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
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/83507
Acceder
id SEDICI_31c74113febf139aab995b4f508076bb
oai_identifier_str oai:sedici.unlp.edu.ar:10915/83507
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling 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:UNLP2025-10-15T11:07:42Zoai: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:13292025-10-15 11:07:42.572SEDICI (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)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.22299

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