Synchronous generation of ovarian hCG binding sites and LH-sensitive adenylate cyclase in immature rats following treatment with pregnant mare serum gonadotropin.
J Cyclic Nucleotide Res, 1977/6;3(3):163-76.
Salomon Y, Yanovsky A, Mintz Y, Amir Y, Lindner HR
PMID: 198442
Abstract
A concomitant increase in the activity of LH-senstive adenylate cyclase and in the number of LH/hCG binding sites was induced in ovaries of immature rats upon administration of pregnant mare serum gonadotropin (PMSG), a hormone preparation known to have predominantly follicle stimulation (FSH-like) activity. When an optimal dose of PMSG (15 i.u./rat) was administered to 25-day-old rats, specific activity of LH-dependent adenylate cyclase and the number of binding sites for LH/hCG per mg protein remained unchanged during the first 24h, but 48h after injection a 2-to 4-fold increase in both parameters was observed. By contrast, there was no change in basal adenylate cyclase activity or in the response of the enzyme to the stimulatory action of guanosine-5'-(beta gamma-imino) triphosphate (Gpp (NH)p), GTP, or NaF. Specific activity of succinate cytochrome c reductase, glucose-6-phosphatase and 5'-nucleotidase were found to be unaffected by the hormonal pretreatment, although total protein determined in these homogenates increased 3-fold in the course of this treatment. It is inferred that during follicular maturation, FSH enhances the responsiveness of ovarian adenylate cyclase to LH by stimulating the insertion of LH/hCG-receptors into the cell membrane.
MeSH terms
Adenylyl Cyclases; Animals; Chorionic Gonadotropin; Dose-Response Relationship, Drug; Female; Glucose-6-Phosphatase; Gonadotropins, Equine; Guanosine Triphosphate; Luteinizing Hormone; Nucleotidases; Ovary; Rats; Receptors, Cell Surface; Succinate Cytochrome c Oxidoreductase
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