Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions
- Autores
- Mattiazzi, Alicia Ramona; Mundiña-Weilenmann, Cecilia; Guoxiang, Chu; Vittone, Leticia; Kranias, Evangelia
- Año de publicación
- 2005
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 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.
Facultad de Ciencias Médicas - Materia
-
Ciencias Médicas
β-adrenergic stimulation
Acidosis
Phospholamban
Thr17 site phosphorylation
Insuficiencia Cardíaca
Isquemia - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/83507
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Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditionsMattiazzi, Alicia RamonaMundiña-Weilenmann, CeciliaGuoxiang, ChuVittone, LeticiaKranias, EvangeliaCiencias Médicasβ-adrenergic stimulationAcidosisPhospholambanThr17 site phosphorylationInsuficiencia CardíacaIsquemiaThe 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.Facultad de Ciencias Médicas2005-10-13info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/83507enginfo:eu-repo/semantics/altIdentifier/issn/0008-6363info:eu-repo/semantics/altIdentifier/doi/10.1016/j.cardiores.2005.08.010info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:15:46Zoai:sedici.unlp.edu.ar:10915/83507Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:15:46.873SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions |
title |
Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions |
spellingShingle |
Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions Mattiazzi, Alicia Ramona Ciencias Médicas β-adrenergic stimulation Acidosis Phospholamban Thr17 site phosphorylation Insuficiencia Cardíaca Isquemia |
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 |
dc.creator.none.fl_str_mv |
Mattiazzi, Alicia Ramona Mundiña-Weilenmann, Cecilia Guoxiang, Chu Vittone, Leticia Kranias, Evangelia |
author |
Mattiazzi, Alicia Ramona |
author_facet |
Mattiazzi, Alicia Ramona Mundiña-Weilenmann, Cecilia Guoxiang, Chu Vittone, Leticia Kranias, Evangelia |
author_role |
author |
author2 |
Mundiña-Weilenmann, Cecilia Guoxiang, Chu Vittone, Leticia Kranias, Evangelia |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
Ciencias Médicas β-adrenergic stimulation Acidosis Phospholamban Thr17 site phosphorylation Insuficiencia Cardíaca Isquemia |
topic |
Ciencias Médicas β-adrenergic stimulation Acidosis Phospholamban Thr17 site phosphorylation Insuficiencia Cardíaca Isquemia |
dc.description.none.fl_txt_mv |
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. Facultad de Ciencias Médicas |
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. |
publishDate |
2005 |
dc.date.none.fl_str_mv |
2005-10-13 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://sedici.unlp.edu.ar/handle/10915/83507 |
url |
http://sedici.unlp.edu.ar/handle/10915/83507 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/issn/0008-6363 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.cardiores.2005.08.010 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
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openAccess |
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http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
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application/pdf |
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SEDICI (UNLP) - Universidad Nacional de La Plata |
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