on &quot;The short chain fatty acid butyrate is a substrate of BCRP&quot;
    Am J Physiol Cell Physiol. 2011 Aug 10;
    Authors: Gill RK, Dudeja PK
    Abstract
    Not applicable.
    PMID: 21832244 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141652</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141652</guid>        </item>
        <item>
            <title>Aldosterone stimulates vacuolar H+-ATPase activity in renal acid-secretory intercalated cells mainly via a protein kinase C dependent pathway.</title>
            <link>http://www.medworm.com/index.php?rid=5141651&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21832245%26dopt%3DAbstract</link>
            <description>Authors: Winter C, Kampik NB, Vedovelli L, Rothenberger F, Paunescu TG, Stehberger PA, Brown D, John H, Wagner CA
    Abstract
    Urinary acidification in the collecting duct is mediated by the activity of H(+)-ATPases and is stimulated by various factors including angiotensin II and aldosterone. Classically, aldosterone effects are mediated via the mineralocorticoid receptor. Recently we demonstrated a non-genomic stimulatory effect of aldosterone on H(+)-ATPase activity in acid-secretory intercalated cells of isolated mouse outer medullary collecting ducts (OMCD). Here we investigated the intracellular signalling cascade mediating this stimulatory effect. Aldosterone stimulated H(+)-ATPase activity in isolated mouse and human OMCDs. This effect was blocked by suramin, a general G-protei...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141651</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141651</guid>        </item>
        <item>
            <title>GLYCOGEN SYNTHASE KINASE-3{beta} IS REQUIRED FOR THE INDUCTION OF SKELETAL MUSCLE ATROPHY.</title>
            <link>http://www.medworm.com/index.php?rid=5141650&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21832246%26dopt%3DAbstract</link>
            <description>In conclusion, our data reveals that myotube atrophy and myofibrillar protein loss is GSK-3Î² dependent, and demonstrates for the first time that basal and atrophy stimulus-induced Atrogin-1 mRNA expression requires GSK-3Î² enzymatic activity, whereas MuRF1 expression depends solely on the physical presence of GSK-3Î².
    PMID: 21832246 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141650</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141650</guid>        </item>
        <item>
            <title>Neurokinin 1 receptor desensitization and resensitization: is it all happening at the membrane?</title>
            <link>http://www.medworm.com/index.php?rid=5141649&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21832247%26dopt%3DAbstract</link>
            <description>Authors: Rozengurt E
    Abstract
    not applicable.
    PMID: 21832247 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141649</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141649</guid>        </item>
        <item>
            <title>Physiological and histological changes in skeletal muscle following in vivo gene transfer by electroporation.</title>
            <link>http://www.medworm.com/index.php?rid=5141648&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21832248%26dopt%3DAbstract</link>
            <description>Authors: Roche JA, Ford-Speelman DL, Ru LW, Densmore AL, Roche R, Reed PW, Bloch RJ
    Abstract
    Electroporation (EP) is used to transfect skeletal muscle fibers in vivo, but its effects on the structure and function of skeletal muscle tissue have not yet been documented in detail. We studied the changes in contractile function and histology after EP, and the influence of the individual steps involved, to determine the mechanism of recovery, the extent of myofiber damage, and the efficiency of expression of a green fluorescent protein (GFP) transgene in the tibialis anterior (TA) muscle of adult male C57Bl/6J mice. Immediately after EP, contractile torque decreased by ~ 80% from pre-EP levels. Within 3 hr, torque recovered to ~ 50% but stayed low until day 3. Functional recovery progre...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141648</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141648</guid>        </item>
        <item>
            <title>Enterohemorrhagic Escherichia Coli Infection Stimulates Shiga toxin 1 Macropinocytosis and Transcytosis across Intestinal Epithelial Cells.</title>
            <link>http://www.medworm.com/index.php?rid=5141647&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21832249%26dopt%3DAbstract</link>
            <description>Authors: Lukyanenko V, Malyukova I, Hubbard AL, Delannoy M, Boedeker E, Zhu C, Cebotaru L, Kovbasnjuk O
    Abstract
    Shiga toxins released into the intestinal lumen during enterohemorrhagic Escherichia coli infection, are major virulence factors responsible for gastrointestinal and systemic complications that include hemolytic uremic syndrome, which is fatal in ~10% of patients. However, the molecular mechanisms of Stx endocytosis by enterocytes and the toxin's movement across the epithelia are largely uncharacterized. We have studied Shiga toxin 1entry into enterohemorrhagic Escherichia coli-infected intestinal epithelial cells and found that bacteria stimulate Shiga toxin 1 macropinocytosis through actin remodeling. This enterohemorrhagic Escherichia coli-caused macropinocytosis occu...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141647</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141647</guid>        </item>
        <item>
            <title>Purinergic regulation of high glucose-induced caspase-1 activation in the rMC-1 rat retinal Muller cell line.</title>
            <link>http://www.medworm.com/index.php?rid=5141646&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21832250%26dopt%3DAbstract</link>
            <description>In this study we characterized how elevated glucose and extracellular purines contribute to the activation of caspase-1 in a cultured rat MÃ¼ller cell model (rMC-1). The ability of high glucose (25 mM, 24h) to activate caspase-1 was attenuated by either apyrase, which metabolizes extracellular ATP to AMP, or adenosine deaminase (ADA), which metabolizes extracellular adenosine to inosine. This suggested that autocrine stimulation of ATP-sensing P2 receptors and adenosine-sensing P1 receptors may in part mediate the response to high glucose. Exogenous ATP, 5'-N-ethylcarboxamido-adenosine (NECA), a non-selective P1 receptor agonist, or forskolin increased caspase-1 activity in rMC-1 cells cultured in control glucose (5 mM) medium. Accumulation of active caspase-1 was also increased by dipyrid...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141646</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141646</guid>        </item>
        <item>
            <title>NF-{kappa}B plays an important role in indoxyl sulfate-induced cellular senescence, fibrotic gene expression and inhibition of proliferation in proximal tubular cells.</title>
            <link>http://www.medworm.com/index.php?rid=5141645&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21832251%26dopt%3DAbstract</link>
            <description>Authors: Shimizu H, Bolati D, Adijiang A, Muteliefu G, Enomoto A, Nishijima F, Dateki M, Niwa T
    Abstract
    We previously demonstrated that indoxyl sulfate induces senescence and dysfunction of proximal tubular cells by activating p53 expression. However, little is known about the role of NF-ÎºB in these processes. The present study examines whether activation (phosphorylation) of NF-ÎºB by indoxyl sulfate promotes senescence and dysfunction in human proximal tubular cells (HK-2 cells). Indoxyl sulfate induced phosphorylation of NF-ÎºB p65 on Ser-276, which was suppressed by N-acetylcysteine, an antioxidant. Furthermore, indoxyl sulfate induced NF-ÎºB p65 expression. Inhibitors of NF-ÎºB (pyrrolidine dithiocarbamate and isohelenin) and NF-ÎºB p65 siRNA suppressed indoxyl sulfate-induc...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141645</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141645</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +35 new citations</title>
            <link>http://www.medworm.com/index.php?rid=5104129&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F07%252F24%252011.00%2522%255BMHDA%255D%253A%25222011%252F08%252F07%252018.30%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F07%252F24%252011.00%2522%255BEDAT%255D%29%29</link>
            <description>35 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/08/07PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5104129</comments>
            <pubDate>Sun, 07 Aug 2011 22:30:01 +0100</pubDate>
            <guid isPermaLink="false">5104129</guid>        </item>
        <item>
            <title>Gaba reverse transport by the neuronal cotransporter gat1: influence of internal chloride depletion.</title>
            <link>http://www.medworm.com/index.php?rid=5058164&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21775701%26dopt%3DAbstract</link>
            <description>GABA REVERSE TRANSPORT BY THE NEURONAL COTRANSPORTER GAT1: INFLUENCE OF INTERNAL CHLORIDE DEPLETION.
