Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

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.

10.1152/ajprenal.00355.2016 http://scihub22266oqcxt.onion/10.1152/ajprenal.00355.2016 C5130455!5130455!27605582     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 278.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Am+J+Physiol+Renal+Physiol 2016 ; 311 (5): F958-66 Nephropedia Template TP {{tp|p=27605582|t=2016. Chronic insulin treatment phosphorylates the renal Na-K-ATPase ?1-subunit at serine 16/23 and reduces its activity involving PI3-kinase-dependent PKC activation |pdf=|usr=}}{{27605582}} gab.com Text Chronic insulin treatment phosphorylates the renal Na-K-ATPase 1-subunit at serine 16/23 and reduces its activity involving PI3-kinase-dependent PKC activation JO: Am J Physiol Renal Physiol http://www.kidney.de/pget.php?&tw=1&pmid=27605582 #FOAvip The regulation of Na-K-ATPase in various tissues is under the control of a number of hormones and peptides that exert both short- and long-term control over its activity. The present study was performed to investigate the effect of chronic insulin treatment on Na-K-ATPase in renal proximal tubular cells. Incubation of opossum kidney (OK) cells, transfected with the rat Na-K-ATPase ?1-subunit, with 1 nmol/l insulin for 48 h decreased Na-K-ATPase activity. Insulin decreased ?1-protein content and increased ?1-serine phosphorylation and ?1-adaptor protein 2 (AP2) interaction. Removal of the 26 NH2-terminal (-NT) amino acid from the ?1-subunit containing serine/threonine sites abolished the insulin-mediated serine phosphorylation and inhibition of Na-K-ATPase. Substitution of serine 16 and 23 with alanine showed a comparable effect on -NT. Insulin increased the activity of protein kinase C (PKC), which was blocked by the phosphatidylinositol 3-kinase (PI3K) inhibitor wortmannin. Both PI3K and PKC inhibitors abolished the insulin-mediated inhibition of Na-K-ATPase. Insulin increased the expression of PKC-?1, -?, -?, and-?; however, only PKC-?/?-specific inhibitors blocked insulin-induced phosphorylation and inhibition of Na-K-ATPase. Our data demonstrate that insulin activates the atypical PKC isoforms-?/? via the PI3K pathway. PKC-?/?-induced phosphorylation of the ?1-subunit at serine 16 and 23 leads to AP2 recruitment, degradation, and a decrease in Na-K-ATPase activity. Twit Text FOAVip Chronic insulin treatment phosphorylates the renal Na-K-ATPase 1-subunit at serine 16/23 and reduces its activity involving PI3-kinase-dependent PKC activation ????Am J Physiol Renal Physiol http://www.kidney.de/pget.php?&tw=1&pmid=27605582 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27605582 #FOAvip English Wikipedia <ref>{{Cite pmid|27605582}}</ref> Chronic insulin treatment phosphorylates the renal Na-K-ATPase ?1-subunit at serine 16/23 and reduces its activity involving PI3-kinase-dependent PKC activation #MMPMID27605582 Banday AA Am J Physiol Renal Physiol 2016[Nov]; 311 (5): F958-66 PMID27605582show ga The regulation of Na-K-ATPase in various tissues is under the control of a number of hormones and peptides that exert both short- and long-term control over its activity. The present study was performed to investigate the effect of chronic insulin treatment on Na-K-ATPase in renal proximal tubular cells. Incubation of opossum kidney (OK) cells, transfected with the rat Na-K-ATPase ?1-subunit, with 1 nmol/l insulin for 48 h decreased Na-K-ATPase activity. Insulin decreased ?1-protein content and increased ?1-serine phosphorylation and ?1-adaptor protein 2 (AP2) interaction. Removal of the 26 NH2-terminal (-NT) amino acid from the ?1-subunit containing serine/threonine sites abolished the insulin-mediated serine phosphorylation and inhibition of Na-K-ATPase. Substitution of serine 16 and 23 with alanine showed a comparable effect on -NT. Insulin increased the activity of protein kinase C (PKC), which was blocked by the phosphatidylinositol 3-kinase (PI3K) inhibitor wortmannin. Both PI3K and PKC inhibitors abolished the insulin-mediated inhibition of Na-K-ATPase. Insulin increased the expression of PKC-?1, -?, -?, and-?; however, only PKC-?/?-specific inhibitors blocked insulin-induced phosphorylation and inhibition of Na-K-ATPase. Our data demonstrate that insulin activates the atypical PKC isoforms-?/? via the PI3K pathway. PKC-?/?-induced phosphorylation of the ?1-subunit at serine 16 and 23 leads to AP2 recruitment, degradation, and a decrease in Na-K-ATPase activity. äChronic insulin treatment phosphorylates the renal Na-K-ATPase ?1-subu(epmc).pdf DeepDyve Pubget Overpricing