The role of CaMKII regulation of phospholamban activity in heart disease

Phospholamban (PLN) is a phosphoprotein in cardiac sarcoplasmic reticulum (SR) that is a reversible regulator of the Ca<sup>2+</sup>-ATPase (SERCA2a) activity and cardiac contractility. Dephosphorylated PLN inhibits SERCA2a and PLN phosphorylation, at either Ser<sup>16</sup>...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Mattiazzi, Alicia Ramona, Kranias, Evangelina G.
Formato: Articulo Revision
Lenguaje:Inglés
Publicado: 2014
Materias:
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/85070
Aporte de:
id I19-R120-10915-85070
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
Heart failure
Ischemia/reperfusion injury
Myocardium
PLN regulation
spellingShingle Ciencias Médicas
Acidosis
CaMKII
Heart failure
Ischemia/reperfusion injury
Myocardium
PLN regulation
Mattiazzi, Alicia Ramona
Kranias, Evangelina G.
The role of CaMKII regulation of phospholamban activity in heart disease
topic_facet Ciencias Médicas
Acidosis
CaMKII
Heart failure
Ischemia/reperfusion injury
Myocardium
PLN regulation
description Phospholamban (PLN) is a phosphoprotein in cardiac sarcoplasmic reticulum (SR) that is a reversible regulator of the Ca<sup>2+</sup>-ATPase (SERCA2a) activity and cardiac contractility. Dephosphorylated PLN inhibits SERCA2a and PLN phosphorylation, at either Ser<sup>16</sup> by PKA or Thr<SUP>17</SUP> by Ca<sup>2+</sup>-calmodulin-dependent protein kinase (CaMKII), reverses this inhibition. Through this mechanism, PLN is a key modulator of SR Ca<sup>2+</sup> uptake, Ca<sup>2+</sup> load, contractility, and relaxation. PLN phosphorylation is also the main determinant of ß1-adrenergic responses in the heart. Although phosphorylation of Thr<SUP>17</SUP> by CaMKII contributes to this effect, its role is subordinate to the PKA-dependent increase in cytosolic Ca<sup>2+</sup>, necessary to activate CaMKII. Furthermore, the effects of PLN and its phosphorylation on cardiac function are subject to additional regulation by its interacting partners, the anti-apoptotic HAX-1 protein and Gm or the anchoring unit of protein phosphatase 1. Regulation of PLN activity by this multimeric complex becomes even more important in pathological conditions, characterized by aberrant Ca<sup>2+</sup>-cycling. In this scenario, CaMKII-dependent PLN phosphorylation has been associated with protective effects in both acidosis and ischemia/reperfusion. However, the beneficial effects of increasing SR Ca<sup>2+</sup> uptake through PLN phosphorylation may be lost or even become deleterious, when these occur in association with alterations in SR Ca<sup>2+</sup> leak. Moreover, a major characteristic in human and experimental heart failure (HF) is depressed SR Ca<sup>2+</sup> uptake, associated with decreased SERCA2a levels and dephosphorylation of PLN, leading to decreased SR Ca<sup>2+</sup> load and impaired contractility. Thus, the strategy of altering SERCA2a and/or PLN levels or activity to restore perturbed SR Ca<sup>2+</sup> uptake is a potential therapeutic tool for HF treatment. We will review here the role of CaMKII-dependent phosphorylation of PLN at Thr<SUP>17</SUP> on cardiac function under physiological and pathological conditions.
format Articulo
Revision
author Mattiazzi, Alicia Ramona
Kranias, Evangelina G.
author_facet Mattiazzi, Alicia Ramona
Kranias, Evangelina G.
author_sort Mattiazzi, Alicia Ramona
title The role of CaMKII regulation of phospholamban activity in heart disease
title_short The role of CaMKII regulation of phospholamban activity in heart disease
title_full The role of CaMKII regulation of phospholamban activity in heart disease
title_fullStr The role of CaMKII regulation of phospholamban activity in heart disease
title_full_unstemmed The role of CaMKII regulation of phospholamban activity in heart disease
title_sort role of camkii regulation of phospholamban activity in heart disease
publishDate 2014
url http://sedici.unlp.edu.ar/handle/10915/85070
work_keys_str_mv AT mattiazzialiciaramona theroleofcamkiiregulationofphospholambanactivityinheartdisease
AT kraniasevangelinag theroleofcamkiiregulationofphospholambanactivityinheartdisease
AT mattiazzialiciaramona roleofcamkiiregulationofphospholambanactivityinheartdisease
AT kraniasevangelinag roleofcamkiiregulationofphospholambanactivityinheartdisease
bdutipo_str Repositorios
_version_ 1764820488912109570