    Am J Physiol Cell Physiol. 2011 Jul 20;
    Authors: Bertram S, Cherubino F, Bossi E, Castagna M, Peres A
    The role of intracellular ions on the reverse GABA transport by the neuronal transporter GAT1 was studied using voltage-clamp and [(3)H]GABA efflux determinations in Xenopus oocytes transfected with heterologous mRNA. Reverse transport was induced by intracellular GABA injections and measured in terms of the net outward current generated by the transporter. Changes in various intracellular ionic conditions affected the reverse current: higher concentrations of Na(+) enhanced the ratio of outward over inward transport current, while a considerable decrease of the outward current ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058164</comments>
            <pubDate>Tue, 19 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058164</guid>        </item>
        <item>
            <title>Low glucose sensitivity and polymodal chemosensing in neonatal rat adrenomedullary chromaffin cells.</title>
            <link>http://www.medworm.com/index.php?rid=5058163&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21775702%26dopt%3DAbstract</link>
            <description>Authors: Livermore S, Piskuric NA, Buttigieg J, Zhang M, Nurse C
    Glucose is the primary metabolic fuel in mammalian fetuses, yet mammals are incapable of endogenous glucose production until several hours after birth. Thus, when the maternal supply of glucose ceases at birth there is a transient hypoglycemia that elicits a counterregulatory surge in circulating catecholamines. Because the innervation of adrenomedullary chromaffin cells (AMC) is immature at birth, we hypothesized that neonatal AMCs act as direct glucosensors, a property that could complement their previously established roles as hypoxia and acid hypercapnia sensors. During perforated-patch, whole-cell recordings low glucose depolarized and/or excited a subpopulation of neonatal AMCs; in addition, aglycemia (0 mM glucose)...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058163</comments>
            <pubDate>Tue, 19 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058163</guid>        </item>
        <item>
            <title>Kinetics of hyperosmotically-stimulated Na-K-2Cl cotransporter in Xenopus laevis oocytes.</title>
            <link>http://www.medworm.com/index.php?rid=5058162&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21775703%26dopt%3DAbstract</link>
            <description>In this study, we derived the velocity equations for K(+) influx under both rapid equilibrium assumptions and combined equilibrium and steady-state assumptions, and demonstrate that the behavior of the equations and curves in Lineweaver-Burke plots are consistent with a model where Cl(-) binds first, followed by Na(+), a second Cl(-), then K(+). We further demonstrate that stimulation of K(+) movement by K(+) on the trans side is an intrinsic property of a carrier that transports multiple substrates. We also demonstrate that K(+) movement through NKCC1 is strictly dependent upon the presence of external Na(+), even though only a fraction of Na(+) is in fact transported. Finally, we propose that the larger transport of K(+), as compared to Na(+), is a result of translocation of partially-un...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058162</comments>
            <pubDate>Tue, 19 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058162</guid>        </item>
        <item>
            <title>Leukocyte rolling and adhesion via ICAM-1 signals to endothelial permeability.</title>
            <link>http://www.medworm.com/index.php?rid=5058161&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21775704%26dopt%3DAbstract</link>
            <description>Authors: Williams MR, Luscinskas FW
    Editorial Focus.
    PMID: 21775704 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058161</comments>
            <pubDate>Tue, 19 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058161</guid>        </item>
        <item>
            <title>Endothelial-Derived GM-CSF Influence Expression of Oncostatin M.</title>
            <link>http://www.medworm.com/index.php?rid=5058160&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21775705%26dopt%3DAbstract</link>
            <description>This report uses an in vitro model with HUVEC and isolated human neutrophils to examine the effects of two locally-derived cytokines, granulocyte-macrophage stimulating factor (GM-CSF) and colony-stimulating factor (CSF) on oncostatin M (OSM) expression. Neutrophils contacting activated HUVEC expressed and released increased amounts of oncostatin M (OSM), a proinflammatory cytokine known to induce PMN adhesion and chemotaxis. Neutrophil transendothelial migration resulted in three fold higher OSM expression and protein levels compared to non-transmigrated cells. Addition of anti-GM-CSF neutralizing antibody reduced OSM expression level but anti-G-CSF was without effect. GM-CSF but not G-CSF protein addition to cultures of isolated neutrophils resulted in a significant increase in OSM prote...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058160</comments>
            <pubDate>Tue, 19 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058160</guid>        </item>
        <item>
            <title>The short-chain fatty acid butyrate is a substrate of breast cancer resistance protein (BCRP).</title>
            <link>http://www.medworm.com/index.php?rid=5058159&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21775706%26dopt%3DAbstract</link>
            <description>Authors: GonÃ§alves P, GregÃ³rio I, Martel F
    Colorectal cancer is one of the most common cancers worldwide. Butyrate (BT) plays a key role in colonic epithelium homeostasis. The aim of this work was to investigate the possibility of BT being transported by P-glycoprotein (MDR1), multidrug resistance proteins (MRPs) or breast cancer resistance protein (BCRP). Uptake and efflux of (14)C-BT and (3)H-folic acid were measured in Caco-2, IEC-6 and MDA-MB-231 cell lines. mRNA expression of BCRP was detected by RT-PCR. Cell viability, proliferation and differentiation were quantified with the lactate dehydrogenase, sulforhodamine B and alkaline phosphatase activity assays, respectively. In both IEC-6 cells and Caco-2 cells, no evidence was found for the involvement of either MDR1 or MRPs in (1...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058159</comments>
            <pubDate>Tue, 19 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058159</guid>        </item>
        <item>
            <title>Endotoxin transiently inhibits protein synthesis through Akt and MAPK mediating pathways in C2C12 myotubes.</title>
            <link>http://www.medworm.com/index.php?rid=5058158&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21775707%26dopt%3DAbstract</link>
            <description>In conclusion, LPS alone transiently decreased the rate of PS by 50% at 3 hours; this effect is most likely mediated via the TLR4-Akt/mTOR pathway, and both p38 and ERK when inhibited in the presence of LPS at 3 hours have a similar effect in preventing the LPS induced reduction in PS.
