Alterations of 20α-Hydroxysteroid Dehydrogenase Activity in Cultured Rat Granulosa Cells by Foil icte-stimu tating Hormone and Testosterone 1
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چکیده
منابع مشابه
The transcription factor Ap-1 regulates monkey 20α-hydroxysteroid dehydrogenase promoter activity in CHO cells
BACKGROUND Monkey 20α-hydroxysteroid dehydrogenase (20α-HSD) is a catabolic enzyme responsible for converting progesterone into biologically inactive 20α-hydroxyprogesterone, thereby playing a key role in the estrous cycle or pregnancy and allowing ovulation and parturition to occur in most mammalian animals. Monkey 20α-HSD was highly abundant in ovarian and placental tissues during the pre-ovu...
متن کاملChanges in Ovarian and Placental 20α-hydroxysteroid Dehydrogenase Activity during the Pregnancy in the Rat
The enzyme 20α-hydroxysteroid dehydrogenase (20α-HSD) catabolizes progesterone to 20α-dihydroprogesterone (20α-OHP), and is appeared in rat corpora luteal and placenta. A polled samples of 10-15 placental and ovarian tissues collected from each individual rat were subjected to measurement of 20α-HSD activity. A 20α-HSD activity in the cytosol fraction was based on the generation of NADPH. In th...
متن کاملMolecular characterization of bovine placental and ovarian 20α-hydroxysteroid dehydrogenase
The enzyme 20α-hydroxysteroid dehydrogenase (20α-HSD) catalyzes the conversion of progesterone to its inactive form, 20α-hydroxyprogesterone. This enzyme plays a critical role in the regulation of luteal function in female mammals. In this study, we conducted the characterization and functional analyses of bovine 20α-HSD from placental and ovarian tissues. The nucleotide sequence of bovine 20α-...
متن کاملBiosynthesis of proteoglycans by rat granulosa cells cultured in vitro.
Rat ovarian granulosa cells were isolated from immature female rats after stimulation with pregnant mare's serum gonadotropin and then maintained in culture. Proteoglycans were labeled using [35S]sulfate, D-[3h]glucosamine, or L-[3H]serine as precursors. 35S-labeled proteoglycans in the medium increased linearly up to 72 h after a 6- to 8-h lag period, and those in a 4 M guanidine HCl extract o...
متن کاملTestosterone decreases 3beta-hydroxysteroid dehydrogenase-isomerase messenger ribonucleic acid in cultured mouse Leydig cells by a strain-specific mechanism.
We previously reported a strain-related difference in basal 3beta-hydroxysteroid dehydrogenase-isomerase (3betaHSD) activity in response to testosterone in cultured Leydig cells. The data suggested that the response to testosterone was androgen receptor mediated and that testosterone was acting via a trans-acting factor distal to the androgen receptor to regulate Leydig cell basal 3betaHSD acti...
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ژورنال
عنوان ژورنال: Biology of Reproduction
سال: 1985
ISSN: 0006-3363,1529-7268
DOI: 10.1095/biolreprod32.5.998