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A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.3390/ijms160819170 http://scihub22266oqcxt.onion/10.3390/ijms160819170 C4581292!4581292 !26287173     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26287173 &cmd=llinks): Failed to open stream: HTTP request failed! 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Cdc42-Interacting Protein 4 Represses E-Cadherin Expression by Promoting ?-Catenin Translocation to the Nucleus in Murine Renal Tubular Epithelial Cells |pdf=|usr=}}{{26287173 }} gab.com Text Cdc42-Interacting Protein 4 Represses E-Cadherin Expression by Promoting -Catenin Translocation to the Nucleus in Murine Renal Tubular Epithelial Cells JO: Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=26287173 #FOAvip Renal fibrosis is an inevitable outcome of end-stage chronic kidney disease. During this process, epithelial cells lose E-cadherin expression. ?-Catenin may act as a mediator by accumulation and translocation to the nucleus. Studies have suggested that CIP4, a Cdc42 effector protein, is associated with ?-catenin. However, whether CIP4 contributes to E-cadherin loss in epithelial cells by regulating ?-catenin translocation is unclear. In this study, we investigated the involvement of CIP4 in ?-catenin translocation. Expression of CIP4 was upregulated in renal tissues of 5/6 nephrectomized rats and mainly distributed in renal tubular epithelia. In TGF-?1-treated NRK-52E cells, upregulation of CIP4 expression was accompanied by reduced expression of E-cadherin. CIP4 overexpression promoted the translocation of ?-catenin to the nucleus, which was accompanied by reduced expression of E-cadherin even without TGF-?1 stimulation. In contrast, CIP4 depletion by using siRNA inhibited the translocation of ?-catenin to the nucleus and reversed the decrease in expression of E-cadherin. The interaction between CIP4 and ?-catenin was detected. We also show that ?-catenin depletion could restore the expression of E-cadherin that was suppressed by CIP4 overexpression. In conclusion, these results suggest that CIP4 overexpression represses E-cadherin expression by promoting ?-catenin translocation to the nucleus. Twit Text FOAVip Cdc42-Interacting Protein 4 Represses E-Cadherin Expression by Promoting -Catenin Translocation to the Nucleus in Murine Renal Tubular Epithelial Cells ????Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=26287173 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26287173 #FOAvip English Wikipedia <ref>{{Cite pmid|26287173 }}</ref> Cdc42-Interacting Protein 4 Represses E-Cadherin Expression by Promoting ?-Catenin Translocation to the Nucleus in Murine Renal Tubular Epithelial Cells #MMPMID26287173 Xu C ; Zhou Q ; Liu L ; Liu P ; Pei G ; Zeng R ; Han M ; Xu G Int J Mol Sci 2015[Aug]; 16 (8 ): 19170-83 PMID26287173 show ga Renal fibrosis is an inevitable outcome of end-stage chronic kidney disease. During this process, epithelial cells lose E-cadherin expression. ?-Catenin may act as a mediator by accumulation and translocation to the nucleus. Studies have suggested that CIP4, a Cdc42 effector protein, is associated with ?-catenin. However, whether CIP4 contributes to E-cadherin loss in epithelial cells by regulating ?-catenin translocation is unclear. In this study, we investigated the involvement of CIP4 in ?-catenin translocation. Expression of CIP4 was upregulated in renal tissues of 5/6 nephrectomized rats and mainly distributed in renal tubular epithelia. In TGF-?1-treated NRK-52E cells, upregulation of CIP4 expression was accompanied by reduced expression of E-cadherin. CIP4 overexpression promoted the translocation of ?-catenin to the nucleus, which was accompanied by reduced expression of E-cadherin even without TGF-?1 stimulation. In contrast, CIP4 depletion by using siRNA inhibited the translocation of ?-catenin to the nucleus and reversed the decrease in expression of E-cadherin. The interaction between CIP4 and ?-catenin was detected. We also show that ?-catenin depletion could restore the expression of E-cadherin that was suppressed by CIP4 overexpression. In conclusion, these results suggest that CIP4 overexpression represses E-cadherin expression by promoting ?-catenin translocation to the nucleus. |Active Transport, Cell Nucleus [MESH] |Animals [MESH] |Cadherins/genetics/*metabolism [MESH] |Cell Line [MESH] |Cell Nucleus/genetics/*metabolism [MESH] |Epithelial Cells/*metabolism [MESH] |Kidney Tubules/*cytology/metabolism [MESH] |Microtubule-Associated Proteins/genetics/*metabolism [MESH] |Minor Histocompatibility Antigens [MESH] |Protein Interaction Maps [MESH] |RNA Interference [MESH] |RNA, Small Interfering/genetics [MESH] |Rats [MESH] |Transforming Growth Factor beta1/metabolism [MESH] |Up-Regulation [MESH]Cdc42-Interacting Protein 4 Represses E-Cadherin Expression by Promoti(epmc).pdf DeepDyve Pubget Overpricing