    PMID: 21775707 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058158</comments>
            <pubDate>Tue, 19 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058158</guid>        </item>
        <item>
            <title>How uniform is cAMP signaling?</title>
            <link>http://www.medworm.com/index.php?rid=5058157&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21775708%26dopt%3DAbstract</link>
            <description>Authors: Harvey R
    None.
    PMID: 21775708 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058157</comments>
            <pubDate>Tue, 19 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058157</guid>        </item>
        <item>
            <title>Decreased Metalloprotease 9 Induction, Cardiac Fibrosis and Higher Autophagy after Pressure Overload in Mice Lacking the Transcriptional Regulator p8.</title>
            <link>http://www.medworm.com/index.php?rid=5058156&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21775709%26dopt%3DAbstract</link>
            <description>Authors: Georgescu SP, Aronovitz MJ, Iovanna JL, Patten RD, Kyriakis JM, Goruppi S
    Left ventricular remodeling, including the deposition of excess extracellular matrix, is key to the pathogenesis of heart failure. The stress-inducible transcriptional regulator p8 is increased in failing human hearts, and is required both for agonist-stimulated cardiomyocyte hypertrophy and for cardiac fibroblasts MMP9 induction. In the heart, upregulation of autophagy is an adaptive response to stress and plays a causative role in cardiomyopathies. We have recently shown that p8 ablation in cardiac cells upregulates autophagy and that in vivo, loss of p8 results in a decrease of cardiac function. Here we investigated the effects of p8 genetic deletion in mediating adverse myocardial remodeling. Unstres...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058156</comments>
            <pubDate>Tue, 19 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058156</guid>        </item>
        <item>
            <title>Hypoxia Elicits Broad and Systematic Changes in Protein Subcellular Localization.</title>
            <link>http://www.medworm.com/index.php?rid=5058168&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21753182%26dopt%3DAbstract</link>
            <description>Authors: Henke RM, Dastidar RG, Shah AN, Cadinu D, Yao X, Hooda J, Zhang L
    Oxygen provides a crucial energy source in eukaryotic cells. Hence, eukaryotes ranging from yeast to humans have developed sophisticated mechanisms to respond to changes in oxygen levels. Regulation of protein localization, like protein modifications, can be an effective mechanism to control protein function and activity. However, the contribution of protein localization in oxygen signaling has not been examined systematically. Here, we examine how hypoxia affects protein distribution on a genome-wide scale in the model eukaryote, the yeast Saccharomyces cerevisiae. We demonstrate, by live cell imaging, that hypoxia systematically alters the cellular distribution of 203 proteins in yeast. These hypoxia-redistrib...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058168</comments>
            <pubDate>Tue, 12 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058168</guid>        </item>
        <item>
            <title>Structure and development of cochlear afferent innervation in mammals.</title>
            <link>http://www.medworm.com/index.php?rid=5058167&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21753183%26dopt%3DAbstract</link>
            <description>Authors: Defourny J, Lallemend F, Malgrange B
    In mammals, sensorineural deafness results from damage to the auditory receptors of the inner ear, the nerve pathways to the brain or the cortical area that receives sound information. In the present review, we first focused on the cellular and molecular events taking part to spiral ganglion axon growth, extension to the organ of Corti and refinement. In the second half, we considered the functional maturation of synaptic contacts between sensory hair cells and their afferent projections. A better understanding of all these processes could open insights into novel therapeutic strategies aimed to re-establish primary connections from sound transducers to the ascending auditory nerve pathways.
    PMID: 21753183 [PubMed - as supplied by publi...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058167</comments>
            <pubDate>Tue, 12 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058167</guid>        </item>
        <item>
            <title>Rescue of the mutant cftr chloride channel by pharmacological correctors and low temperature analyzed by gene expression profiling.</title>
            <link>http://www.medworm.com/index.php?rid=5058166&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21753184%26dopt%3DAbstract</link>
            <description>RESCUE OF THE MUTANT CFTR CHLORIDE CHANNEL BY PHARMACOLOGICAL CORRECTORS AND LOW TEMPERATURE ANALYZED BY GENE EXPRESSION PROFILING.
    Am J Physiol Cell Physiol. 2011 Jul 13;
    Authors: Sondo E, Tomati V, Caci E, Esposito AI, Pfeffer U, Pedemonte N, Galietta LJ
    The F508del mutation, the most frequent in cystic fibrosis (CF), impairs the maturation of the CFTR chloride channel. The F508del defect can be partially overcome at low temperature (27 Â°C) or with pharmacological correctors. However, the efficacy of correctors on the mutant protein appears to be dependent on the cell expression system. We have used a bronchial epithelial cell line, CFBE41o-, to determine the efficacy of various known treatments and to discover new correctors. Compared to other cell types, CFBE41o- shows the...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058166</comments>
            <pubDate>Tue, 12 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058166</guid>        </item>
        <item>
            <title>The {alpha}7{beta}1 Integrin Accelerates Fiber Hypertrophy and Myogenesis Following a Single Bout of Eccentric Exercise.</title>
            <link>http://www.medworm.com/index.php?rid=5058165&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21753185%26dopt%3DAbstract</link>
            <description>This study provides the first demonstration that the presence of the Î±7Î²1 integrin in skeletal muscle increases fiber hypertrophy and new fiber synthesis in the early time course following a single bout of eccentric exercise. Further studies are necessary to elucidate the precise mechanism by which the Î±7 integrin can enhance muscle hypertrophy following exercise.
