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Regulation of insulin receptor kinase activity by insulin mimickers and an insulin antagonist


Biochemical & Biophysical Research Communications 115(1): 245-252
Regulation of insulin receptor kinase activity by insulin mimickers and an insulin antagonist
Three agents which mimic insulin action in intact cells (concanavalin A, wheat germ agglutinin and polyclonal insulin receptor antibody), mimicked insulin's ability to stimulate the kinase activity of purified insulin receptors. In contrast, monoclonal insulin receptor antibody, an antagonist of insulin action, did not stimulate the phosphorylation of the insulin receptor either in intact [human lymphocytes] IM-9 cells or in purified receptor preparations. This antibody, however, antagonized the ability of insulin to stimulate the phosphorylation of the receptor both in intact cells and in the purified receptor. These studies with insulin mimickers and an insulin antagonist are consistent with a role for the kinase activity of the receptor mediating the actions of insulin.

Accession: 006288767

PMID: 6351861

DOI: 10.1016/0006-291x(83)90996-8

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