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10.1016/j.prostaglandins.2016.08.001

http://scihub22266oqcxt.onion/10.1016/j.prostaglandins.2016.08.001
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C5099119!5099119!27554058
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suck abstract from ncbi


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pmid27554058      Prostaglandins+Other+Lipid+Mediat 2016 ; 126 (ä): 1-8
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  • Cytosolic phospholipase A2? increases proliferation and de-differentiation of human renal tubular epithelial cells #MMPMID27554058
  • Montford JR; Lehman AM; Scobey MS; Weiser-Evans MC; Nemenoff RA; Furgeson SB
  • Prostaglandins Other Lipid Mediat 2016[Nov]; 126 (ä): 1-8 PMID27554058show ga
  • The group IVA calcium-dependent cytosolic phospholipase A2 (cPLA2?) enzyme controls the release of arachidonic acid from membrane bound phospholipids and is the rate-limiting step in production of eicosanoids. A variety of different kidney injuries activate cPLA2?, therefore we hypothesized that cPLA2? activity would regulate pathologic processes in HK-2 cells, a human renal tubular epithelial cell line, by regulating cell phenotype and proliferation. In two lentiviral cPLA2?-silenced knockdowns, we observed decreased proliferation and increased apoptosis compared to control HK-2 cells. cPLA2?-silenced cells also demonstrated an altered morphology, had increased expression E-cadherin, and decreased expression of Ncadherin. Increased levels of E-cadherin were associated with increased promoter activity and decreased levels of SNAIL1, SNAIL2, and ZEB1, transcriptional repressors of E-cadherin expression. Addition of exogenous arachidonic acid, but not PGE2, reversed the phenotypic changes in cPLA2?-silenced cells. These data suggest that cPLA2? may play a key role in renal repair after injury through a PGE2-independent mechanism.
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