Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194216
Type: Artigo de periódico
Title: Insulin Induces Tyrosine Phosphorylation Of Shc And Stimulates Shc/grb2 Association In Insulin-sensitive Tissues Of The Intact Rat.
Author: Páez-Espinosa, V
Carvalho, C R
Alvarez-Rojas, F
Janeri, L
Velloso, L A
Boschero, A C
Saad, M J
Abstract: Shc is a novel type of tyrosine-phosphorylated protein activated in response to a wide variety of polypeptide ligands. In this study, we used immunoprecipitation and immunoblotting to examine the effect of insulin on Shc tyrosine phosphorylation and Shc/GRB2 association in insulin-sensitive tissues of the intact rat. Following an infusion of insulin, Shc was tyrosine-phosphorylated in the liver, skeletal muscle, and adipose tissue in a time- and dose-dependent fashion, which peaked 5 min after exposure to the hormone and, except in the case of adipose tissue, returned to basal values after 15 min. There was coimmunoprecipitation of Shc and the insulin receptor after stimulation with insulin. Receptor tyrosine kinase activity toward Shc was also observed. Following an infusion of insulin, Shc was found to associate with GRB2. These results demonstrate that after stimulation of rat tissues with insulin, Shc binds to the insulin receptor, is tyrosine-phosphorylated, and subsequently associated with GRB2.
Subject: Adaptor Proteins, Signal Transducing
Adaptor Proteins, Vesicular Transport
Adipose Tissue
Animals
Grb2 Adaptor Protein
Immunoblotting
Immunosorbent Techniques
Insulin
Liver
Male
Muscle, Skeletal
Phosphorylation
Phosphotyrosine
Proteins
Rats
Rats, Wistar
Receptor Protein-tyrosine Kinases
Receptor, Insulin
Shc Signaling Adaptor Proteins
Rights: fechado
Identifier DOI: 10.1385/ENDO:8:2:193
Address: http://www.ncbi.nlm.nih.gov/pubmed/9704577
Date Issue: 1998
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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