CaMKLL regulation of phospholamban and SR Ca2 load

Autores
Mattiazzi, Ramona Alicia; Kranias, Evangelia G.
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Mattiazzi, Ramona Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigaciones Cardiovasculares ; Argentina
Fil: Kranias, Evangelia G.. University of Cincinnati; Estados Unidos
Materia
ACIDOSIS
CAMKII
ISCHEMIA/REPERFUSION
PHOSPHOLAMBAN PHOSPHORYLATION
RYANODINE RECEPTORS
SARCOPLASMIC RETICULUM
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/60872
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/60872
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling CaMKLL regulation of phospholamban and SR Ca2 loadMattiazzi, Ramona AliciaKranias, Evangelia G.ACIDOSISCAMKIIISCHEMIA/REPERFUSIONPHOSPHOLAMBAN PHOSPHORYLATIONRYANODINE RECEPTORSSARCOPLASMIC RETICULUMhttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Phospholamban (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.Fil: Mattiazzi, Ramona Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigaciones Cardiovasculares ; ArgentinaFil: Kranias, Evangelia G.. University of Cincinnati; Estados UnidosElsevier Science Inc2011-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/60872Mattiazzi, Ramona Alicia; Kranias, Evangelia G.; CaMKLL regulation of phospholamban and SR Ca2 load; Elsevier Science Inc; Heart Rhythm; 8; 5; 5-2011; 784-7871547-5271CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.heartrhythmjournal.com/article/S1547-5271(10)01282-8/fulltextinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.hrthm.2010.11.035info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:01:59Zoai:ri.conicet.gov.ar:11336/60872instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:01:59.779CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv CaMKLL regulation of phospholamban and SR Ca2 load
title CaMKLL regulation of phospholamban and SR Ca2 load
spellingShingle CaMKLL regulation of phospholamban and SR Ca2 load
Mattiazzi, Ramona Alicia
ACIDOSIS
CAMKII
ISCHEMIA/REPERFUSION
PHOSPHOLAMBAN PHOSPHORYLATION
RYANODINE RECEPTORS
SARCOPLASMIC RETICULUM
title_short CaMKLL regulation of phospholamban and SR Ca2 load
title_full CaMKLL regulation of phospholamban and SR Ca2 load
title_fullStr CaMKLL regulation of phospholamban and SR Ca2 load
title_full_unstemmed CaMKLL regulation of phospholamban and SR Ca2 load
title_sort CaMKLL regulation of phospholamban and SR Ca2 load
dc.creator.none.fl_str_mv Mattiazzi, Ramona Alicia
Kranias, Evangelia G.
author Mattiazzi, Ramona Alicia
author_facet Mattiazzi, Ramona Alicia
Kranias, Evangelia G.
author_role author
author2 Kranias, Evangelia G.
author2_role author
dc.subject.none.fl_str_mv ACIDOSIS
CAMKII
ISCHEMIA/REPERFUSION
PHOSPHOLAMBAN PHOSPHORYLATION
RYANODINE RECEPTORS
SARCOPLASMIC RETICULUM
topic ACIDOSIS
CAMKII
ISCHEMIA/REPERFUSION
PHOSPHOLAMBAN PHOSPHORYLATION
RYANODINE RECEPTORS
SARCOPLASMIC RETICULUM
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv 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.
Fil: Mattiazzi, Ramona Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigaciones Cardiovasculares ; Argentina
Fil: Kranias, Evangelia G.. University of Cincinnati; Estados Unidos
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.
publishDate 2011
dc.date.none.fl_str_mv 2011-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/60872
Mattiazzi, Ramona Alicia; Kranias, Evangelia G.; CaMKLL regulation of phospholamban and SR Ca2 load; Elsevier Science Inc; Heart Rhythm; 8; 5; 5-2011; 784-787
1547-5271
CONICET Digital
CONICET
url http://hdl.handle.net/11336/60872
identifier_str_mv Mattiazzi, Ramona Alicia; Kranias, Evangelia G.; CaMKLL regulation of phospholamban and SR Ca2 load; Elsevier Science Inc; Heart Rhythm; 8; 5; 5-2011; 784-787
1547-5271
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.heartrhythmjournal.com/article/S1547-5271(10)01282-8/fulltext
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.hrthm.2010.11.035
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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