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Interaction of the Monoclonal Antibodies lR-1 and IR-3 with Insulin and Somatomedin-C Receptors

The Wellcome Research Laboratories, Research Triangle Park North Carolina 27709;
The Department of Pediatrics, University of North Carolina School of Medicine Chapel Hill,North Carolina 27514

Address requests for reprints to: Dr. Steven Jacobs, Wellcome Research Laboratories, Burroughs Wellcome Company, 3030 Cornwallis Road, Research Triangle Park, North Carolina 27709.

Abstract

IR-3, a monoclonal antibody that interacts with the somatomedin-C receptor, inhibited the binding of somatomedin- C, but not of insulin, to human placental membranes and intact IM-9 cells. IR-1, a monoclonal antibody that interacts with the insulin receptor, did not inhibit the binding of either hormone. Inhibition of somatomedin-C binding by IR-3 was mainly due to a decrease in its affinity. ¹²⁵I-Labeled IR-3 bound specifically to placental membranes and intact IM-9 cells and was inhibited by concentrations of unlabeled IR-3 that were lower than those required to inhibit somatomedin-C binding. [¹²⁵I]IR-3 binding was also inhibited by somatomedin-C and insulin, but only at very high concentrations. A410, a rabbit antiserum that reacts with both receptors for insulin and somatomedin- C, also inhibited labeled IR-3 binding. IR-I did not. These results help to define the epitopes with which these antibodies interact. (Endocrinology 118: 223-226, 1986)

Received March 21, 1985.

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