Lamprey but not porcine insulin binds with different affinity to lamprey and rat hepatocytes.

The displacement of porcine [125I] insulin bound to rat and lamprey isolated hepatocytes with unlabeled lamprey and porcine insulins was investigated. Binding affinity of lamprey insulin for insulin receptor of rat was similar to that of porcine insulin. In contrast, the binding affinity of lamprey insulin for its own insulin receptor was higher than for a rat receptor. To determine the binding affinity constants of lamprey insulin receptor, the competition binding experiments were carried out on isolated lamprey hepatocytes using lamprey insulin as unlabeled ligand and tracer. The affinity of the same binding sites on lamprey hepatocytes was assessed in similar experiments but employing porcine insulin as unlabeled ligand and tracer. It was found that while Kd of low affinity binding sites on lamprey hepatocytes were similar for lamprey and porcine insulins, the Kd of high affinity binding sites was different: the displacement curve for lamprey insulin being shifted to the left as compared to the curve for porcine insulin. The number of high and low affinity binding sites, calculated independently in Scatchard plots, was equal. We conclude that the high affinity insulin binding sites of lamprey but not of rat hepatocytes reveal some species specificity in ligand-receptor interaction.