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10.1161/CIRCRESAHA.114.300569 http://scihub22266oqcxt.onion/10.1161/CIRCRESAHA.114.300569 C4040460!4040460!24723657     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 276.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 276.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Circ+Res 2014 ; 114 (8): 1320-7 Nephropedia Template TP {{tp|p=24723657|t=2014. Controversies in Cardiovascular Research: Role of Protein Kinase A Mediated Hyperphosphorylation of the Ryanodine Receptor at Serine 2808 in Heart Failure and Arrhythmias |pdf=|usr=}}{{24723657}} gab.com Text Controversies in Cardiovascular Research: Role of Protein Kinase A Mediated Hyperphosphorylation of the Ryanodine Receptor at Serine 2808 in Heart Failure and Arrhythmias JO: Circ Res http://www.kidney.de/pget.php?&tw=1&pmid=24723657 #FOAvip This ?Controversies in Research? article discusses the hypothesis that protein kinase A mediated phosphorylation of the Ryanodine Receptor (RyR) at a single serine (RyRS2808) is essential for normal sympathetic regulation of cardiac myocyte contractility and is responsible for the disturbed Ca2+ regulation that underlies depressed contractility in heart failure. Studies supporting this hypothesis have associated ?hyper? phosphorylation of RyRS2808 and heart failure progression in animals and humans and have shown that a phosphorylation defective RyR mutant mouse (RyRS2808A) does not respond normally to sympathetic agonists and does not exhibit heart failure symptoms after myocardial infarction (MI). Studies to confirm and extend these ideas have failed to support the original data. Experiments from many different laboratories have convincingly shown that PKA-mediated RyRS2808 phosphorylation does not play any significant role in the normal sympathetic regulation of sarcoplasmic reticulum (SR) Ca2+ release or cardiac contractility. Hearts and myocytes from RyRS2808A mice have been shown to respond normally to sympathetic agonists, and to increase Ca2+ influx, Ca2+ transients, and Ca2+ efflux. While the RyR is involved in heart failure related Ca2+ disturbances, this results from CaMKII and reactive oxygen species mediated regulation rather than by RyR2808 phosphorylation. Also, a new study has shown that RyRS2808A mice are not protected from MI. Collectively, there is now a clear consensus in the published literature showing that dysregulated RyRs contribute to the altered Ca2+ regulatory phenotype of the failing heart, but PKA-mediated phosphorylation of RyRS2808 has little or no role in these alterations. Twit Text FOAVip Controversies in Cardiovascular Research: Role of Protein Kinase A Mediated Hyperphosphorylation of the Ryanodine Receptor at Serine 2808 in Heart Failure and Arrhythmias ????Circ Res http://www.kidney.de/pget.php?&tw=1&pmid=24723657 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24723657 #FOAvip English Wikipedia <ref>{{Cite pmid|24723657}}</ref> Controversies in Cardiovascular Research: Role of Protein Kinase A Mediated Hyperphosphorylation of the Ryanodine Receptor at Serine 2808 in Heart Failure and Arrhythmias #MMPMID24723657 Houser SR Circ Res 2014[Apr]; 114 (8): 1320-7 PMID24723657show ga This ?Controversies in Research? article discusses the hypothesis that protein kinase A mediated phosphorylation of the Ryanodine Receptor (RyR) at a single serine (RyRS2808) is essential for normal sympathetic regulation of cardiac myocyte contractility and is responsible for the disturbed Ca2+ regulation that underlies depressed contractility in heart failure. Studies supporting this hypothesis have associated ?hyper? phosphorylation of RyRS2808 and heart failure progression in animals and humans and have shown that a phosphorylation defective RyR mutant mouse (RyRS2808A) does not respond normally to sympathetic agonists and does not exhibit heart failure symptoms after myocardial infarction (MI). Studies to confirm and extend these ideas have failed to support the original data. Experiments from many different laboratories have convincingly shown that PKA-mediated RyRS2808 phosphorylation does not play any significant role in the normal sympathetic regulation of sarcoplasmic reticulum (SR) Ca2+ release or cardiac contractility. Hearts and myocytes from RyRS2808A mice have been shown to respond normally to sympathetic agonists, and to increase Ca2+ influx, Ca2+ transients, and Ca2+ efflux. While the RyR is involved in heart failure related Ca2+ disturbances, this results from CaMKII and reactive oxygen species mediated regulation rather than by RyR2808 phosphorylation. Also, a new study has shown that RyRS2808A mice are not protected from MI. Collectively, there is now a clear consensus in the published literature showing that dysregulated RyRs contribute to the altered Ca2+ regulatory phenotype of the failing heart, but PKA-mediated phosphorylation of RyRS2808 has little or no role in these alterations. äControversies in Cardiovascular Research: Role of Protein Kinase A Med(epmc).pdf DeepDyve Pubget Overpricing