Regulation of insulin-stimulated tyrosine phosphorylation of Shc and IRS-1 in the muscle of rats: Effect of growth hormone and epinephrine

Ana C.P. Thirone, Enma V. Paez-Espinosa, Carla R.O. Carvalho, Mario J.A. Saad

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

17 Citas (Scopus)


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.

Idioma originalInglés
Páginas (desde-hasta)191-196
Número de páginas6
PublicaciónFEBS Letters
EstadoPublicada - 16 ene. 1998
Publicado de forma externa

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