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Type: Artigo de periódico
Title: Regulation Of Insulin-stimulated Tyrosine Phosphorylation Of Shc And Shc/grb2 Association In Liver, Muscle, And Adipose Tissue Of Epinephrine- And Streptozotocin-treated Rats.
Author: Páez-Espinosa, V
Rocha, E M
Velloso, L A
Saad, M J
Abstract: Shc 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.
Subject: Adaptor Proteins, Signal Transducing
Adaptor Proteins, Vesicular Transport
Adipose Tissue
Adrenergic Agonists
Diabetes Mellitus, Experimental
Grb2 Adaptor Protein
Muscle, Skeletal
Receptor, Insulin
Shc Signaling Adaptor Proteins
Src Homology Domains
Citation: Endocrine. v. 14, n. 3, p. 295-302, 2001-Apr.
Rights: fechado
Identifier DOI: 10.1385/ENDO:14:3:295
Date Issue: 2001
Appears in Collections:Unicamp - Artigos e Outros Documentos

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