Michael Waterman
Faculty Member
Last active: 2/12/2015

Regulation of the biosynthesis of steroidogenic enzymes.

Simpson ER, Mason JI, John ME, Zuber MX, Rodgers RJ, Waterman MR
J Steroid Biochem. 1987 27 (4-6): 801-5

PMID: 2826909 · DOI:10.1016/0022-4731(87)90152-x

Recombinant DNA technology can permit study of the regulation of steroid hydroxylase gene expression at three levels. The first of these is cAMP-regulated gene expression. In the adrenal, ACTH, via cAMP, increases the expression of the genes for all of the cytochrome P-450 species involved in the steroid biosynthetic pathway, as well as the iron-sulfur protein, adrenodoxin. This action of cAMP is inhibited by cycloheximide, suggestive of the involvement of a regulatory protein factor in mediating this action of cAMP. The second level is tissue-specific regulation of steroid hydroxylase gene expression. An example of this which we have studied is the expression of cholesterol side-chain cleavage cytochrome P-450 (P-450sec) and 17 alpha-hydroxylase cytochrome P-450 (P-450(17) alpha) in the bovine ovary. P-450sec is expressed at high levels in the corpus luteum but at low levels in follicles, whereas P-450(17)alpha is expressed in follicles, but is undetectable in the corpus luteum. The third level is fetal imprinting. A number of the cytochrome P-450 species involving in the steroidogenic pathway are expressed in the fetal adrenal at a time when exposure of the gland to ACTH is very low, suggestive that factor(s) other than pituitary ACTH mediate this expression in fetal life.

MeSH Terms (9)

Adrenal Glands Adrenocorticotropic Hormone Animals Cyclic AMP Cytochrome P-450 Enzyme System Female Gene Expression Regulation Ovary Steroid Hydroxylases

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