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Regulation of insulin‐stimulated tyrosine phosphorylation of Shc and IRS‐1 in the muscle of rats: effect of growth hormone and epinephrine
Author(s) -
Thirone Ana C.P,
Paez-Espinosa Enma V,
Carvalho Carla R.O,
Saad Mario J.A
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01560-3
Subject(s) - insulin receptor , phosphorylation , insulin receptor substrate , tyrosine phosphorylation , insulin , endocrinology , irs1 , medicine , insulin like growth factor 1 receptor , irs2 , chemistry , receptor , biology , biochemistry , insulin resistance , growth factor
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.