Sex differences in the effects of pregnenolone, progesterone, and ACTH on corticosterone secretion of bank vole (Clethrionomys glareolus) adrenals in tissue culture

1986 ◽  
Vol 64 (8) ◽  
pp. 1679-1683 ◽  
Author(s):  
Klaus M. Tähkä ◽  
Arvi I. Kahri ◽  
Raimo Voutilainen ◽  
Henrik Wallgren

Possible sex-specific differences in the basal as well as the pregnenolone-, progesterone-, and ACTH-induced glucocorticoid secretion of bank vole adrenals was studied in tissue culture by column and gas–liquid chromatography. The adrenals were cultured for 12 days and the medium was replaced after 6 days. The main glucocorticoid in this species, as in many other rodents, seems to be corticosterone since no cortisol was detected. During the first 6 days of cultivation, the administration of pregnanes (20 μg as a single dose) as well as ACTH (0.1 IU∙mL−1∙day−1) induced a marked increase (P < 0.01 or P < 0.001) in the corticosterone secretion in both sexes. The basal as well as the pregnenolone- and the ACTH-induced secretion of corticosterone was significantly (P < 0.02 or P < 0.01) greater in female than male adrenals. These functional differences were almost totally abolished after 12 days of culture. This study suggests that despite the existence of a 3β-hydroxysteroid dehydrogenase negative juxtamedullary zone (at least by histochemical criteria), female adrenals have a greater capacity to convert endogenous as well as exogenous precursors to corticosterone than male adrenals. This is at least partly due to sex differences in the activity (per gland) of the steroidogenic enzymes distal to cholesterol side-chain cleavage, 3β-hydroxysteroid Δ5-Δ4-isomerase in particular.

2009 ◽  
Vol 94 (2) ◽  
pp. 623-631 ◽  
Author(s):  
Erkut Attar ◽  
Hideki Tokunaga ◽  
Gonca Imir ◽  
M. Bertan Yilmaz ◽  
David Redwine ◽  
...  

Abstract Context: Products of at least five specific steroidogenic genes, including steroidogenic acute regulatory protein (StAR), which facilitates the entry of cytosolic cholesterol into the mitochondrion, side chain cleavage P450 enzyme, 3β-hydroxysteroid-dehydrogenase-2, 17-hydroxylase/17-20-lyase, and aromatase, which catalyzes the final step, are necessary for the conversion of cholesterol to estrogen. Expression and biological activity of StAR and aromatase were previously demonstrated in endometriosis but not in normal endometrium. Prostaglandin E2 (PGE2) induces aromatase expression via the transcriptional factor steroidogenic factor-1 (SF1) in endometriosis, which is opposed by chicken-ovalbumin upstream-transcription factor (COUP-TF) and Wilms’ tumor-1 (WT1) in endometrium. Objective: The aim of the study was to demonstrate a complete steroidogenic pathway leading to estrogen biosynthesis in endometriotic cells and the transcriptional mechanisms that regulate basal and PGE2-stimulated estrogen production in endometriotic cells and endometrium. Results: Compared with normal endometrial tissues, mRNA levels of StAR, side chain cleavage P450, 3β-hydroxysteroid-dehydrogenase-2, 17-hydroxylase/17-20-lyase, aromatase, and SF1 were significantly higher in endometriotic tissues. PGE2 induced the expression of all steroidogenic genes; production of progesterone, estrone, and estradiol; and StAR promoter activity in endometriotic cells. Overexpression of SF1 induced, whereas COUP-TFII or WT1 suppressed, StAR promoter activity. PGE2 induced coordinate binding of SF1 to StAR and aromatase promoters but decreased COUP-TFII binding in endometriotic cells. COUP-TFII or WT1 binding to both promoters was significantly higher in endometrial compared with endometriotic cells. Conclusion: Endometriotic cells contain the full complement of steroidogenic genes for de novo synthesis of estradiol from cholesterol, which is stimulated by PGE2 via enhanced binding of SF1 to promoters of StAR and aromatase genes in a synchronous fashion.


1995 ◽  
Vol 7 (5) ◽  
pp. 1213 ◽  
Author(s):  
RJ Rodgers ◽  
CA Vella ◽  
FM Young ◽  
XC Tian ◽  
JE Fortune

Prostaglandin F2 alpha (PGF2 alpha)-induced regression of the corpus luteum causes both plasma progesterone concentrations and luteal concentrations of mRNA encoding the steroidogenic enzyme 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD) to fall in parallel. To investigate the hypothesis that a decline in the concentrations of mRNA encoding steroidogenic enzymes causes plasma progesterone to fall, the luteal concentrations of the enzymes 3 beta-HSD and cytochrome P450 cholesterol side-chain cleavage were measured during induced luteolysis. Holstein heifers were treated with PGF2 alpha (25 mg Lutalyse) on Day 6 or Day 7 of the oestrous cycle and corpora lutea were collected 0 h, 2 h, 12 h, and 24 h later (n = 6, 4, 4, and 4 respectively). Analyses of the steroidogenic enzymes were carried out by Western immunoblotting. The luteal concentrations of both steroidogenic enzymes did not decrease over the 24-h period. It is concluded that, although the concentrations of mRNA encoding steroidogenic enzymes may decline in response to PGF2 alpha, this does not lead to a sufficiently rapid reduction in the concentrations of the enzymes to precede, and thus cause, the decline in plasma progesterone concentrations. Thus, the mechanism for the initial decline in plasma progesterone concentrations during luteolysis is still not known.


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