    PMID: 21753185 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058165</comments>
            <pubDate>Tue, 12 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058165</guid>        </item>
        <item>
            <title>ABCA1 increases extracellular ATP to mediate cholesterol efflux to apoA-I.</title>
            <link>http://www.medworm.com/index.php?rid=4961931&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21697542%26dopt%3DAbstract</link>
            <description>In this study we analyzed the extracellular ATP levels in the medium of ABCA1-expressing BHK cells and RAW macrophages and compared them to the medium of non-expressing cells. We found that the extracellular ATP concentrations are significantly elevated when cells express ABCA1. Importantly, a dysfunctional ABCA1 mutant (A937V), when expressed similarly as wt ABCA1, is unable to raise extracellular ATP concentration, which suggests a casual relationship between functional ABCA1 and elevated extracellular ATP. To explore the physiological role of extracellular ATP, we analyzed ABCA1-mediated cholesterol efflux under the conditions where extracellular ATP levels were modulated. We found that increasing extracellular ATP within the physiological range, i.e. &amp;lt; Î¼M, promotes cholesterol effl...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4961931</comments>
            <pubDate>Tue, 21 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4961931</guid>        </item>
        <item>
            <title>Large conductance voltage- and Ca2+-activated K+ channels regulate human detrusor smooth muscle function.</title>
            <link>http://www.medworm.com/index.php?rid=4961930&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21697543%26dopt%3DAbstract</link>
            <description>Authors: Hristov KL, Chen M, Kellett WF, Rovner ES, Petkov GV
    The large conductance voltage- and Ca(2+)-activated K(+) (BK) channel is expressed in many smooth muscle types, but its role in human detrusor smooth muscle (DSM) is unclear. With a multidisciplinary approach spanning channel molecules, single-channel activity, freshly isolated human DSM cells, intact DSM preparations, and the BK channel specific inhibitor, iberiotoxin, we elucidated human DSM BK channel function and regulation. Native human DSM tissues were obtained during open surgeries from patients with no preoperative history of overactive bladder. RT-PCR experiments on single human DSM cells showed mRNA expression of BK channel Î±Î±, Î²1, and Î²4 subunits. Western blot and immunocytochemistry confirmed BK channel Î±, Î...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4961930</comments>
            <pubDate>Tue, 21 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4961930</guid>        </item>
        <item>
            <title>Enhanced Ca2+ Transport and muscle relaxation in skeletal muscle from sarcolipin-null mice.</title>
            <link>http://www.medworm.com/index.php?rid=4961929&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21697544%26dopt%3DAbstract</link>
            <description>Authors: Tupling AR, Bombardier E, Gupta SC, Hussain D, Vigna C, Bloemberg D, Quadrilatero J, Trivieri MG, Babu GJ, Backx PH, Periasamy M, Maclennan DH, Gramolini AO
    Sarcolipin (SLN) inhibits SERCA pumps. To evaluate the physiological significance of SLN in skeletal muscle, we compared muscle contractility and SERCA activity between Sln-null and wild type mice. SLN protein expression in wild type mice was abundant in soleus and red gastrocnemius (RG), low in extensor digitorum longus (EDL) and absent from white gastrocnemius (WG). SERCA activity rates were increased in soleus and RG, but not in EDL or WG, from Sln-null muscles, compared to wild type. No differences were seen between wild type and Sln-null EDL muscles in force-frequency curves or maximum rates of force development (+dF/...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4961929</comments>
            <pubDate>Tue, 21 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4961929</guid>        </item>
        <item>
            <title>Deficiency of Prdx6 in lens epithelial cells induces ER stress-response-mediated impaired homeostasis and apoptosis.</title>
            <link>http://www.medworm.com/index.php?rid=4961936&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21677259%26dopt%3DAbstract</link>
            <description>Authors: Fatma N, Singh P, Chhunchha B, Kubo E, Shinohara T, Bhargavan B, Singh DP
    The multifunctional cytoprotective protein Peroxiredoxin 6 (Prdx6) maintains cellular homeostasis and membrane integrity by regulating expression of intracellular reactive oxygen species (ROS) and phospholipid turnover. Using cells derived from targeted inactivation of Prdx6 gene or its depletion by RNA interference or aging, we showed that Prdx6 deficiency in cells evoked unfolded protein response (UPR), evidenced by increased expression or activation of proapoptotic factors, CHOP, ATF4, PERK, IRE-Î± and eIF2-Î± and by increased caspases 3 and 12 processing. Those cells displayed enhanced and sustained expression of endoplasmic reticulum (ER) stress related chaperon proteins, Bip/GRP78, calnexin and cal...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4961936</comments>
            <pubDate>Tue, 14 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4961936</guid>        </item>
        <item>
            <title>Gap junctions favor normal rat kidney epithelial cell adaptation to chronic hypertonicity.</title>
            <link>http://www.medworm.com/index.php?rid=4961935&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21677260%26dopt%3DAbstract</link>
            <description>GAP JUNCTIONS FAVOR NORMAL RAT KIDNEY EPITHELIAL CELL ADAPTATION TO CHRONIC HYPERTONICITY.
    Am J Physiol Cell Physiol. 2011 Jun 15;
    Authors: Desforges B, Savarin P, Bounedjah O, Delga S, Hamon L, Curmi PA, Pastre D
    Upon hypertonic stress most often resulting from high salinity, cells need to balance their osmotic pressure by accumulating neutral osmolytes called compatible osmolytes like betaine, myo-inositol and taurine. However the massive uptake of compatible osmolytes is a slow process, compared to other defense mechanisms related to oxidative or heat stress. This is especially critical for cycling cells as they have to double their volume while keeping a hospitable intracellular environment for the molecular machineries. Here we propose that clustered cells can accelerate t...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4961935</comments>
            <pubDate>Tue, 14 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4961935</guid>        </item>
        <item>
            <title>Crosstalk Between Oxygen Sensing and the Cell Cycle Machinery.</title>
            <link>http://www.medworm.com/index.php?rid=4961934&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21677261%26dopt%3DAbstract</link>
            <description>Authors: Semenza GL
    A fundamental physiological property of mammalian cells is the regulation of proliferation according to O(2) availability. Progression through the cell cycle is inhibited under hypoxic conditions in many, but not all, cell types and this G1 arrest is dependent on hypoxia-inducible factor (HIF) 1Î±. Components of the hexameric MCM helicase, which binds to replication origins prior to the onset of DNA synthesis, are present in large excess in mammalian cells relative to origins, suggesting that they may have additional functions. Screens for HIF-1Î± interacting proteins revealed that MCM7 binds to the amino-terminal PAS domain of HIF-1Î± and stimulates prolyl hydroxylation-dependent ubiquitination and degradation of HIF-1Î±, whereas MCM3 binds to the carboxyl terminus...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4961934</comments>
            <pubDate>Tue, 14 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4961934</guid>        </item>
        <item>
            <title>A Molecular Formula for Heart Failure and Sudden Cardiac Death.</title>
            <link>http://www.medworm.com/index.php?rid=4961933&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21677262%26dopt%3DAbstract</link>
            <description>Authors: Kaczorowski GJ
    NA.
