Artículos de revistas
Regulation of insulin-stimulated tyrosine phosphorylation of Shc and IRS-1 in the muscle of rats: effect of growth hormone and epinephrine
Registro en:
Febs Letters. Elsevier Science Bv, v. 421, n. 3, n. 191, n. 196, 1998.
0014-5793
WOS:000071737700004
10.1016/S0014-5793(97)01560-3
Autor
Thirone, ACP
Paez-Espinosa, EV
Carvalho, CRO
Saad, MJA
Institución
Resumen
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. (C) 1998 Federation of European Biochemical Societies. 421 3 191 196