Role of carbohydrate in human chorionic gonadotropin: Deglycosylation uncouples hormone-receptor complex and adenylate cyclase system

Previous work has shown that deglycosylation of human chorionic gonadotropin (hCG) does not affect its receptor binding characteristics, but its ability to stimulate intracellular cyclic AMP accumulation and steroidogenesis in ovarian cells is abolished. To identify the site at which carbohydrate of hCG is involved in the mechanism of action of the hormone, we have studied adenylate cyclase activity in ovarian membrane preparations in response to deglycosylated and native hCG. The deglycosylated hCG does not stimulate adenylate cyclase of ovarian membrane preparation and also it acts as an inhibitor of hCG action. Data are presented to show that both hCG- and catecholamine receptors are coupled to the same adenylate cyclase complex. Since adenylate cyclase activity in the presence of deglycosylated hCG remains still responsive maximally to catecholamines, it indicates that the adenylate cyclase complex is functional and is unaffected by the interaction of deglycosylated hCG to its receptor. This is further supported by the fact that the deglycosylated hCG does not impair the maximal stimulation of adenylate cyclase by guanine nucleotides. Thus, the site of action of the carbohydrate of hCG is prior to the coupling of the hormone-receptor complex and the adenylate cyclase system.