    PMID: 21677262 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4961933</comments>
            <pubDate>Tue, 14 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4961933</guid>        </item>
        <item>
            <title>Nav1.5-dependent persistent Na+ influx activates CaMKII in rat ventricular myocytes and N1325S mice.</title>
            <link>http://www.medworm.com/index.php?rid=4961932&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21677263%26dopt%3DAbstract</link>
            <description>Authors: Yao L, Fan P, Jiang Z, Viatchenko-Karpinski S, Wu Y, Kornyeyev D, Hirakawa R, Budas GR, Rajamani S, Shryock JC, Belardinelli L
    Late Na(+) current (INaL) and CaMKII are both increased in the diseased heart. Recently, CaMKII was found to phosphorylate the Na(+) channel 1.5 (Na(v)1.5), resulting in enhanced I(NaL). Conversely, an increase of I(NaL) would be expected to cause elevation of intracellular Ca(2+) and activation of CaMKII. However, a relationship between enhancement of INaL and activation of CaMKII has yet to be demonstrated. We investigated whether Na(+) influx via Na(v)1.5 leads to CaMKII activation and explored the functional significance of this pathway. In neonatal rat ventricular myocytes (NRVM), treatment with the I(NaL) activators anemone toxin II (ATX-II) or v...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4961932</comments>
            <pubDate>Tue, 14 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4961932</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +19 new citations</title>
            <link>http://www.medworm.com/index.php?rid=4912729&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F05%252F27%252003.30%2522%255BMHDA%255D%253A%25222011%252F06%252F10%252007.30%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F05%252F27%252003.30%2522%255BEDAT%255D%29%29</link>
            <description>19 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/06/10PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4912729</comments>
            <pubDate>Fri, 10 Jun 2011 11:30:09 +0100</pubDate>
            <guid isPermaLink="false">4912729</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +38 new citations</title>
            <link>http://www.medworm.com/index.php?rid=4866031&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F05%252F12%252012.30%2522%255BMHDA%255D%253A%25222011%252F05%252F27%252003.30%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F05%252F12%252012.30%2522%255BEDAT%255D%29%29</link>
            <description>38 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/05/27PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4866031</comments>
            <pubDate>Fri, 27 May 2011 07:30:02 +0100</pubDate>
            <guid isPermaLink="false">4866031</guid>        </item>
        <item>
            <title>Unforeseen decreases in dissolved oxygen levels affect tube formation kinetics in collagen gels.</title>
            <link>http://www.medworm.com/index.php?rid=4814193&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21543738%26dopt%3DAbstract</link>
            <description>This study is the first demonstration of the critical and unexpected role of O(2) during 3D in vitro culture models of tubulogenesis in atmospheric conditions.
    PMID: 21543738 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814193</comments>
            <pubDate>Tue, 03 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814193</guid>        </item>
        <item>
            <title>Dual functional significance of Calcineurin homologous protein 1 (CHP1) binding to Na+/H+ exchanger isoform 1 (NHE1).</title>
            <link>http://www.medworm.com/index.php?rid=4814190&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21543739%26dopt%3DAbstract</link>
            <description>Authors: Matsushita M, Tanaka H, Mitsui K, Kanazawa H
    Calcineurin Homologous Protein 1 (CHP1) binds to the hydrophilic tail of the Na(+)/H(+) exchanger isoform 1 (NHE1). Previous gene-knockout of CHP1 revealed that the loss of CHP1 caused a decrease in the total amount of NHE1, suggesting the destabilization of NHE1 molecules without CHP1 (Am.J.Physiol.Cell.Physiol. (2007) 293(1), C246-). However, Pang et al (J.Biol.Chem. (2001) 276, 17367-) reported that NHE1 without a CHP1 binding site was found in the plasma membrane, suggesting no requirement of CHP1 binding for plasma membrane localization of NHE1. Here, the functional significance of CHP1 binding to NHE1 was examined to resolve these contradictory results. In CV1 cells, which overexpressed wild-type NHE1, overexpression of CHP1 c...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814190</comments>
            <pubDate>Tue, 03 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814190</guid>        </item>
        <item>
            <title>Ion Channels and the Control of Cancer Cell Migration.</title>
            <link>http://www.medworm.com/index.php?rid=4814188&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21543740%26dopt%3DAbstract</link>
            <description>Authors: Cuddapah VA, Sontheimer H
    A hallmark of high-grade cancers is the ability of malignant cells to invade unaffected tissue and spread disease. This is particularly apparent in gliomas, the most common and lethal type of primary brain cancer affecting adults. Migrating cells encounter restricted spaces and appear able to adjust their shape to accommodate to narrow extracellular spaces. A growing body of work suggests that cell migration/invasion is facilitated by ion channels and transporters. The emerging concept is that K(+) and Cl(-) function as osmotically active ions, which cross the plasma membrane in concert with obligated water thereby adjusting a cell's shape and volume. In glioma cells NKCC1 transporters actively accumulate K(+) and Cl(-) , establishing a gradient for K...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814188</comments>
            <pubDate>Tue, 03 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814188</guid>        </item>
        <item>
            <title>Rho Rocks H+-ATPases.</title>
            <link>http://www.medworm.com/index.php?rid=4814182&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21543741%26dopt%3DAbstract</link>
            <description>Authors: Wagner CA
    N/A.
    PMID: 21543741 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814182</comments>
            <pubDate>Tue, 03 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814182</guid>        </item>
        <item>
            <title>An Intramolecular Transport Metabolon: Fusion of Carbonic Anhydrase II to the C-terminus of the Cl-/HCO3- Exchanger, AE1.</title>
            <link>http://www.medworm.com/index.php?rid=4814181&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21543742%26dopt%3DAbstract</link>
            <description>Authors: Sowah D, Casey JR
    AE1 is the plasma membrane Cl(-)/HCO(3)(-) exchanger of erythrocytes. Carbonic anhydrases (CA) provide substrate for AE1 by catalyzing the reaction, H(2)O+CO(2)â†”HCO(3)(-)+H(+). The physical complex of CAII with AE1 has been proposed to maximize anion exchange activity. To examine the effect of CAII catalysis on AE1 transport rate, we fused either CAII-wildtype or catalytically-inactive CAII-V143Y to the cytoplasmic C-terminus of AE1, to form AE1.CAII and AE1.CAII-V143Y, respectively. When expressed in transfected HEK293 cells, AE1.CAII had a similar Cl(-)/HCO(3)(-) exchange activity to AE1 alone, as assessed by the flux of H(+) equivalents (87Â±4% versus AE1) or rate of change of intracellular [Cl(-)] (93Â±4% versus AE1), suggesting that CAII does not activ...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814181</comments>
            <pubDate>Tue, 03 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814181</guid>        </item>
        <item>
            <title>Cholinergic and glutamatergic agonists induce gamma frequency activity in dorsal subcoeruleus nucleus neurons s.</title>
            <link>http://www.medworm.com/index.php?rid=4814178&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21543743%26dopt%3DAbstract</link>
            <description>Authors: Simon C, Kezunovic N, Williams DK, Urbano FJ, Garcia-Rill E
    The dorsal subcoeruleus nucleus (SubCD) is involved in generating two signs of REM sleep: muscle atonia and ponto-geniculo-occipital (PGO) waves. We tested the hypothesis that single cell and/or population responses of SubCD neurons are capable of generating gamma frequency activity in response to intracellular stimulation or receptor agonist activation. Whole-cell patch clamp recordings (immersion chamber) and population responses (interface chamber) were conducted on 9-20 days old rat brainstem slices. All SubCD neurons (n=103) fired at gamma frequency when subjected to depolarizing steps. Two statistically distinct populations of neurons were observed, which were distinguished by their high (&amp;gt;80 Hz, n=24) vs. lo...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814178</comments>
            <pubDate>Tue, 03 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814178</guid>        </item>
        <item>
            <title>Paving new paths for neuregulin-1-assisted cardiac regenerative medicine.</title>
            <link>http://www.medworm.com/index.php?rid=4814176&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21543744%26dopt%3DAbstract</link>
            <description>Authors: Lemmens K, De Keulenaer GW
    N/A.
