Direct stimulation of nucleoside triphosphatase activity in human ovarian nuclear membranes by human chorionic gonadotropin.

We previously reported that nuclei isolated from ovaries of premenopausal women contain binding sites for hCG/human LH (hLH). This study was undertaken to determine the possible functional significance of these nuclear binding sites. Upon addition to isolated ovarian (mostly luteal cells) nuclear membranes, hCG and hLH stimulated nucleoside triphosphatase (NTPase), an enzyme involved in nucleocytoplasmic transfer of mRNA, but not Mg2+-ATPase or NADH cytochrome c reductase activities, in a concentration-dependent manner. Heat-denatured hCG, isolated alpha- and beta-subunits of hCG, human FSH, PRL, and porcine relaxin had no effect on the enzyme. Addition of hCG antiserum blocked hCG's ability to stimulate NTPase activity. cAMP, which is a second messenger in hCG- and hLH-stimulated steroidogenesis, had no effect on NTPase activity. These results, which demonstrate that hCG acts on human ovarian nuclei directly, raise the possibility that internalized hCG might influence nuclear function(s) before it is eventually degraded in the lysosomes of ovarian cells.