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dc.contributor.authorGalban, Victor Diaz-
dc.contributor.authorEvangelista, Elísio Alberto-
dc.contributor.authorMigliorini, Renato Hélios-
dc.contributor.authorKettelhut, Isis do Carmo-
dc.date.accessioned2017-06-07T16:07:21Z-
dc.date.available2017-06-07T16:07:21Z-
dc.date.issued2001-
dc.identifier.citationGALBAN, V. D. et al. Role of ubiquitin-proteasome-dependent proteolytic process in degradation of muscle proteic from diabetic rabbits. Molecular and Cellular Biochemistry, v. 225, n.1, p. 35-41, 2001. Disponível em: <http://link.springer.com/article/10.1023/A:1012260605910>. Acesso em: 19 fev. 2017.pt_BR
dc.identifier.issn1573-4919-
dc.identifier.urihttp://www.repositorio.ufop.br/handle/123456789/7914-
dc.description.abstractThe activity of ATP, ubiquitin (Ub)-dependent proteases partially purified from skeletal muscle (psoas) from alloxan diabetic rabbits was determined at different periods of insulin deficiency. Two days after alloxan injection, no change was observed in the activity of ATP, Ub-dependent proteases, but this activity increased 3 and 5 days after diabetes induction, attaining 181% of control values on the 5th day. However, after this early rise, the activity of muscle ATP, Ub-dependent proteases decreased, returning to values that did not differ significantly from controls 7 and 10 days after alloxan injection. After 15 days, the activity of these proteases was 57% lower than in muscle from control rabbits. Both the initial increase and the subsequent fall in the activity of the enzymes were prevented by insulin treatment of alloxan diabetic rabbits. The data suggest that Ub-proteasomedependent proteolysis have an important role in the control of muscle protein degradation and may be regulated by insulin.pt_BR
dc.language.isoen_USpt_BR
dc.rightsrestritopt_BR
dc.subjectInsulin deficiencypt_BR
dc.subjectSkeletal muscle extractspt_BR
dc.titleRole of ubiquitin-proteasome-dependent proteolytic process in degradation of muscle proteic from diabetic rabbits.pt_BR
dc.typeArtigo publicado em periodicopt_BR
dc.identifier.uri2http://link.springer.com/article/10.1023/A:1012260605910pt_BR
dc.identifier.doihttps://doi.org/10.1023/A:1012260605910-
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