Mcardle disease: New insights into its underlying molecular mechanisms

Autores
Llavero, Francisco; Sastre, Alazne Arrazola; Montoro, Miriam Luque; Gálvez, Patricia; Lacerda, Hadriano M.; Parada, Luis Antonio; Zugaza, José Luis
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
McArdle disease, also known as glycogen storage disease type V (GSDV), is characterized by exercise intolerance, the second wind phenomenon, and high serum creatine kinase activity. Here, we recapitulate PYGM mutations in the population responsible for this disease. Traditionally, McArdle disease has been considered a metabolic myopathy caused by the lack of expression of the muscle isoform of the glycogen phosphorylase (PYGM). However, recent findings challenge this view, since it has been shown that PYGM is present in other tissues than the skeletal muscle. We review the latest studies about the molecular mechanism involved in glycogen phosphorylase activity regulation. Further, we summarize the expression and functional significance of PYGM in other tissues than skeletal muscle both in health and McArdle disease. Furthermore, we examine the different animal models that have served as the knowledge base for better understanding of McArdle disease. Finally, we give an overview of the latest state-of-the-art clinical trials currently being carried out and present an updated view of the current therapies.
Fil: Llavero, Francisco. Universidad del País Vasco; España. Universidad Europea de Madrid; España
Fil: Sastre, Alazne Arrazola. Universidad del País Vasco; España
Fil: Montoro, Miriam Luque. Universidad del País Vasco; España
Fil: Gálvez, Patricia. Universidad del País Vasco; España. Parque Tecnológico de Ciencias de la Salud; España
Fil: Lacerda, Hadriano M.. Universidad del País Vasco; España
Fil: Parada, Luis Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Patología Experimental. Universidad Nacional de Salta. Facultad de Ciencias de la Salud. Instituto de Patología Experimental; Argentina
Fil: Zugaza, José Luis. Universidad del País Vasco; España. Fundación Vasca para la Ciencia; España
Materia
GLYCOGEN PHOSPHORYLASE
GLYCOGEN STORAGE DISEASE TYPE V
HEXOSAMINE BIOSYNTHETIC PATHWAY
MCARDLE DISEASE
O-GLYCOSYLATION
SMALL GTPASES
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:11336/117964
Acceder
id CONICETDig_16d40836d4e0f79053050b4f04826b84
oai_identifier_str oai:ri.conicet.gov.ar:11336/117964
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Mcardle disease: New insights into its underlying molecular mechanismsLlavero, FranciscoSastre, Alazne ArrazolaMontoro, Miriam LuqueGálvez, PatriciaLacerda, Hadriano M.Parada, Luis AntonioZugaza, José LuisGLYCOGEN PHOSPHORYLASEGLYCOGEN STORAGE DISEASE TYPE VHEXOSAMINE BIOSYNTHETIC PATHWAYMCARDLE DISEASEO-GLYCOSYLATIONSMALL GTPASEShttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3McArdle disease, also known as glycogen storage disease type V (GSDV), is characterized by exercise intolerance, the second wind phenomenon, and high serum creatine kinase activity. Here, we recapitulate PYGM mutations in the population responsible for this disease. Traditionally, McArdle disease has been considered a metabolic myopathy caused by the lack of expression of the muscle isoform of the glycogen phosphorylase (PYGM). However, recent findings challenge this view, since it has been shown that PYGM is present in other tissues than the skeletal muscle. We review the latest studies about the molecular mechanism involved in glycogen phosphorylase activity regulation. Further, we summarize the expression and functional significance of PYGM in other tissues than skeletal muscle both in health and McArdle disease. Furthermore, we examine the different animal models that have served as the knowledge base for better understanding of McArdle disease. Finally, we give an overview of the latest state-of-the-art clinical trials currently being carried out and present an updated view of the current therapies.Fil: Llavero, Francisco. Universidad del País Vasco; España. Universidad Europea de Madrid; EspañaFil: Sastre, Alazne Arrazola. Universidad del País Vasco; EspañaFil: Montoro, Miriam Luque. Universidad del País Vasco; EspañaFil: Gálvez, Patricia. Universidad del País Vasco; España. Parque Tecnológico de Ciencias de la Salud; EspañaFil: Lacerda, Hadriano M.. Universidad del País Vasco; EspañaFil: Parada, Luis Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Patología Experimental. Universidad Nacional de Salta. Facultad de Ciencias de la Salud. Instituto de Patología Experimental; ArgentinaFil: Zugaza, José Luis. Universidad del País Vasco; España. Fundación Vasca para la Ciencia; EspañaMolecular Diversity Preservation International2019-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/117964Llavero, Francisco; Sastre, Alazne Arrazola; Montoro, Miriam Luque; Gálvez, Patricia; Lacerda, Hadriano M.; et al.; Mcardle disease: New insights into its underlying molecular mechanisms; Molecular Diversity Preservation International; International Journal of Molecular Sciences; 20; 23; 12-2019; 1-151422-0067CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/ijms20235919info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1422-0067/20/23/5919info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:00:24Zoai:ri.conicet.gov.ar:11336/117964instacron: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:34982025-10-22 12:00:24.638CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Mcardle disease: New insights into its underlying molecular mechanisms
title Mcardle disease: New insights into its underlying molecular mechanisms
spellingShingle Mcardle disease: New insights into its underlying molecular mechanisms
Llavero, Francisco
GLYCOGEN PHOSPHORYLASE
GLYCOGEN STORAGE DISEASE TYPE V
HEXOSAMINE BIOSYNTHETIC PATHWAY
MCARDLE DISEASE
O-GLYCOSYLATION
SMALL GTPASES
title_short Mcardle disease: New insights into its underlying molecular mechanisms
title_full Mcardle disease: New insights into its underlying molecular mechanisms
title_fullStr Mcardle disease: New insights into its underlying molecular mechanisms
title_full_unstemmed Mcardle disease: New insights into its underlying molecular mechanisms
title_sort Mcardle disease: New insights into its underlying molecular mechanisms
dc.creator.none.fl_str_mv Llavero, Francisco
Sastre, Alazne Arrazola
Montoro, Miriam Luque
Gálvez, Patricia
Lacerda, Hadriano M.
