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Título: | Role of ubiquitin-proteasome-dependent proteolytic process in degradation of muscle proteic from diabetic rabbits. |
Autor(es): | Galban, Victor Diaz Evangelista, Elísio Alberto Migliorini, Renato Hélios Kettelhut, Isis do Carmo |
Palavras-chave: | Insulin deficiency Skeletal muscle extracts |
Data do documento: | 2001 |
Referência: | GALBAN, 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. |
Resumo: | The 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. |
URI: | http://www.repositorio.ufop.br/handle/123456789/7914 |
Link para o artigo: | http://link.springer.com/article/10.1023/A:1012260605910 |
DOI: | https://doi.org/10.1023/A:1012260605910 |
ISSN: | 1573-4919 |
Aparece nas coleções: | DECBI - Artigos publicados em periódicos |
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ARTIGO_RoleUbiquitinProteasome.pdf Restricted Access | 183,05 kB | Adobe PDF | Visualizar/Abrir |
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