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Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/64803
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dc.creatorNatalia Lautherbachpt_BR
dc.creatorIsis C. Kettelhutpt_BR
dc.creatorDawit Albieiro Pinheiro Gonçalvespt_BR
dc.creatorWilian A. Silveirapt_BR
dc.creatorSílvia Paula-Gomespt_BR
dc.creatorRafael Rossi Valentimpt_BR
dc.creatorNeuza M. Zanonpt_BR
dc.creatorMarcelo G. Pereirapt_BR
dc.creatorElen H. Miyabarapt_BR
dc.creatorLuiz C. C. Navegantespt_BR
dc.date.accessioned2024-02-27T16:22:11Z-
dc.date.available2024-02-27T16:22:11Z-
dc.date.issued2022-
dc.citation.volume60pt_BR
dc.citation.spage101492pt_BR
dc.citation.epage16pt_BR
dc.identifier.doihttps://doi.org/10.1016/j.molmet.2022.101492pt_BR
dc.identifier.issn2212-8778pt_BR
dc.identifier.urihttp://hdl.handle.net/1843/64803-
dc.description.resumoObjective Although it is well established that urocortin 2 (Ucn2), a peptide member of the corticotrophin releasing factor (CRF) family, and its specific corticotrophin-releasing factor 2 receptor (CRF2R) are highly expressed in skeletal muscle, the role of this peptide in the regulation of skeletal muscle mass and protein metabolism remains elusive. Methods To elucidate the mechanisms how Ucn2 directly controls protein metabolism in skeletal muscles of normal mice, we carried out genetic tools, physiological and molecular analyses of muscles in vivo and in vitro. Results Here, we demonstrated that Ucn2 overexpression activated cAMP signaling and promoted an expressive muscle hypertrophy associated with higher rates of protein synthesis and activation of Akt/mTOR and ERK1/2 signaling pathways. Furthermore, Ucn2 induced a decrease in mRNA levels of atrogin-1 and in autophagic flux inferred by an increase in the protein content of LC3-I, LC3-II and p62. Accordingly, Ucn2 reduced both the transcriptional activity of FoxO in vivo and the overall protein degradation in vitro through an inhibition of lysosomal proteolytic activity. In addition, we demonstrated that Ucn2 induced a fast-to-slow fiber type shift and improved fatigue muscle resistance, an effect that was completely blocked in muscles co-transfected with mitogen-activated protein kinase phosphatase 1 (MKP-1), but not with dominant-negative Akt mutant (Aktmt). Conclusions These data suggest that Ucn2 triggers an anabolic and anti-catabolic response in skeletal muscle of normal mice probably through the activation of cAMP cascade and participation of Akt and ERK1/2 signaling. These findings open new perspectives in the development of therapeutic strategies to cope with the loss of muscle mass.pt_BR
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológicopt_BR
dc.description.sponsorshipFAPEMIG - Fundação de Amparo à Pesquisa do Estado de Minas Geraispt_BR
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superiorpt_BR
dc.description.sponsorshipFAPESP - Fundação de Amparo à Pesquisa do Estado de São Paulopt_BR
dc.format.mimetypepdfpt_BR
dc.languageengpt_BR
dc.publisherUniversidade Federal de Minas Geraispt_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.departmentEEF - DEPARTAMENTO DE EDUCAÇÃO FÍSICApt_BR
dc.publisher.departmentEEFFTO - ESCOLA DE EDUCAÇÃO FISICA, FISIOTERAPIA E TERAPIA OCUPACIONALpt_BR
dc.publisher.initialsUFMGpt_BR
dc.relation.ispartofMolecular Metabolismpt_BR
dc.rightsAcesso Abertopt_BR
dc.subjectUrocortin 2pt_BR
dc.subjectHypertrophypt_BR
dc.subjectFatigue resistancept_BR
dc.subjectcAMPpt_BR
dc.subject.otherHipertrofiapt_BR
dc.subject.otherFadigapt_BR
dc.subject.otherProteínaspt_BR
dc.titleUrocortin 2 promotes hypertrophy and enhances skeletal muscle function through cAMP and insulin/IGF-1 signaling pathwayspt_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://www.sciencedirect.com/science/article/pii/S2212877822000618?via%3Dihubpt_BR
dc.identifier.orcidhttps://orcid.org/0000-0003-2621-3330pt_BR
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