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10.1152/ajprenal.00030.2010 http://scihub22266oqcxt.onion/10.1152/ajprenal.00030.2010 C5510016!5510016 !20335315     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=20335315 &cmd=llinks): Failed to open stream: HTTP request failed! 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CLIC5A, a component of the ezrin-podocalyxin complex in glomeruli, is a determinant of podocyte integrity |pdf=|usr=}}{{20335315 }} gab.com Text CLIC5A, a component of the ezrin-podocalyxin complex in glomeruli, is a determinant of podocyte integrity JO: Am J Physiol Renal Physiol http://www.kidney.de/pget.php?&tw=1&pmid=20335315 #FOAvip The chloride intracellular channel 5A (CLIC5A) protein, one of two isoforms produced by the CLIC5 gene, was isolated originally as part of a cytoskeletal protein complex containing ezrin from placental microvilli. Whether CLIC5A functions as a bona fide ion channel is controversial. We reported previously that a CLIC5 transcript is enriched approximately 800-fold in human renal glomeruli relative to most other tissues. Therefore, this study sought to explore CLIC5 expression and function in glomeruli. RT-PCR and Western blots show that CLIC5A is the predominant CLIC5 isoform expressed in glomeruli. Confocal immunofluorescence and immunogold electron microscopy reveal high levels of CLIC5A protein in glomerular endothelial cells and podocytes. In podocytes, CLIC5A localizes to the apical plasma membrane of foot processes, similar to the known distribution of podocalyxin and ezrin. Ezrin and podocalyxin colocalize with CLIC5A in glomeruli, and podocalyxin coimmunoprecipitates with CLIC5A from glomerular lysates. In glomeruli of jitterbug (jbg/jbg) mice, which lack the CLIC5A protein, ezrin and phospho-ERM levels in podocytes are markedly lower than in wild-type mice. Transmission electron microscopy reveals patchy broadening and effacement of podocyte foot processes as well as vacuolization of glomerular endothelial cells. These ultrastructural changes are associated with microalbuminuria at baseline and increased susceptibility to adriamycin-induced glomerular injury compared with wild-type mice. Together, the data suggest that CLIC5A is required for the development and/or maintenance of the proper glomerular endothelial cell and podocyte architecture. We postulate that the interaction between podocalyxin and subjacent filamentous actin, which requires ezrin, is compromised in podocytes of CLIC5A-deficient mice, leading to dysfunction under unfavorable genetic or environmental conditions. Twit Text FOAVip CLIC5A, a component of the ezrin-podocalyxin complex in glomeruli, is a determinant of podocyte integrity ????Am J Physiol Renal Physiol http://www.kidney.de/pget.php?&tw=1&pmid=20335315 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=20335315 #FOAvip English Wikipedia <ref>{{Cite pmid|20335315 }}</ref> CLIC5A, a component of the ezrin-podocalyxin complex in glomeruli, is a determinant of podocyte integrity #MMPMID20335315 Wegner B ; Al-Momany A ; Kulak SC ; Kozlowski K ; Obeidat M ; Jahroudi N ; Paes J ; Berryman M ; Ballermann BJ Am J Physiol Renal Physiol 2010[Jun]; 298 (6 ): F1492-503 PMID20335315 show ga The chloride intracellular channel 5A (CLIC5A) protein, one of two isoforms produced by the CLIC5 gene, was isolated originally as part of a cytoskeletal protein complex containing ezrin from placental microvilli. Whether CLIC5A functions as a bona fide ion channel is controversial. We reported previously that a CLIC5 transcript is enriched approximately 800-fold in human renal glomeruli relative to most other tissues. Therefore, this study sought to explore CLIC5 expression and function in glomeruli. RT-PCR and Western blots show that CLIC5A is the predominant CLIC5 isoform expressed in glomeruli. Confocal immunofluorescence and immunogold electron microscopy reveal high levels of CLIC5A protein in glomerular endothelial cells and podocytes. In podocytes, CLIC5A localizes to the apical plasma membrane of foot processes, similar to the known distribution of podocalyxin and ezrin. Ezrin and podocalyxin colocalize with CLIC5A in glomeruli, and podocalyxin coimmunoprecipitates with CLIC5A from glomerular lysates. In glomeruli of jitterbug (jbg/jbg) mice, which lack the CLIC5A protein, ezrin and phospho-ERM levels in podocytes are markedly lower than in wild-type mice. Transmission electron microscopy reveals patchy broadening and effacement of podocyte foot processes as well as vacuolization of glomerular endothelial cells. These ultrastructural changes are associated with microalbuminuria at baseline and increased susceptibility to adriamycin-induced glomerular injury compared with wild-type mice. Together, the data suggest that CLIC5A is required for the development and/or maintenance of the proper glomerular endothelial cell and podocyte architecture. We postulate that the interaction between podocalyxin and subjacent filamentous actin, which requires ezrin, is compromised in podocytes of CLIC5A-deficient mice, leading to dysfunction under unfavorable genetic or environmental conditions. |Animals [MESH] |Blotting, Western [MESH] |Cattle [MESH] |Cells, Cultured [MESH] |Chloride Channels/genetics/*metabolism [MESH] |Cytoskeletal Proteins/*metabolism [MESH] |Doxorubicin/toxicity [MESH] |Endothelial Cells/metabolism [MESH] |Fluorescent Antibody Technique [MESH] |Humans [MESH] |Immunohistochemistry [MESH] |Male [MESH] |Membrane Proteins/metabolism [MESH] |Mice [MESH] |Mice, Inbred C3H [MESH] |Mice, Mutant Strains [MESH] |Microfilament Proteins/genetics/*metabolism [MESH] |Microscopy, Confocal [MESH] |Multiprotein Complexes [MESH] |Phosphorylation [MESH] |Podocytes/drug effects/*metabolism/ultrastructure [MESH] |RNA, Messenger/metabolism [MESH] |Reverse Transcriptase Polymerase Chain Reaction [MESH]CLIC5A, a component of the ezrin-podocalyxin complex in glomeruli, is (epmc).pdf DeepDyve Pubget Overpricing