Targeted Disruption Of Inos Prevents Lps-induced S-nitrosation Of Irbeta/irs-1 And Akt And Insulin Resistance In Muscle Of Mice.

dc.creatorCarvalho-Filho, Marco A
dc.creatorUeno, Mirian
dc.creatorCarvalheira, José B C
dc.creatorVelloso, Lício A
dc.creatorSaad, Mario J A
dc.date2006-Sep
dc.date2015-11-27T13:05:23Z
dc.date2015-11-27T13:05:23Z
dc.date.accessioned2018-03-29T01:02:42Z
dc.date.available2018-03-29T01:02:42Z
dc.identifierAmerican Journal Of Physiology. Endocrinology And Metabolism. v. 291, n. 3, p. E476-82, 2006-Sep.
dc.identifier0193-1849
dc.identifier10.1152/ajpendo.00422.2005
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/16638822
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/196741
dc.identifier16638822
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1296974
dc.descriptionWe 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 beta-subunit (IRbeta), insulin receptor substrate 1(IRS-1), and Akt. S-nitrosation of IRbeta 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 IRbeta 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 IRbeta/IRS-1 and Akt. In the muscle of iNOS(-/-) mice, we did not observe enhanced iNOS expression or any S-nitrosation of IRbeta/IRS-1 and Akt after LPS treatment. Moreover, insulin resistance was not present. The preservation of insulin-induced tyrosine phosphorylation of IRbeta 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.
dc.description291
dc.descriptionE476-82
dc.languageeng
dc.relationAmerican Journal Of Physiology. Endocrinology And Metabolism
dc.relationAm. J. Physiol. Endocrinol. Metab.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAdipose Tissue
dc.subjectAnimals
dc.subjectBlood Glucose
dc.subjectInsulin
dc.subjectInsulin Receptor Substrate Proteins
dc.subjectInsulin Resistance
dc.subjectLipopolysaccharides
dc.subjectLiver
dc.subjectMice
dc.subjectMice, Inbred Balb C
dc.subjectMice, Knockout
dc.subjectMuscle, Skeletal
dc.subjectNitric Oxide Synthase Type Ii
dc.subjectNitrosation
dc.subjectPhosphoproteins
dc.subjectPhosphorylation
dc.subjectProtein Processing, Post-translational
dc.subjectProto-oncogene Proteins C-akt
dc.subjectReceptor, Insulin
dc.titleTargeted Disruption Of Inos Prevents Lps-induced S-nitrosation Of Irbeta/irs-1 And Akt And Insulin Resistance In Muscle Of Mice.
dc.typeArtículos de revistas


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