Artículos de revistas
Targeted Disruption Of Inos Prevents Lps-induced S-nitrosation Of Irβ/irs-1 And Akt And Insulin Resistance In Muscle Of Mice
Registro en:
American Journal Of Physiology - Endocrinology And Metabolism. , v. 291, n. 3, p. E476 - E482, 2006.
1931849
10.1152/ajpendo.00422.2005
2-s2.0-33748470543
Autor
Carvalho-Filho M.A.
Ueno M.
Carvalheira J.B.C.
Velloso L.A.
Saad M.J.A.
Institución
Resumen
We have previously demonstrated that the insulin resistance associated with inducible nitric oxide synthase (iNOS) induction in two different models of obesity, diet-induced obesity and the ob/ob mice, is mediated by S-nitrosation of proteins involved in insulin signal transduction: insulin receptor β-subunit (IRβ), insulin receptor substrate 1(IRS-1), and Akt. S-nitrosation of IRβ and Akt impairs their kinase activities, and S-nitrosation of IRS-1 reduces its tissue expression. In this study, we observed that LPS-induced insulin resistance in the muscle of wild-type mice, as demonstrated by reduced insulin-induced tyrosine phosphorylation of IRβ and IRS-1, reduced IRS-1 expression and reduced insulin-induced serine phosphorylation of Akt. This resistance occurred in parallel with enhanced iNOS expression, which was accompanied by S-nitrosation of IRβ/IRS-1 and Akt. In the muscle of iNOS-/- mice, we did not observe enhanced iNOS expression or any S-nitrosation of IRβ/IRS-1 and Akt after LPS treatment. Moreover, insulin resistance was not present. The preservation of insulin-induced tyrosine phosphorylation of IRβ and IRS-1, of IRS-1 protein expression, and of insulin-induced serine phosphorylation of Akt observed in LPS-treated iNOS-/- mice strongly suggests that the insulin resistance induced by LPS is iNOS mediated, probably through S-nitrosation of proteins of early steps of insulin signaling. 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