Characteristics of steroid hormone binding systems in hepatocyte plasma membranes

Abstract

Parameters of binding of cortisone and estradiol to plasma membranes of rat hepatocytes were studied by the method of liquid scintillation radiometry. The presence of two systems for the binding of these hormones in the membranes was demonstrated. One system is specific (saturable) and binds hormones in physiological concentrations. The capacity and affinity of this system for cortisone are significantly higher than for estradiol. The binding parameters within the temperature range from 4 to 37°C for cortisone and estradiol respectively are: Dissociation constant 2.1–3 and 2.7–4.5 nM, number of binding sites 2–2.4 and 0.14–0.18 nmoles/mg protein. Experiments with p-chloromercuribenzoate demonstrate the role of proteins in the working of this system. The second (unsaturable) system is nonspecific and its function is determined by the lipid component of the membranes. The affinity of corticosteroids for hepatocytes is probably due to the activity of the (saturable) specific system of the plasma membranes of these cells.