Parada, Luis Antonio
Zugaza, José Luis
author Llavero, Francisco
author_facet Llavero, Francisco
Sastre, Alazne Arrazola
Montoro, Miriam Luque
Gálvez, Patricia
Lacerda, Hadriano M.
Parada, Luis Antonio
Zugaza, José Luis
author_role author
author2 Sastre, Alazne Arrazola
Montoro, Miriam Luque
Gálvez, Patricia
Lacerda, Hadriano M.
Parada, Luis Antonio
Zugaza, José Luis
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv GLYCOGEN PHOSPHORYLASE
GLYCOGEN STORAGE DISEASE TYPE V
HEXOSAMINE BIOSYNTHETIC PATHWAY
MCARDLE DISEASE
O-GLYCOSYLATION
SMALL GTPASES
topic GLYCOGEN PHOSPHORYLASE
GLYCOGEN STORAGE DISEASE TYPE V
HEXOSAMINE BIOSYNTHETIC PATHWAY
MCARDLE DISEASE
O-GLYCOSYLATION
SMALL GTPASES
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv McArdle disease, also known as glycogen storage disease type V (GSDV), is characterized by exercise intolerance, the second wind phenomenon, and high serum creatine kinase activity. Here, we recapitulate PYGM mutations in the population responsible for this disease. Traditionally, McArdle disease has been considered a metabolic myopathy caused by the lack of expression of the muscle isoform of the glycogen phosphorylase (PYGM). However, recent findings challenge this view, since it has been shown that PYGM is present in other tissues than the skeletal muscle. We review the latest studies about the molecular mechanism involved in glycogen phosphorylase activity regulation. Further, we summarize the expression and functional significance of PYGM in other tissues than skeletal muscle both in health and McArdle disease. Furthermore, we examine the different animal models that have served as the knowledge base for better understanding of McArdle disease. Finally, we give an overview of the latest state-of-the-art clinical trials currently being carried out and present an updated view of the current therapies.
Fil: Llavero, Francisco. Universidad del País Vasco; España. Universidad Europea de Madrid; España
Fil: Sastre, Alazne Arrazola. Universidad del País Vasco; España
Fil: Montoro, Miriam Luque. Universidad del País Vasco; España
Fil: Gálvez, Patricia. Universidad del País Vasco; España. Parque Tecnológico de Ciencias de la Salud; España
Fil: Lacerda, Hadriano M.. Universidad del País Vasco; España
Fil: Parada, Luis Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Patología Experimental. Universidad Nacional de Salta. Facultad de Ciencias de la Salud. Instituto de Patología Experimental; Argentina
Fil: Zugaza, José Luis. Universidad del País Vasco; España. Fundación Vasca para la Ciencia; España
description McArdle disease, also known as glycogen storage disease type V (GSDV), is characterized by exercise intolerance, the second wind phenomenon, and high serum creatine kinase activity. Here, we recapitulate PYGM mutations in the population responsible for this disease. Traditionally, McArdle disease has been considered a metabolic myopathy caused by the lack of expression of the muscle isoform of the glycogen phosphorylase (PYGM). However, recent findings challenge this view, since it has been shown that PYGM is present in other tissues than the skeletal muscle. We review the latest studies about the molecular mechanism involved in glycogen phosphorylase activity regulation. Further, we summarize the expression and functional significance of PYGM in other tissues than skeletal muscle both in health and McArdle disease. Furthermore, we examine the different animal models that have served as the knowledge base for better understanding of McArdle disease. Finally, we give an overview of the latest state-of-the-art clinical trials currently being carried out and present an updated view of the current therapies.
publishDate 2019
dc.date.none.fl_str_mv 2019-12
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/11336/117964
Llavero, Francisco; Sastre, Alazne Arrazola; Montoro, Miriam Luque; Gálvez, Patricia; Lacerda, Hadriano M.; et al.; Mcardle disease: New insights into its underlying molecular mechanisms; Molecular Diversity Preservation International; International Journal of Molecular Sciences; 20; 23; 12-2019; 1-15
1422-0067
CONICET Digital
CONICET
url http://hdl.handle.net/11336/117964
identifier_str_mv Llavero, Francisco; Sastre, Alazne Arrazola; Montoro, Miriam Luque; Gálvez, Patricia; Lacerda, Hadriano M.; et al.; Mcardle disease: New insights into its underlying molecular mechanisms; Molecular Diversity Preservation International; International Journal of Molecular Sciences; 20; 23; 12-2019; 1-15
1422-0067
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3390/ijms20235919
info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1422-0067/20/23/5919
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
dc.publisher.none.fl_str_mv Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
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
_version_ 1846782330348240896
score 12.982451

Publicaciones similares