Regulation of insulin receptor kinase activity by insulin mimickers and an insulin antagonist |
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| Authors: | R A Roth D J Cassell B A Maddux I D Goldfine |
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| Institution: | 1. Cell Biology Laboratory, Mount Zion Hospital and Medical Center, San Francisco, CA 94120 USA;2. Department of Medicine, Mount Zion Hospital and Medical Center, San Francisco, CA 94120 USA;3. Department of Physiology, University of California, San Francisco, CA, USA;4. Department of Medicine, University of California, San Francisco, CA, USA |
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| Abstract: | 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 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. |
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| Keywords: | To whom correspondence should be addressed Present address: King's College London Department of Physiology Strand London WC2R 2LS |
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