CaMKII regulation of phospholamban and SR Ca<SUP>2+</SUP> load

Phospholamban (PLN) is a small phosphoprotein in the cardiac sarcoplasmic reticulum (SR). Dephosphorylated PLN tonically inhibits the SR Ca2 -ATPase (SERCA2a), and phosphorylation of PLN, at either Ser16 by PKA or Thr17 by Ca2 - calmodulin–dependent protein kinase (CaMKII), reverses this inhibition....

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Detalles Bibliográficos
Autores principales:	Mattiazzi, Alicia Ramona, Kranias, Evangelia G.
Formato:	Articulo Preprint
Lenguaje:	Inglés
Publicado:	2011
Materias:	Ciencias Médicas Acidosis CamKII Ischemia/reperfusion Phospholamban phosphorylation Ryanodine receptors Sarcoplasmic reticulum
Acceso en línea:	http://sedici.unlp.edu.ar/handle/10915/104800 http://hdl.handle.net/11336/60872
Aporte de:	SEDICI (UNLP) de Universidad Nacional de La Plata

id	I19-R120-10915-104800
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 Acidosis CamKII Ischemia/reperfusion Phospholamban phosphorylation Ryanodine receptors Sarcoplasmic reticulum
spellingShingle	Ciencias Médicas Acidosis CamKII Ischemia/reperfusion Phospholamban phosphorylation Ryanodine receptors Sarcoplasmic reticulum Mattiazzi, Alicia Ramona Kranias, Evangelia G. CaMKII regulation of phospholamban and SR Ca<SUP>2+</SUP> load
topic_facet	Ciencias Médicas Acidosis CamKII Ischemia/reperfusion Phospholamban phosphorylation Ryanodine receptors Sarcoplasmic reticulum
description	Phospholamban (PLN) is a small phosphoprotein in the cardiac sarcoplasmic reticulum (SR). Dephosphorylated PLN tonically inhibits the SR Ca2 -ATPase (SERCA2a), and phosphorylation of PLN, at either Ser16 by PKA or Thr17 by Ca2 - calmodulin–dependent protein kinase (CaMKII), reverses this inhibition. Consequently, there are increases in SERCA2a activity, SR Ca2 uptake rate, and SR Ca2 load. Through this mechanism, PLN is a major regulator of basal cardiac Ca2 cycling, contractility, and relaxation and the main determinant of -adrenergic mechanical responses in the heart. In this article, we briefly review the functional role of CaMKII-dependent PLN phosphorylation at the Thr17 site and the new findings that link this phosphorylation to beneficial or detrimental effects in pathophysiological situations.
format	Articulo Preprint
author	Mattiazzi, Alicia Ramona Kranias, Evangelia G.
author_facet	Mattiazzi, Alicia Ramona Kranias, Evangelia G.
author_sort	Mattiazzi, Alicia Ramona
title	CaMKII regulation of phospholamban and SR Ca<SUP>2+</SUP> load
title_short	CaMKII regulation of phospholamban and SR Ca<SUP>2+</SUP> load
title_full	CaMKII regulation of phospholamban and SR Ca<SUP>2+</SUP> load
title_fullStr	CaMKII regulation of phospholamban and SR Ca<SUP>2+</SUP> load
title_full_unstemmed	CaMKII regulation of phospholamban and SR Ca<SUP>2+</SUP> load
title_sort	camkii regulation of phospholamban and sr ca<sup>2+</sup> load
publishDate	2011
url	http://sedici.unlp.edu.ar/handle/10915/104800 http://hdl.handle.net/11336/60872
work_keys_str_mv	AT mattiazzialiciaramona camkiiregulationofphospholambanandsrcasup2supload AT kraniasevangeliag camkiiregulationofphospholambanandsrcasup2supload
bdutipo_str	Repositorios
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CaMKII regulation of phospholamban and SR Ca<SUP>2+</SUP> load

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