Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194130
Type: Artigo de periódico
Title: Regulation Of Insulin-stimulated Tyrosine Phosphorylation Of Shc And Irs-1 In The Muscle Of Rats: Effect Of Growth Hormone And Epinephrine.
Author: Thirone, A C
Paez-Espinosa, E V
Carvalho, C R
Saad, M J
Abstract: Insulin receptor substrate-1 (IRS-1) and Shc protein have the same binding site at the insulin receptor and compete in their association with the phosphorylated receptor. The present study demonstrates that a decrease in the level of muscle insulin receptor phosphorylation induced by chronic growth hormone (GH) treatment or acute epinephrine infusion is accompanied by a reduction in the level of IRS-1 phosphorylation and in the association with phosphatidylinositol 3-kinase. In contrast, no change is observed in insulin-stimulated Shc tyrosine phosphorylation, or in the association of this substrate with Grb2. These data suggest that a reduction in insulin receptor phosphorylation may affect post-receptor processes differentially by preserving the phosphorylation of some substrates and pathways, but not of others.
Subject: Amino Acid Sequence
Animals
Epinephrine
Hindlimb
Human Growth Hormone
Insulin
Insulin Receptor Substrate Proteins
Male
Molecular Sequence Data
Muscles
Phosphoproteins
Phosphorylation
Rats
Rats, Wistar
Tyrosine
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/9468304
Date Issue: 1998
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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