Regulation of Cbl-associated protein/Cbl pathway in muscle and adipose tissues of two animal models of insulin resistance

dc.creatorThirone, ACP
dc.creatorCarvalheira, JBC
dc.creatorHirata, AE
dc.creatorVelloso, LA
dc.creatorSaad, MJA
dc.date2004
dc.dateJAN
dc.date2014-11-15T12:54:08Z
dc.date2015-11-26T16:11:21Z
dc.date2014-11-15T12:54:08Z
dc.date2015-11-26T16:11:21Z
dc.date.accessioned2018-03-28T22:59:51Z
dc.date.available2018-03-28T22:59:51Z
dc.identifierEndocrinology. Endocrine Soc, v. 145, n. 1, n. 281, n. 293, 2004.
dc.identifier0013-7227
dc.identifierWOS:000187677400037
dc.identifier10.1210/en.2003-0575
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/80033
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/80033
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/80033
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1267067
dc.descriptionThe phosphatidylinositol 3-kinase-independent pathway to induce glucose transport may involve the tyrosine phosphorylation of the protooncogene c-Cbl. In the present study, we examined whether acute exposure to insulin stimulates the tyrosine phosphorylation of Cbl and its association with Cbl-associated protein ( CAP) in muscle and adipose tissue of rats in vivo. We report herein that insulin induces Cbl tyrosine phosphorylation and association with CAP in adipose tissue but not in muscle. We also examined the expression and tyrosyl-phosphorylation state of Cbl and CAP/Cbl association in adipose tissue of rats submitted to prolonged fasting and in monosodium glutamate (MSG)-insulin-resistant rats. An increase in Cbl phosphorylation is observed in the fat of MSG rats, parallel with an increase in association of CAP-Cbl as well as an augment in CAP and Cbl protein expression in the adipose tissue of these animals. These events are accompanied by a decrease in insulin-stimulated insulin receptor/ insulin receptor substrate (IRS)-1 tyrosine phosphorylation and an increase in the IRS-2/phosphatidylinositol 3-kinase/ Akt/Foxo1 pathway. In adipocytes of fasted rats, there is a decrease in CAP and Cbl protein expression, insulin-induced Cbl phosphorylation, and the association with CAP. In parallel, there is also a decrease in the insulin receptor/ IRSs/Akt/ Foxo1 pathway. Thus, insulin is able to induce Cbl tyrosine phosphorylation and its association with CAP in the adipose tissue of normal rats. In addition, our data provide evidence that the CAP-Cbl pathway may have a role in the modulation of adiposity in fasting and in MSG-treated rats.
dc.descriptiono TEXTO COMPLETO DESTE ARTIGO, ESTARÁ DISPONÍVEL À PARTIR DE AGOSTO DE 2015.
dc.description145
dc.description1
dc.description281
dc.description293
dc.languageen
dc.publisherEndocrine Soc
dc.publisherBethesda
dc.publisherEUA
dc.relationEndocrinology
dc.relationEndocrinology
dc.rightsembargo
dc.sourceWeb of Science
dc.subjectPhosphatidylinositol 3-kinase Activation
dc.subject3t3-l1 Adipocytes
dc.subjectRat Adipocytes
dc.subjectTyrosine Phosphorylation
dc.subjectSignaling Pathways
dc.subjectGlucose-transport
dc.subjectKinase-b
dc.subjectTranscription Factors
dc.subjectReceptor Substrate
dc.subjectGlycogen-synthase
dc.titleRegulation of Cbl-associated protein/Cbl pathway in muscle and adipose tissues of two animal models of insulin resistance
dc.typeArtículos de revistas


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