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10.3390/biom2020269 http://scihub22266oqcxt.onion/10.3390/biom2020269 C4030845!4030845!24970137     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       Biomolecules 2012 ; 2 (2): 269-81 Nephropedia Template TP {{tp|p=24970137|t=2012. DeSUMOylation Controls Insulin Exocytosis in Response to Metabolic Signals |pdf=|usr=}}{{24970137}} gab.com Text DeSUMOylation Controls Insulin Exocytosis in Response to Metabolic Signals JO: Biomolecules http://www.kidney.de/pget.php?&tw=1&pmid=24970137 #FOAvip The secretion of insulin by pancreatic islet ?-cells plays a pivotal role in glucose homeostasis and diabetes. Recent work suggests an important role for SUMOylation in the control of insulin secretion from ?-cells. In this paper we discuss mechanisms whereby (de)SUMOylation may control insulin release by modulating ?-cell function at one or more key points; and particularly through the acute and reversible regulation of the exocytotic machinery. Furthermore, we postulate that the SUMO-specific protease SENP1 is an important mediator of insulin exocytosis in response to NADPH, a metabolic secretory signal and major determinant of ?-cell redox state. Dialysis of mouse ?-cells with NADPH efficiently amplifies ?-cell exocytosis even when extracellular glucose is low; an effect that is lost upon knockdown of SENP1. Conversely, over-expression of SENP1 itself augments ?-cell exocytosis in a redox-dependent manner. Taken together, we suggest that (de)SUMOylation represents an important mechanism that acutely regulates insulin secretion and that SENP1 can act as an amplifier of insulin exocytosis. Twit Text FOAVip DeSUMOylation Controls Insulin Exocytosis in Response to Metabolic Signals ????Biomolecules http://www.kidney.de/pget.php?&tw=1&pmid=24970137 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24970137 #FOAvip English Wikipedia <ref>{{Cite pmid|24970137}}</ref> DeSUMOylation Controls Insulin Exocytosis in Response to Metabolic Signals #MMPMID24970137 Vergari E; Plummer G; Dai X; MacDonald PE Biomolecules 2012[Jun]; 2 (2): 269-81 PMID24970137show ga The secretion of insulin by pancreatic islet ?-cells plays a pivotal role in glucose homeostasis and diabetes. Recent work suggests an important role for SUMOylation in the control of insulin secretion from ?-cells. In this paper we discuss mechanisms whereby (de)SUMOylation may control insulin release by modulating ?-cell function at one or more key points; and particularly through the acute and reversible regulation of the exocytotic machinery. Furthermore, we postulate that the SUMO-specific protease SENP1 is an important mediator of insulin exocytosis in response to NADPH, a metabolic secretory signal and major determinant of ?-cell redox state. Dialysis of mouse ?-cells with NADPH efficiently amplifies ?-cell exocytosis even when extracellular glucose is low; an effect that is lost upon knockdown of SENP1. Conversely, over-expression of SENP1 itself augments ?-cell exocytosis in a redox-dependent manner. Taken together, we suggest that (de)SUMOylation represents an important mechanism that acutely regulates insulin secretion and that SENP1 can act as an amplifier of insulin exocytosis. äDeSUMOylation Controls Insulin Exocytosis in Response to Metabolic Sig(epmc).pdf DeepDyve Pubget Overpricing