    PMID: 21543744 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814176</comments>
            <pubDate>Tue, 03 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814176</guid>        </item>
        <item>
            <title>NP603, a novel and potent inhibitor of FGFR1 tyrosine kinase, inhibits hepatic stellate cell proliferation and ameliorates hepatic fibrosis in rats.</title>
            <link>http://www.medworm.com/index.php?rid=4814175&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21543745%26dopt%3DAbstract</link>
            <description>Authors: Lin N, Chen S, Pan W, Xu L, Hu K, Xu R
    Background/Aims: Fibroblast growth factor 2 (FGF-2) and its main receptor FGFR1 have been shown to promote hepatic stellate cell (HSC) activation and proliferation. However, scant information is available on the anti-fibrogenic activity of FGFR1 inhibitors. The aim of this study was to assess the impact of a selective FGFR1 tyrosine kinase inhibitor NP603 on HSC proliferation and hepatic fibrosis. We demonstrated that rat primary HSCs secreted significant amounts of FGF-2, and its tyrosine phosphorylation of FGFR1 was attenuated by NP603. NP603 inhibited HSC activaton by measuring the expression of Î±-smooth muscle actin (Î±-SMA) and the production of type I collagen using ELISA. Furthermore, NP603 (25 Î¼M) in vitro strongly suppressed HS...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814175</comments>
            <pubDate>Tue, 03 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814175</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +48 new citations</title>
            <link>http://www.medworm.com/index.php?rid=4759999&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F03%252F29%252023.30%2522%255BMHDA%255D%253A%25222011%252F04%252F28%252014.00%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F03%252F29%252023.30%2522%255BEDAT%255D%29%29</link>
            <description>48 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/04/28PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4759999</comments>
            <pubDate>Thu, 28 Apr 2011 18:00:02 +0100</pubDate>
            <guid isPermaLink="false">4759999</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +26 new citations</title>
            <link>http://www.medworm.com/index.php?rid=4652014&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F03%252F15%252011.45%2522%255BMHDA%255D%253A%25222011%252F03%252F29%252023.30%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F03%252F15%252011.45%2522%255BEDAT%255D%29%29</link>
            <description>26 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/03/29PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4652014</comments>
            <pubDate>Wed, 30 Mar 2011 03:30:02 +0100</pubDate>
            <guid isPermaLink="false">4652014</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +27 new citations</title>
            <link>http://www.medworm.com/index.php?rid=4583168&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F02%252F15%252002.15%2522%255BMHDA%255D%253A%25222011%252F03%252F15%252011.45%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F02%252F15%252002.15%2522%255BEDAT%255D%29%29</link>
            <description>27 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/03/15PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583168</comments>
            <pubDate>Tue, 15 Mar 2011 15:45:02 +0100</pubDate>
            <guid isPermaLink="false">4583168</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +53 new citations</title>
            <link>http://www.medworm.com/index.php?rid=4476175&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222011%252F01%252F29%252002.45%2522%255BMHDA%255D%253A%25222011%252F02%252F15%252002.15%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222011%252F01%252F29%252002.45%2522%255BEDAT%255D%29%29</link>
            <description>53 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/02/15PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4476175</comments>
            <pubDate>Tue, 15 Feb 2011 07:15:06 +0100</pubDate>
            <guid isPermaLink="false">4476175</guid>        </item>
        <item>
            <title>Temporal and spatial patterns of endogenous danger signal expression after wound healing and in response to lymphedema.</title>
            <link>http://www.medworm.com/index.php?rid=4411878&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21248077%26dopt%3DAbstract</link>
            <description>In conclusion, HMGB1 and HSP70 are expressed along spatial gradients and upregulated in chronic lymphatic fluid stasis; furthermore, acute expression of endogenous danger signals may play a role in inflammatory lymphangiogenesis.
    PMID: 21248077 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411878</comments>
            <pubDate>Wed, 19 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4411878</guid>        </item>
        <item>
            <title>Wnt4 Activates the Canonical {beta}-Catenin Pathway and Regulates Negatively Myostatin: Functional Implication in Myogenesis.</title>
            <link>http://www.medworm.com/index.php?rid=4411877&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21248078%26dopt%3DAbstract</link>
            <description>Authors: Bernardi H, Gay S, Fedon Y, Vernus B, Bonnieu A, Bacou F
    Expression of Wnt proteins is known to be important for developmental processes such as embryonic pattern formation and determination of cell fate. Previous studies have shown that Wn4 was involved in the myogenic fate of somites, in the myogenic proliferation and differentiation of skeletal muscle. However, the function of this factor in adult muscle homeostasis remains not well understood. Here, we focus on the roles of Wnt4 during C2C12 myoblasts and satellite cells differentiation. We analysed its myogenic activity, its mechanism of action and its interaction with the anti-myogenic factor myostatin during differentiation. Established expression profiles indicate clearly that both types of cells express a few Wnts and...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411877</comments>
            <pubDate>Wed, 19 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4411877</guid>        </item>
        <item>
            <title>The Small GTPase Rab11b Regulates Degradation of Surface Membrane L-Type Cav1.2 Channels.</title>
            <link>http://www.medworm.com/index.php?rid=4411876&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21248079%26dopt%3DAbstract</link>
            <description>Authors: Best JM, Foell JD, Buss CR, Delisle BP, Balijepalli RC, January CT, Kamp TJ
    L-type Ca(2+) channels (LTCCs) play a critical role in Ca(2+)-dependent signaling processes in a variety of cell types. The number of functional LTCCs at the plasma membrane strongly influences the strength and duration of Ca(2+) signals. Recent studies demonstrated that endosomal trafficking provides a mechanism for dynamic changes in LTCC surface membrane density. The purpose of the current study was to determine whether the small GTPase Rab11b, a known regulator of endosomal recycling, impacts plasmalemmal expression of Ca(v)1.2 LTCCs. Disruption of endogenous Rab11b function with a dominant negative Rab11b S25N mutant led to a significant 64% increase in peak L-type Ba(2+) current (I(Ba,L)) in HEK2...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411876</comments>
            <pubDate>Wed, 19 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4411876</guid>        </item>
        <item>
            <title>Beyond Translation: The Renal Phosphate Census Focus on &quot;Large-Scale Phosphoproteomic Analysis of Membrane Proteins in Renal Proximal and Distal Tubule&quot;</title>
            <link>http://www.medworm.com/index.php?rid=4411875&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21248080%26dopt%3DAbstract</link>
            <description>Beyond Translation: The Renal Phosphate Census Focus on &quot;Large-Scale Phosphoproteomic Analysis of Membrane Proteins in Renal Proximal and Distal Tubule&quot;
    Am J Physiol Cell Physiol. 2011 Jan 19;
    Authors: Pluznick JL
    na.
