Ryanodine receptor mutations: in sickness and in health

Autores
Alvarado, Francisco J.; Valdivia, Carmen R.
Año de publicación
2018
Idioma
inglés
Tipo de recurso
reseña artículo
Estado
versión publicada
Descripción
Ryanodine Receptors (RyR) are large ion channels necessary for Ca2+ release from intracellular stores in many cell types. Since RyR was discovered nearly 30 years ago, a fruitful research field has devoted to understanding the physiological regulation of the three protein isoforms in health, and the mechanisms underlying their dysfunction in sickness. This minireview discusses the structural characteristics of RyR2, the cardiac isoform, its regulation during cardiac function and the clinical significance of specific mutations. While hundreds of RyR2 mutations are associated with cardiac disease with different levels of confidence, close to 1500 variants appear in the general population without inducing harmful phenotypes. Hence, studying RyR2 mutations variants may shed light on overall protein regulation and the mechanisms that compensate for constitutive changes in RyR2 function.
Sociedad Argentina de Fisiología
Materia
Bioquímica
Excitation-contraction coupling
Ryanodine receptor
Calcium
Cardiac arrhythmia
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/127226

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network_name_str SEDICI (UNLP)
spelling Ryanodine receptor mutations: in sickness and in healthAlvarado, Francisco J.Valdivia, Carmen R.BioquímicaExcitation-contraction couplingRyanodine receptorCalciumCardiac arrhythmiaRyanodine Receptors (RyR) are large ion channels necessary for Ca2+ release from intracellular stores in many cell types. Since RyR was discovered nearly 30 years ago, a fruitful research field has devoted to understanding the physiological regulation of the three protein isoforms in health, and the mechanisms underlying their dysfunction in sickness. This minireview discusses the structural characteristics of RyR2, the cardiac isoform, its regulation during cardiac function and the clinical significance of specific mutations. While hundreds of RyR2 mutations are associated with cardiac disease with different levels of confidence, close to 1500 variants appear in the general population without inducing harmful phenotypes. Hence, studying RyR2 mutations variants may shed light on overall protein regulation and the mechanisms that compensate for constitutive changes in RyR2 function.Sociedad Argentina de Fisiología2018-06info:eu-repo/semantics/reviewinfo:eu-repo/semantics/publishedVersionRevisionhttp://purl.org/coar/resource_type/c_dcae04bcinfo:ar-repo/semantics/resenaArticuloapplication/pdf23-35http://sedici.unlp.edu.ar/handle/10915/127226enginfo:eu-repo/semantics/altIdentifier/issn/1669-5410info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:30:43Zoai:sedici.unlp.edu.ar:10915/127226Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:30:44.231SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Ryanodine receptor mutations: in sickness and in health
title Ryanodine receptor mutations: in sickness and in health
spellingShingle Ryanodine receptor mutations: in sickness and in health
Alvarado, Francisco J.
Bioquímica
Excitation-contraction coupling
Ryanodine receptor
Calcium
Cardiac arrhythmia
title_short Ryanodine receptor mutations: in sickness and in health
title_full Ryanodine receptor mutations: in sickness and in health
title_fullStr Ryanodine receptor mutations: in sickness and in health
title_full_unstemmed Ryanodine receptor mutations: in sickness and in health
title_sort Ryanodine receptor mutations: in sickness and in health
dc.creator.none.fl_str_mv Alvarado, Francisco J.
Valdivia, Carmen R.
author Alvarado, Francisco J.
author_facet Alvarado, Francisco J.
Valdivia, Carmen R.
author_role author
author2 Valdivia, Carmen R.
author2_role author
dc.subject.none.fl_str_mv Bioquímica
Excitation-contraction coupling
Ryanodine receptor
Calcium
Cardiac arrhythmia
topic Bioquímica
Excitation-contraction coupling
Ryanodine receptor
Calcium
Cardiac arrhythmia
dc.description.none.fl_txt_mv Ryanodine Receptors (RyR) are large ion channels necessary for Ca2+ release from intracellular stores in many cell types. Since RyR was discovered nearly 30 years ago, a fruitful research field has devoted to understanding the physiological regulation of the three protein isoforms in health, and the mechanisms underlying their dysfunction in sickness. This minireview discusses the structural characteristics of RyR2, the cardiac isoform, its regulation during cardiac function and the clinical significance of specific mutations. While hundreds of RyR2 mutations are associated with cardiac disease with different levels of confidence, close to 1500 variants appear in the general population without inducing harmful phenotypes. Hence, studying RyR2 mutations variants may shed light on overall protein regulation and the mechanisms that compensate for constitutive changes in RyR2 function.
Sociedad Argentina de Fisiología
description Ryanodine Receptors (RyR) are large ion channels necessary for Ca2+ release from intracellular stores in many cell types. Since RyR was discovered nearly 30 years ago, a fruitful research field has devoted to understanding the physiological regulation of the three protein isoforms in health, and the mechanisms underlying their dysfunction in sickness. This minireview discusses the structural characteristics of RyR2, the cardiac isoform, its regulation during cardiac function and the clinical significance of specific mutations. While hundreds of RyR2 mutations are associated with cardiac disease with different levels of confidence, close to 1500 variants appear in the general population without inducing harmful phenotypes. Hence, studying RyR2 mutations variants may shed light on overall protein regulation and the mechanisms that compensate for constitutive changes in RyR2 function.
publishDate 2018
dc.date.none.fl_str_mv 2018-06
dc.type.none.fl_str_mv info:eu-repo/semantics/review
info:eu-repo/semantics/publishedVersion
Revision
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info:ar-repo/semantics/resenaArticulo
format review
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/127226
url http://sedici.unlp.edu.ar/handle/10915/127226
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1669-5410
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
23-35
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
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