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
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/127226
Ver los metadatos del registro completo
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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 http://purl.org/coar/resource_type/c_dcae04bc info:ar-repo/semantics/resenaArticulo |
format |
review |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://sedici.unlp.edu.ar/handle/10915/127226 |
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http://sedici.unlp.edu.ar/handle/10915/127226 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
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info:eu-repo/semantics/altIdentifier/issn/1669-5410 |
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info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
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openAccess |
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http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
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application/pdf 23-35 |
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SEDICI (UNLP) - Universidad Nacional de La Plata |
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