    PMID: 21248080 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411875</comments>
            <pubDate>Wed, 19 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4411875</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +69 new citations</title>
            <link>http://www.medworm.com/index.php?rid=4346554&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222010%252F12%252F22%252017.30%2522%255BMHDA%255D%253A%25222011%252F01%252F14%252013.45%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222010%252F12%252F22%252017.30%2522%255BEDAT%255D%29%29</link>
            <description>69 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2011/01/14PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4346554</comments>
            <pubDate>Fri, 14 Jan 2011 18:45:02 +0100</pubDate>
            <guid isPermaLink="false">4346554</guid>        </item>
        <item>
            <title>Am J Physiol Cell Physiol; +58 new citations</title>
            <link>http://www.medworm.com/index.php?rid=4279695&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fsites%2Fentrez%3Fcmd%3DSearch%26db%3Dpubmed%26term%3D%28%28%28Am%2520J%2520Physiol%2520Cell%2520Physiol%29%2520AND%2520%25222010%252F12%252F13%252004.00%2522%255BMHDA%255D%253A%25222010%252F12%252F22%252017.30%2522%255BMHDA%255D%29%29%2520NOT%2520%28%28%2520%28%28%28%2522Am%2520J%2520Physiol%2520Cell%2520Physiol%2522%255BTIAB%255D%29%29%29%2520AND%2520%25220001%2522%255BEDAT%255D%253A%25222010%252F12%252F13%252004.00%2522%255BEDAT%255D%29%29</link>
            <description>58 new pubmed citations were retrieved for your search.
Click on the search hyperlink below to display the complete search results:

Am J Physiol Cell Physiol
These pubmed results were generated on 2010/12/22PubMed, a service of the National Library of Medicine, includes over 15 million 
citations for biomedical articles back to the 1950's.
These citations are from MEDLINE and additional life science journals. 
PubMed includes links to many sites providing full text articles and other related resources. (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4279695</comments>
            <pubDate>Wed, 22 Dec 2010 22:30:02 +0100</pubDate>
            <guid isPermaLink="false">4279695</guid>        </item>
        <item>
            <title>Biophysical Properties of Normal and Diseased Renal Glomeruli.</title>
            <link>http://www.medworm.com/index.php?rid=4252292&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21123730%26dopt%3DAbstract</link>
            <description>Authors: Wyss HM, Henderson JM, Byfield FJ, Bruggeman LA, Ding Y, Huang C, Suh JH, Franke T, Mele E, Pollak MR, Miner JH, Janmey PA, Weitz DA, Miller RT
    The mechanical properties of tissues and cells including renal glomeruli are important determinants of their differentiated state, function, and responses to injury, but are not well characterized or understood. Understanding glomerular mechanics is important for understanding renal diseases attributable to abnormal expression or assembly of structural proteins and abnormal hemodynamics. We use atomic force microscopy (AFM) and a new technique, capillary micromechanics, to measure the elastic properties of rat glomeruli. The Young's modulus of glomeruli was 2,500 Pa, and it was reduced to 1,100 Pa by cytochalasin and latunculin, and to...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252292</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252292</guid>        </item>
        <item>
            <title>Chronically elevated glucose compromises myocardial mitochondrial DNA (mtDNA) integrity by alteration of mitochondrial topoisomerase function.</title>
            <link>http://www.medworm.com/index.php?rid=4252291&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21123731%26dopt%3DAbstract</link>
            <description>Authors: Medikayala S, Piteo B, Zhao X, Edwards JG
    Mitochondrial dysfunction has a significant role in the development and complications of diabetic cardiomyopathy. Mitochondrial dysfunction and mitochondrial DNA (mtDNA) mutations are also associated with different types of cancer and neurodegenerative diseases. The goal of this study was to determine if chronically elevated glucose increase in mtDNA damage contributed to mitochondrial dysfunction and identify the underlying basis for mtDNA damage. H9c2 myotubes (a cardiac-derived cell line) were studied in the presence of 5.5, 16.5, or 33.0 mM glucose for up to 13 days. Tests of mitochondria function (Complex I &amp; IV activity and ATP generation) were all significantly depressed by elevated media glucose. Intramitochondrial superoxi...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252291</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252291</guid>        </item>
        <item>
            <title>Increased matriptase zymogen activation in inflammatory skin disorders.</title>
            <link>http://www.medworm.com/index.php?rid=4252290&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21123732%26dopt%3DAbstract</link>
            <description>Authors: Chen CJ, Wu BY, Tsao PI, Chen CY, Wu MH, Chan YL, Lee HS, Johnson MD, Eckert RL, Chen YW, Chou F, Wang JK, Lin CY
    Matriptase, a type 2 transmembrane serine protease, and its inhibitor hepatocyte growth factor activator inhibitor (HAI)-1 are required for normal epidermal barrier function, and matriptase activity is tightly regulated during this process. Given that abnormal matriptase function has been demonstrated to cause skin dysfunction, we hypothesized that matriptase deregulation may be associated with skin disease. To test this, we examined the level and activation state of matriptase in twenty-three human skin disorders. We first examined matriptase and HAI-1 protein distirubtion in normal epidermis. Matriptase was detected at high levels at cell-cell junctions in the ba...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252290</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252290</guid>        </item>
        <item>
            <title>Hypoxia regulates Cell Metabolism.</title>
            <link>http://www.medworm.com/index.php?rid=4252289&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21123733%26dopt%3DAbstract</link>
            <description>Authors: Wheaton WW, Chandel NS
    Adaptation to lowering oxygen levels (hypoxia) requires coordinated down-regulation of metabolic demand and supply to prevent a mismatch in ATP utilization and production that might culminate in a bioenergetic collapse. Hypoxia diminishes ATP utilization by down-regulating protein translation and the activity of the Na/K-ATPase. Hypoxia diminishes ATP production in part by lowering the activity of the electron transport chain through activation of the transcription factor HIF-1. The decrease in electron transport limits the overproduction of ROS during hypoxia and slows the rate of oxygen depletion to prevent anoxia. In this review, we discuss these mechanisms that diminish metabolic supply and demand for adaptation to hypoxia.
