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10.1172/JCI76453 http://scihub22266oqcxt.onion/10.1172/JCI76453 C4362265!4362265!25689261     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Clin+Invest 2015 ; 125 (3): 1299-310 Nephropedia Template TP {{tp|p=25689261|t=2015. Disturbed flow-activated p90RSK kinase accelerates atherosclerosis by inhibiting SENP2 function |pdf=|usr=}}{{25689261}} gab.com Text Disturbed flow-activated p90RSK kinase accelerates atherosclerosis by inhibiting SENP2 function JO: J Clin Invest http://www.kidney.de/pget.php?&tw=1&pmid=25689261 #FOAvip Disturbed blood flow (d-flow) causes endothelial cell (EC) dysfunction, leading to atherosclerotic plaque formation. We have previously shown that d-flow increases SUMOylation of p53 and ERK5 through downregulation of sentrin/SUMO-specific protease 2 (SENP2) function; however, it is not known how SENP2 itself is regulated by d-flow. Here, we determined that d-flow activated the serine/threonine kinase p90RSK, which subsequently phosphorylated threonine 368 (T368) of SENP2. T368 phosphorylation promoted nuclear export of SENP2, leading to downregulation of eNOS expression and upregulation of proinflammatory adhesion molecule expression and apoptosis. In an LDLR-deficient murine model of atherosclerosis, EC-specific overexpression of p90RSK increased EC dysfunction and lipid accumulation in the aorta compared with control animals; however, these pathologic changes were not observed in atherosclerotic mice overexpressing dominant negative p90RSK (DN-p90RSK). Moreover, depletion of SENP2 in these mice abolished the protective effect of DN-p90RSK overexpression. We propose that p90RSK-mediated SENP2-T368 phosphorylation is a master switch in d-flow?induced signaling, leading to EC dysfunction and atherosclerosis. Twit Text FOAVip Disturbed flow-activated p90RSK kinase accelerates atherosclerosis by inhibiting SENP2 function ????J Clin Invest http://www.kidney.de/pget.php?&tw=1&pmid=25689261 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25689261 #FOAvip English Wikipedia <ref>{{Cite pmid|25689261}}</ref> Disturbed flow-activated p90RSK kinase accelerates atherosclerosis by inhibiting SENP2 function #MMPMID25689261 Heo KS; Le NT; Cushman HJ; Giancursio CJ; Chang E; Woo CH; Sullivan MA; Taunton J; Yeh ET; Fujiwara K; Abe Ji J Clin Invest 2015[Mar]; 125 (3): 1299-310 PMID25689261show ga Disturbed blood flow (d-flow) causes endothelial cell (EC) dysfunction, leading to atherosclerotic plaque formation. We have previously shown that d-flow increases SUMOylation of p53 and ERK5 through downregulation of sentrin/SUMO-specific protease 2 (SENP2) function; however, it is not known how SENP2 itself is regulated by d-flow. Here, we determined that d-flow activated the serine/threonine kinase p90RSK, which subsequently phosphorylated threonine 368 (T368) of SENP2. T368 phosphorylation promoted nuclear export of SENP2, leading to downregulation of eNOS expression and upregulation of proinflammatory adhesion molecule expression and apoptosis. In an LDLR-deficient murine model of atherosclerosis, EC-specific overexpression of p90RSK increased EC dysfunction and lipid accumulation in the aorta compared with control animals; however, these pathologic changes were not observed in atherosclerotic mice overexpressing dominant negative p90RSK (DN-p90RSK). Moreover, depletion of SENP2 in these mice abolished the protective effect of DN-p90RSK overexpression. We propose that p90RSK-mediated SENP2-T368 phosphorylation is a master switch in d-flow?induced signaling, leading to EC dysfunction and atherosclerosis. äDisturbed flow-activated p90RSK kinase accelerates atherosclerosis by (epmc).pdf DeepDyve Pubget Overpricing