The platelet insulin receptor: detection, partial characterization, and search for a function.

A direct demonstration and partial characterization of the insulin receptor on human platelets was obtained by immunoprecipitation with a monoclonal antibody against the human insulin receptor. Two subunits were detected, one with a MW of 95 KD, which dose-dependently was phosphorylated upon challenge of the platelets with insulin and another with a MW of 69 KD that does not become phosphorylated. Retention on wheat germ agglutinin indicates that at least part of the receptor protein is glycosylated. In a search for cellular effects provoked by insulin on platelets, no changes could be detected in cAMP formation or degradation, inositol phosphate formation or phosphorylation of proteins other than the receptor itself.