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Department of Medicine, University of California, San Diego, La Jolla, California, 92161; the Medical Research Service of the Veterans Administration Medical Center, San Diego, California 92161; Department of Medicine, of Chicago Chicago, Illinois 60616
Address all correspondence and requests for reprints to: Jerrold M. Olefsky, M.D., Veterans Administration Medical Center, Medical Research Service (V-111G), 3350 La Jolla Village Drive, SAn Diego, California 92161.
An insulin-requiring diabetic patient with intermittent periods of increased insulin requirements and insulinresistance was studied. The patient was found to have high titers of antiinsulin antibodies; subfractionation of the patients serum revealed several populations of antiinsulin antibodies with differing affinities and titers for insulin. The ability of one of the insulin antibody fractions to bind [125I]iodoinsulin was markedly inhibited by the patients serum (insulin depleted) and by purified total immunoglobulin G from which antiinsulin antibodies and insulin were removed. These findings suggested an antiidiotypic antibody in the patients immunoglobulin G fraction reacting specifically with the antiinsulin antibody subfraction. Finally, the patients serum contained an antiinsulin receptor antibody, as demonstrated by the ability of serum to specifically immunoprecipitate covalently labeled soluble insulin receptors. In conclusion, these results suggest that this patient generated a widespread polyclonal response to insulin, with the development of several populations of antiinsulin antibodies. An antiidiotypic antibody to a specific insulin antibody subfraction was present in the patients serum which we believe had structural similarity to thebinding site of the insulin molecule, accounting for the reactivity of the antiidiotypic antibody with the insulin receptor. (J Clin Endocrinol Metab63: 56,1986)
Received December 9, 1985.
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