CAMP-dependent protein kinase inhibits FoxO activity and regulates skeletal muscle plasticity in mice.

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MetadadosDescriçãoIdioma
Autor(es): dc.creatorSilveira, Wilian de Assis-
Autor(es): dc.creatorGonçalves, Dawit Alberto Pinheiro-
Autor(es): dc.creatorMachado, Juliano-
Autor(es): dc.creatorSilva, Natalia Lautherbach Ennes da-
Autor(es): dc.creatorBorges, Danilo Lustrino-
Autor(es): dc.creatorGomes, Sílvia de Paula-
Autor(es): dc.creatorPereira, Marcelo G.-
Autor(es): dc.creatorMiyabara, Elen Haruka-
Autor(es): dc.creatorSandri, Marco-
Autor(es): dc.creatorKettelhut, Isis do Carmo-
Autor(es): dc.creatorNavegantes, Luiz Carlos Carvalho-
Data de aceite: dc.date.accessioned2025-08-21T15:16:01Z-
Data de disponibilização: dc.date.available2025-08-21T15:16:01Z-
Data de envio: dc.date.issued2023-05-15-
Data de envio: dc.date.issued2023-05-15-
Data de envio: dc.date.issued2019-
Fonte completa do material: dc.identifierhttp://www.repositorio.ufop.br/jspui/handle/123456789/16565-
Fonte completa do material: dc.identifierhttps://faseb.onlinelibrary.wiley.com/doi/epdf/10.1096/fj.201902102RR-
Fonte completa do material: dc.identifierhttps://doi.org/10.1096/fj.201902102RR-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1008502-
Descrição: dc.descriptionAlthough we have shown that catecholamines suppress the activity of the Ubiquitin- Proteasome System (UPS) and atrophy-related genes expression through a cAMP-de- pendent manner in skeletal muscle from rodents, the underlying mechanisms remain unclear. Here, we report that a single injection of norepinephrine (NE; 1 mg kg−1; s.c) attenuated the fasting-induced up-regulation of FoxO-target genes in tibialis anterior (TA) muscles by the stimulation of PKA/CREB and Akt/FoxO1 signaling pathways. In addition, muscle-specific activation of PKA by the overexpression of PKA catalytic subunit (PKAcat) suppressed FoxO reporter activity induced by (1) a wild-type; (2) a non-phosphorylatable; (3) a non-phosphorylatable and non-acet- ylatable forms of FoxO1 and FoxO3; (4) downregulation of FoxO protein content, and probably by (5) PGC-1α up-regulation. Consistently, the overexpression of the PKAcat inhibitor (PKI) up-regulated FoxO activity and the content of Atrogin-1 and MuRF1, as well as induced muscle fiber atrophy, the latter effect being prevented by the overexpression of a dominant negative (d. n.) form of FoxO (d.n.FoxO). The sustained overexpression of PKAcat induced fiber-type transition toward a smaller, slower, and more oxidative phenotype and improved muscle resistance to fatigue. Taken together, our data provide the first evidence that endogenous PKA activity is required to restrain the basal activity of FoxO and physiologically important to maintain skeletal muscle mass.-
Formato: dc.formatapplication/pdf-
Idioma: dc.languageen-
Direitos: dc.rightsrestrito-
Palavras-chave: dc.subjectSkeletal muscle plasticity-
Palavras-chave: dc.subjectUbiquitin-proteasome system-
Palavras-chave: dc.subjectAdrenergic signaling-
Palavras-chave: dc.subjectProtein metabolism-
Palavras-chave: dc.subjectSkeletal muscle atrophy-
Título: dc.titleCAMP-dependent protein kinase inhibits FoxO activity and regulates skeletal muscle plasticity in mice.-
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