dc.creatorRojas, FA
dc.creatorHirata, AE
dc.creatorSaad, MJA
dc.date2001
dc.dateOCT 25
dc.date2014-11-15T12:15:04Z
dc.date2015-11-26T17:19:48Z
dc.date2014-11-15T12:15:04Z
dc.date2015-11-26T17:19:48Z
dc.date.accessioned2018-03-29T00:07:28Z
dc.date.available2018-03-29T00:07:28Z
dc.identifierMolecular And Cellular Endocrinology. Elsevier Sci Ireland Ltd, v. 183, n. 41671, n. 63, n. 69, 2001.
dc.identifier0303-7207
dc.identifierWOS:000172077600009
dc.identifier10.1016/S0303-7207(01)00597-4
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/80061
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/80061
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/80061
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1282988
dc.descriptionIntracellular insulin signaling involves a series of alternative and complementary pathways created by the multiple substrates of the insulin receptor (IRS) and the various isoforms of the SH2 domain signaling molecules that can interact with substrate. In this study we investigated IRS-1 and IRS-2 tyrosine phosphorylation, their association with P13-kinase and the phosphorylation of Akt, a serine-threonine kinase situated downstream to PI 3-kinase, in liver and muscle of two animal models of insulin resistance: 72 h of fasting and STZ-diabetic rats. There was an upregulation in insulin-induced IRS-1 and IRS-2 tyrosine phosphorylation and association with P13-kinase in liver and muscle of both animal models of insulin resistance. However, Akt phosphorylation showed different regulation, increasing in fasting and decreasing in STZ-diabetic rats, Since an important difference between these two animal models of insulin resistance is the plasma glucose levels, we can suggest that in STZ diabetic rats, the reduction in Akt phosphorylation is probably related to hyperglycemia and may certainly contribute to the molecular mechanism of insulin resistance observed in these animals. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.
dc.description183
dc.description41671
dc.description63
dc.description69
dc.languageen
dc.publisherElsevier Sci Ireland Ltd
dc.publisherClare
dc.publisherIrlanda
dc.relationMolecular And Cellular Endocrinology
dc.relationMol. Cell. Endocrinol.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectinsulin
dc.subjectIRS-2
dc.subjectliver muscle
dc.subjectInsulin-receptor Substrate-1
dc.subjectProtein-kinase Akt
dc.subjectPhosphatidylinositol 3-kinase
dc.subjectGlucose-transport
dc.subjectSignal-transduction
dc.subjectGene-expression
dc.subjectAnimal-models
dc.subjectGrowth-factor
dc.subjectMuscle
dc.subjectResistant
dc.titleRegulation of IRS-2 tyrosine phosphorylation in fasting and diabetes
dc.typeArtículos de revistas


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