Ca2+-Calmodulin–Dependent Protein Kinase Phosphorylation of Ryanodine Receptor May Contribute to the β-Adrenergic Regulation of Myocardial Contractility Independently of Increases in Heart Rate

In a recent article, MacDonnell et al. reported that protein kinase A (PKA) phosphorylation of ryanodine receptor (RyR2) (the Ca2+ release channel of the sarcoplasmic reticulum [SR]) at Ser2808/09 site does not have a major role in the sympathetic nervous system (SNS) regulation of cardiac function....

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Detalles Bibliográficos
Autores principales: Mattiazzi, Alicia Ramona, Vittone, Leticia Beatriz, Mundiña-Weilenmann, Cecilia
Formato: Articulo
Lenguaje:Inglés
Publicado: 2008
Materias:
Ciencias Médicas
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/141457
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-141457
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Médicas
spellingShingle Ciencias Médicas
Mattiazzi, Alicia Ramona
Vittone, Leticia Beatriz
Mundiña-Weilenmann, Cecilia
Ca2+-Calmodulin–Dependent Protein Kinase Phosphorylation of Ryanodine Receptor May Contribute to the β-Adrenergic Regulation of Myocardial Contractility Independently of Increases in Heart Rate
topic_facet Ciencias Médicas
description In a recent article, MacDonnell et al. reported that protein kinase A (PKA) phosphorylation of ryanodine receptor (RyR2) (the Ca2+ release channel of the sarcoplasmic reticulum [SR]) at Ser2808/09 site does not have a major role in the sympathetic nervous system (SNS) regulation of cardiac function. This conclusion was based on comparing the effect of isoproterenol on ventricular performance, in vivo, in isolated hearts and myocytes, in wild-type mice and in a genetically modified mouse in which Ser2808 of RyR2 was replaced by alanine (S2808A) to prevent PKA-mediated phosphorylation at this site. Isoproterenol produced an increase in cardiac function both in vivo and in isolated hearts, as well as an enhancement in the L-type Ca2+ current ( I CaL), the amplitude of the Ca2+ transient and the excitation–contraction coupling (ECC) gain in isolated myocytes, which were not significantly different between wild-type and …
format Articulo
Articulo
author Mattiazzi, Alicia Ramona
Vittone, Leticia Beatriz
Mundiña-Weilenmann, Cecilia
author_facet Mattiazzi, Alicia Ramona
Vittone, Leticia Beatriz
Mundiña-Weilenmann, Cecilia
author_sort Mattiazzi, Alicia Ramona
title Ca2+-Calmodulin–Dependent Protein Kinase Phosphorylation of Ryanodine Receptor May Contribute to the β-Adrenergic Regulation of Myocardial Contractility Independently of Increases in Heart Rate
title_short Ca2+-Calmodulin–Dependent Protein Kinase Phosphorylation of Ryanodine Receptor May Contribute to the β-Adrenergic Regulation of Myocardial Contractility Independently of Increases in Heart Rate
title_full Ca2+-Calmodulin–Dependent Protein Kinase Phosphorylation of Ryanodine Receptor May Contribute to the β-Adrenergic Regulation of Myocardial Contractility Independently of Increases in Heart Rate
title_fullStr Ca2+-Calmodulin–Dependent Protein Kinase Phosphorylation of Ryanodine Receptor May Contribute to the β-Adrenergic Regulation of Myocardial Contractility Independently of Increases in Heart Rate
title_full_unstemmed Ca2+-Calmodulin–Dependent Protein Kinase Phosphorylation of Ryanodine Receptor May Contribute to the β-Adrenergic Regulation of Myocardial Contractility Independently of Increases in Heart Rate
title_sort ca2+-calmodulin–dependent protein kinase phosphorylation of ryanodine receptor may contribute to the β-adrenergic regulation of myocardial contractility independently of increases in heart rate
publishDate 2008
url http://sedici.unlp.edu.ar/handle/10915/141457
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