Regulation Of Insulin-stimulated Tyrosine Phosphorylation Of Shc And Shc/grb2 Association In Liver, Muscle, And Adipose Tissue Of Epinephrine- And Streptozotocin-treated Rats.

dc.creatorPáez-Espinosa, V
dc.creatorRocha, E M
dc.creatorVelloso, L A
dc.creatorSaad, M J
dc.date2001-Apr
dc.date2015-11-27T12:29:21Z
dc.date2015-11-27T12:29:21Z
dc.date.accessioned2018-03-29T00:56:07Z
dc.date.available2018-03-29T00:56:07Z
dc.identifierEndocrine. v. 14, n. 3, p. 295-302, 2001-Apr.
dc.identifier1355-008X
dc.identifier10.1385/ENDO:14:3:295
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/11444425
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/195042
dc.identifier11444425
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1295275
dc.descriptionShc protein phosphorylation has been extensively characterized as the initial step that activates a complex mitogenic pathway through its association with Grb2. In the present study, we investigated the adrenergic control of insulin-induced Shc phosphorylation and Shc-Grb2 association, and the modulating effect of streptozotocin-induced diabetes mellitus on Shc phosphorylation and Shc/Grb2 association. Acute treatment with epinephrine, which leads to a normoglycemic insulin-resistant state, does not affect insulin-induced Shc tyrosine phosphorylation or Shc-Grb2 association in liver, muscle, or fat. By contrast, a significant increase in insulin-induced Shc phosphorylation is observed in liver and muscle of rats treated with streptozotocin. The association of Shc/Grb2 is also increased in both tissues following insulin treatment. These data suggest that while epinephrine preserves the insulin-induced phosphorylation of Shc and the mitogenic pathway stimulated by Shc-Grb2 association, treatment with streptozotocin leads to a tissue-specific increase in the activity of the initial step that ultimately results in the activation of the Shc/Grb2 mitogenic pathway.
dc.description14
dc.description295-302
dc.languageeng
dc.relationEndocrine
dc.relationEndocrine
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAdaptor Proteins, Signal Transducing
dc.subjectAdaptor Proteins, Vesicular Transport
dc.subjectAdipose Tissue
dc.subjectAdrenergic Agonists
dc.subjectAnimals
dc.subjectDiabetes Mellitus, Experimental
dc.subjectEpinephrine
dc.subjectGrb2 Adaptor Protein
dc.subjectInsulin
dc.subjectLiver
dc.subjectMuscle, Skeletal
dc.subjectPhosphorylation
dc.subjectProteins
dc.subjectRats
dc.subjectReceptor, Insulin
dc.subjectShc Signaling Adaptor Proteins
dc.subjectTyrosine
dc.subjectSrc Homology Domains
dc.titleRegulation Of Insulin-stimulated Tyrosine Phosphorylation Of Shc And Shc/grb2 Association In Liver, Muscle, And Adipose Tissue Of Epinephrine- And Streptozotocin-treated Rats.
dc.typeArtículos de revistas


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