Regulation of the Synthesis of Cholesterol Side-chain Cleavage Cytochrome P-450 and Adrenodoxin in Rat Leydig Cells in Culture

1984 ◽  
Vol 438 (1 Hormonal Cont) ◽  
pp. 259-268
Author(s):  
CHRISTEN M. ANDERSON ◽  
CAROLE R. MENDELSON
Keyword(s):  
Leydig Cells ◽  
Side Chain ◽  
Side Chain Cleavage ◽  
Cells In Culture ◽  
Chain Cleavage ◽  
Cytochrome P 450

Biosynthesis of Cholesterol Side-Chain Cleavage Cytochrome P-450 in Human Fetal Adrenal Cells in Culture*

Endocrinology ◽  
1983 ◽  
Vol 112 (6) ◽  
pp. 2039-2045 ◽  
Author(s):  
MASAO OHASHI ◽  
EVAN R. SIMPSON ◽  
J. IAN MASON ◽  
MICHAEL R. WATERMAN
Keyword(s):  
Side Chain ◽  
Adrenal Cells ◽  
Side Chain Cleavage ◽  
Cells In Culture ◽  
Chain Cleavage ◽  
Cytochrome P 450

scholarly journals Stimulation of cholesterol side-chain cleavage by a luteinizing-hormone-releasing hormone (luliberin) agonist (ICI 118630) in rat Leydig cells

1983 ◽  
Vol 216 (3) ◽  
pp. 747-752 ◽  
Author(s):  
M H F Sullivan ◽  
B A Cooke
Keyword(s):  
Luteinizing Hormone ◽  
Leydig Cells ◽  
Side Chain ◽  
Luteinizing Hormone Releasing Hormone ◽  
Releasing Hormone ◽  
Side Chain Cleavage ◽  
Chain Cleavage ◽  
Cleavage Enzyme ◽  
Cytochrome P 450 ◽  
Stimulation Of

The action of a luliberin (luteinizing-hormone-releasing hormone) agonist (ICI 118630) and lutropin (luteinizing hormone) on the activity of the cytochrome P-450 cholesterol side-chain cleavage enzyme in rat Leydig cells has been investigated. This has been carried out by studying the metabolism of exogenous (22R)-22- and 25-hydroxycholesterol to testosterone. It was found that both hydroxycholesterols increased testosterone production to higher levels than achieved by lutropin alone. Addition of luliberin agonist but not lutropin was found to increase further the metabolism of the hydroxycholesterol to testosterone; this occurred in the presence of saturating and subsaturating levels of the hydroxycholesterols. This effect of luliberin agonist was potentiated in the presence of lutropin. The protein synthesis inhibitor, cycloheximide, inhibited the luliberin agonist-induced stimulation of the hydroxycholesterol metabolism. At low calcium levels (1.1 microM), testosterone production was increased by addition of (22R)-22-hydroxycholesterol but the luliberin agonist effect was negated. The calmodulin inhibitor trifluoperazine inhibited (22R)-22-hydroxycholesterol-stimulated steroidogenesis and negated the luliberin agonist effect. These results indicate that luliberin agonist specifically increases the synthesis of the cytochrome P-450 cholesterol side-chain cleavage enzyme in rat testis Leydig cells.

Alteration in the expression of genes for cholesterol side-chain cleavage enzyme and 21-hydroxylase by hypophysectomy and ACTH administration in the rat adrenal

1990 ◽  
Vol 4 (3) ◽  
pp. 239-245 ◽  
Author(s):  
T. Imai ◽  
H. Seo ◽  
Y. Murata ◽  
M. Ohno ◽  
Y. Satoh ◽  
...  
Keyword(s):  
Steady State ◽  
Adrenal Weight ◽  
Side Chain ◽  
Total Rna ◽  
Side Chain Cleavage ◽  
Chain Cleavage ◽  
Acth Treatment ◽  
Steady State Levels ◽  
Cytochrome P 450

ABSTRACT The changes in steady-state levels of mRNA for cholesterol side-chain cleavage cytochrome P-450 (P-450scc) and steroid 21-hydroxylase cytochrome P-450 (P-450c21) caused by hypophysectomy and ACTH treatment were determined in rat adrenals. Hypophysectomy caused marked decreases in adrenal weight and total RNA per gland. Administration of ACTH resulted in increases in adrenal weight and total RNA. A significant correlation between the amount of RNA and adrenal weight was observed. Both P-450scc and P-450c21 mRNAs were decreased by hypophysectomy and increased by ACTH treatment. P-450scc mRNA decreased to 20% and P-450c21 mRNA to 76% of control values 1 day after hypophysectomy. ACTH caused a significant increase in P-450scc mRNA after 3 h. However, a significant increase in P-450c21 mRNA was observed 12 h after administration of ACTH. These results are concordant with previous studies in vitro utilizing cultured adrenocortical cells. Moreover, the induction of steady-state levels of P-450scc mRNA was faster than that observed by other investigators in studies in vitro. These results may indicate that integrity of the adrenal gland in vivo is important for the action of ACTH.

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