Regulation of insulin-stimulated tyrosine phosphorylation of Shc and IRS-1 in the muscle of rats: effect of growth hormone and epinephrine.
FEBS Lett
; 421(3): 191-6, 1998 Jan 16.
Article
em En
| MEDLINE
| ID: mdl-9468304
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfoproteínas
/
Tirosina
/
Epinefrina
/
Hormônio do Crescimento Humano
/
Insulina
/
Músculos
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Reino Unido