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INSULIN RECEPTORS IN HUMAN ENDOTHELIAL CELLS: IDENTIFICATION AND CHARACTERIZATION¹

Divisions of Endocrinology and Hematology, U. of Iowa and VA Hosps. Iowa City, IA 52242

Specific binding of ¹²⁵I-insulin was found in cultured human endotheiial cells obtained from human umbilical veins. The binding reaction was rapid and reversible, demonstrated receptor site-site interactions of the negatively cooperative type, and was dependent on the temperature, pH and duration of incubation. At 21°C, steady-state conditions of binding occurred in 90 minutes, the pH optimum was 7.8 and less than 10% of the labeled hormone was degraded. Binding of tracer amounts of ¹²⁵I-insulin was inhibited by concentrations of unlabeled insulin as low as 0.2 ng/ml and 50% inhibition was obtained at 2–5 ng/ml of unlabeled insulin. Unlabeled porcine insulin, porcine proinsulin and desoctapeptide insulin inhibited the binding of ¹²⁵I - porcine insulin in direct proportion to their biological potencies, whereas unrelated peptide hormones were without effect. In addition, insulin binding to the cells was inhibited by antibodies against insulin receptors. We conclude that human endothelial cells possess specific receptors for insulin whose physio-chemical properties are similar to those of insulin receptors in other tissues.

Accepted May 10, 1978.

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