Testicular receptors of human chorionic gonadotrophin in adult men. Binding and degradation of the hormone.

Abstract

Binding and degradation of human chorionic gonadotrophin (hCG) to testicular tissue obtained by biopsy from 9 men with gonadal disorders were investigated. Vacant hCG receptors were assayed in partially purified testicular homogenates using [125I]hCG (radioiodinated with chloramine T). Degradation of [125I]hCG during exposure to human testicular preparations was measured in terms of the ability of supernatants to specifically bind to rat testicular receptors. Binding of [125]hCG was time and temperature dependent. At 37 degrees C, a maximum was reached at 8 h. It was also found to be a saturable process with respect to homogenate and hormone concentrations. Association constants and number of binding sites determined in 9 men, using Scatchard plot and saturation curve analysis ranged, respectively, from 0.2 to 1.8 x 10(10) M-1 and from 92 to 3427 fmol/g testis or 7 to 380 fmol/mg protein. Degradation of [125I]hCG increased with temperature and time of exposure to human testicular homogenate. It increased also with increasing human testicular homogenate concentration and substrate concentrations. For a similar concentration of [125I]hCG, per cent of degraded hormone ranged from 32 to 57, according to the subjects. These results show that human testicular homogenates are capable of binding and degrading hCG in vitro. Biological and physiological implications of degradation for hormone binding are discussed.