    PMID: 21123733 [PubMed...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252289</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252289</guid>        </item>
        <item>
            <title>Nox4 NADPH oxidase-derived reactive oxygen species, via endogenous carbon monoxide, promote survival of brain endothelial cells during TNF-{alpha}-induced apoptosis.</title>
            <link>http://www.medworm.com/index.php?rid=4252288&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21123734%26dopt%3DAbstract</link>
            <description>We present the data demonstrating that the Nox4 NADPH oxidase-derived ROS also initiate a cell survival mechanism by increasing production of a gaseous antioxidant mediator, carbon monoxide (CO), by constitutive heme oxygenase-2 (HO-2). TNF-Î± rapidly enhanced endogenous CO production in a superoxide- and NADPH oxidase-dependent manner in CMVEC with innate but not with siRNA-downregulated Nox4 activity. A CO-releasing molecule, CORM-A1, selectively inhibited Nox4-mediated ROS production and enhanced cell survival in TNF-Î±-challenged CMVEC. The ROS-induced CO-mediated survival mechanism requires functional interactions between the protein kinase B/Akt and ERK/p38 MAP kinase signaling pathways activated by TNF-Î±. In Akt siRNA-transfected CMVEC, as well as in cells with pharmacologically in...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252288</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252288</guid>        </item>
        <item>
            <title>Soluble adenylyl cyclase mediates bicarbonate -dependent corneal endothelial cell protection.</title>
            <link>http://www.medworm.com/index.php?rid=4252287&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21123735%26dopt%3DAbstract</link>
            <description>We examined the effects of HCO(3)(-), pH, PDE4 inhibition by rolipram, sAC inhibition by 2HE (2-hydroxyestradiol), and sAC siRNA knockdown on basal and staurosporine mediated apoptosis. 40 mM HCO(3)(-) or 50 Î¼M rolipram raised [cAMP] to similar levels and protected endothelial cells by 50% relative to a bicarbonate-free control, whereas 2HE, which decreased [cAMP] by 40%, and H89 (PKA inhibitor) doubled the apoptotic rate. sAC expression was reduced by two-thirds in the absence of HCO(3)(-), and was reduced to 15% of control by sAC siRNA. Protection by HCO(3)(-) was eliminated in siRNA treated cells. Similarly, caspase 3 activity and cytochrome c release were reduced by HCO(3)(-) and enhanced by 2HE or siRNA. Analysis of % AnnexinV+ cells as a function of [cAMP] revealed an inverse, non-l...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252287</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252287</guid>        </item>
        <item>
            <title>Anion exchanger 1b, but not sodium-bicarbonate cotransporter 1b, plays a role in transport functions of zebrafish H+-ATPase-rich cells.</title>
            <link>http://www.medworm.com/index.php?rid=4252286&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21123736%26dopt%3DAbstract</link>
            <description>Authors: Lee YC, Yan JJ, Cruz S, Horng JL, Hwang PP
    Similar to mammalian proximal tubular cells, H(+)-ATPase rich (HR) cells in zebrafish skin and gills are also responsible for Na+ uptake and acid secretion functions. However, the basolateral transport pathways in HR cells are still unclear. In the present study, we tested the hypothesis if there are specific slc4 members involved in basolateral ion transport pathways in HR cells. Fourteen isoforms were identified in the zebrafish(z) slc4 family, and the full-length cDNAs of two novel isoforms, zslc4a1b (anion exchanger, zAE1b) and zslc4a4a (Na+/HCO3- cotransporter, zNBCe1b), were sequenced. mRNA signals of zslc4a1b and zslc4a4a were mainly detected in certain groups of ionocytes in zebrafish skin/gills. Further double immunocytochemi...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252286</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252286</guid>        </item>
        <item>
            <title>Sca-1 influences the innate immune response during skeletal muscle regeneration.</title>
            <link>http://www.medworm.com/index.php?rid=4252285&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21123737%26dopt%3DAbstract</link>
            <description>Authors: Long KK, Pavlath GK, Montano M
    Efficient muscle regeneration requires the clearance of dead and dying tissue via phagocytosis prior to remodeling. We have previously shown that mice lacking Sca-1 (Stem Cell Antigen-1) display a defect in skeletal muscle regeneration characterized by increased fibrosis and decreased turnover of the extracellular matrix. In the present study we demonstrate that Sca-1(-/-) mice have a defect in their capacity to recruit soluble IgM, and subsequently C3 complement, to damaged muscle. We hypothesize that this defect in recruitment delays or decreases phagocytosis by macrophages, contributing to the previously observed fibrotic phenotype of these mice. As the primary source of soluble IgM is peritoneal B-1a cells, which are a subset of self-renewing...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252285</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252285</guid>        </item>
        <item>
            <title>Calcium Activated K+ Channels Increase Cell Proliferation Independent of K+ Conductance.</title>
            <link>http://www.medworm.com/index.php?rid=4252284&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21123738%26dopt%3DAbstract</link>
            <description>Authors: Millership JE, Devor DC, Hamilton KL, Balut CM, Bruce JI, Fearon IM
    The intermediate conductance calcium-activated potassium channel (IK1) promotes cell proliferation of numerous cell types including endothelial cells, T lymphocytes and several cancer cell lines. The mechanism underlying IK1-mediated cell proliferation was examined in HEK293 cells expressing recombinant human IK1 (hIK1) channels. Inhibition of hIK1 with TRAM-34 reduced cell proliferation, while expression of hIK1 in HEK293 cells increased proliferation. When HEK293 cells were transfected with a mutant (GYG/AAA) hIK1 channel, which neither conducts K(+) ions nor promotes Ca(2+) entry, proliferation was increased relative to mock-transfected cells. Furthermore, when HEK293 cells were transfected with a trafficki...</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252284</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252284</guid>        </item>
        <item>
            <title>Placenta growth factor expression is regulated by hydrogen peroxide in vascular smooth muscle cells.</title>
            <link>http://www.medworm.com/index.php?rid=4252283&amp;cid=s_30452_171_f&amp;fid=30452&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21123739%26dopt%3DAbstract</link>
            <description>In this study, we demonstrate that EC-released H(2)O(2) acts as a positive regulator of PLGF gene and protein expression in vascular SMC. To our knowledge, this is the first study to describe H(2)O(2) as a regulator of PLGF expression and therefore an upstream mediator of PLGF-driven arteriogenesis.
    PMID: 21123739 [PubMed - as supplied by publisher] (Source: Am J Physiol Cell Ph...)</description>
            <author>Am J Physiol Cell Ph...</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252283</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252283</guid>        </item>
    </channel>
</rss>

