Antibodies to purified insulin receptor have insulin-like activity.
Antibodies to insulin receptors purified from rat liver membranes do not complete with [125I]insulin for binding to the insulin receptor but do precipitate solubilized receptors labeled with [125I]insulin. These antibodies have the insulin-like activities of enhancing glucose oxidation and inhibiting epinephrine-induced lipolysis in rat adipocytes. Thus, antibody binds to the receptor at a different site from that to which insulin binds, yet the interaction can initiate an effective biological response. These results indicate that the previously studied insulin-binding sites are the physiological macromolecular receptors for insulin.
D000052:Acanthosis Nigricans / Q000503:physiopathology; D000273:Adipose Tissue / Q000378:metabolism; D000818:Animals; D000906:Antibodies; D000937:Antigen-Antibody Reactions; D001665:Binding Sites; D001667:Binding, Competitive; D001692:Biological Transport; D004837:Epinephrine / Q000494:pharmacology; D005947:Glucose / Q000378:metabolism; D007328:Insulin / Q000378:metabolism; D008053:Lipid Mobilization; D008099:Liver / Q000276:immunology; D051381:Rats; D011972:Receptor, Insulin / Q000502:physiology*
D000906:Antibodies; D007328:Insulin; D011972:Receptor, Insulin; D005947:Glucose; D004837:Epinephrine