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Effect of glucagon on insulin receptor substrate‐1 (IRS‐1) phosphorylation and association with phosphatidylinositol 3‐kinase (PI 3‐kinase)
Author(s) -
Saad Mario J.A.,
Hartmann Luiz G.C.,
de Carvalho Daniela S.,
Galoro Cesar A.O.,
Brenelli Sigisfredo L.,
Carvalho Carla R.O.
Publication year - 1995
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 - 10.1016/0014-5793(95)00809-n
Subject(s) - phosphatidylinositol , insulin receptor , insulin receptor substrate , pi , kinase , irs1 , phosphorylation , chemistry , irs2 , endocrinology , medicine , insulin , biochemistry , biology , insulin resistance
In the present study we have examined the levels and phosphorylation state of the insulin receptor and insulin receptor substrate 1 (IRS‐1) as well as the association between IRS‐1 and phosphatidylinositol 3‐kinase (PI 3‐kinase) in the liver and muscle of rats treated with glucagon. There was a decrease in the insulin‐stimulated receptor and IRS‐1 phosphorylation levels which was paralleled by a reduced association between IRS‐1 and PI 3‐kinase in vivo in the liver and muscle of glucagon‐treated rats. These observations suggest that glucagon, probably acting through cAMP, may impair insulin signaling in the three early steps in insulin action after binding.