Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions

The sarcoplasmic reticulum (SR) Ca2+-ATPase (SERCA2a) is under the control of a closely associated SR protein named phospholamban (PLN). Dephosphorylated PLN inhibits the SR Ca2+ pump, whereas phosphorylation of PLN, at either Ser16 by PKA or Thr17 by calmodulin-dependent protein kinase II (CaMKII),...

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Autores principales: Mattiazzi, Alicia Ramona, Mundiña-Weilenmann, Cecilia, Guoxiang, Chu, Vittone, Leticia, Kranias, Evangelia
Formato: Articulo
Lenguaje:Inglés
Publicado: 2005
Materias:
Ciencias Médicas
β-adrenergic stimulation
Acidosis
Phospholamban
Thr17 site phosphorylation
Insuficiencia Cardíaca
Isquemia
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/83507
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-83507
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
β-adrenergic stimulation
Acidosis
Phospholamban
Thr17 site phosphorylation
Insuficiencia Cardíaca
Isquemia
spellingShingle Ciencias Médicas
β-adrenergic stimulation
Acidosis
Phospholamban
Thr17 site phosphorylation
Insuficiencia Cardíaca
Isquemia
Mattiazzi, Alicia Ramona
Mundiña-Weilenmann, Cecilia
Guoxiang, Chu
Vittone, Leticia
Kranias, Evangelia
Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions
topic_facet Ciencias Médicas
β-adrenergic stimulation
Acidosis
Phospholamban
Thr17 site phosphorylation
Insuficiencia Cardíaca
Isquemia
description The sarcoplasmic reticulum (SR) Ca2+-ATPase (SERCA2a) is under the control of a closely associated SR protein named phospholamban (PLN). Dephosphorylated PLN inhibits the SR Ca2+ pump, whereas phosphorylation of PLN, at either Ser16 by PKA or Thr17 by calmodulin-dependent protein kinase II (CaMKII), reverses this inhibition, thus increasing SERCA2a activity and the rate of Ca2+ uptake by the SR. This would in turn lead to an increase in the velocity of relaxation, SR Ca 2+ load, and myocardial contractility. Thus, PLN is a major determinant of cardiac contractility and relaxation. Although in the intact heart, β-adrenoceptor stimulation results in phosphorylation of PLN at both Ser16 and Thr17 residues, the role of Thr17 site has long remained equivocal. In this review, we attempt to highlight the signaling cascade and the physiological relevance of the phosphorylation of this residue in the heart under both physiological and pathological situations.
format Articulo
Articulo
author Mattiazzi, Alicia Ramona
Mundiña-Weilenmann, Cecilia
Guoxiang, Chu
Vittone, Leticia
Kranias, Evangelia
author_facet Mattiazzi, Alicia Ramona
Mundiña-Weilenmann, Cecilia
Guoxiang, Chu
Vittone, Leticia
Kranias, Evangelia
author_sort Mattiazzi, Alicia Ramona
title Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions
title_short Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions
title_full Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions
title_fullStr Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions
title_full_unstemmed Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions
title_sort role of phospholamban phosphorylation on thr17 in cardiac physiological and pathological conditions
publishDate 2005
url http://sedici.unlp.edu.ar/handle/10915/83507
work_keys_str_mv AT mattiazzialiciaramona roleofphospholambanphosphorylationonthr17incardiacphysiologicalandpathologicalconditions
AT mundinaweilenmanncecilia roleofphospholambanphosphorylationonthr17incardiacphysiologicalandpathologicalconditions
AT guoxiangchu roleofphospholambanphosphorylationonthr17incardiacphysiologicalandpathologicalconditions
AT vittoneleticia roleofphospholambanphosphorylationonthr17incardiacphysiologicalandpathologicalconditions
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bdutipo_str Repositorios
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