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

Comparison of cAMP-responsive DNA sequences and their binding proteins associated with expression of the bovine CYP17 and CYP11A and human CYP21B genes.

Waterman MR, Kagawa N, Zanger UM, Momoi K, Lund J, Simpson ER
J Steroid Biochem Mol Biol. 1992 43 (8): 931-5

PMID: 22217838 · DOI:10.1016/0960-0760(92)90321-9

Maintenance of optimal steriodogenic capacity in the adrenal cortex requires the action of the peptide hormone ACTH. Upon binding to its cell surface receptor ACTH activates adenylate cyclase leading to elevated levels of intracellular cAMP which in turn enhances transcription of the genes encoding the enzymes involved in the conversion of cholesterol to the steroid hormones. By deletion analysis of their upstream regions, the genes encoding the steroid hydroxylases P450c17, P450c21 and P450scc (CYP17, CYP21B and CYP11A, respectively) were found to contain unique cAMP-responsive sequences (CRSs). These sequences are unique in the sense that they have not previously been described to be associated with other genes whose transcription is regulated by cAMP. Furthermore they appear to bind unique nuclear proteins or transcription factors not previously associated with cAMP-dependent transcription. This review summarizes the relatedness of these CRSs in the bovine CYP17 and CYP11A genes and the human CYP12B gene and provides an up-to-date summary of the properties of their nuclear DNA-binding proteins.

Copyright © 1992. Published by Elsevier Ltd.

MeSH Terms (12)

Adrenal Cortex Animals Cattle Cholesterol Side-Chain Cleavage Enzyme Cyclic AMP Cyclic AMP Response Element-Binding Protein Gene Expression Regulation, Enzymologic Humans Isoenzymes Response Elements Steroid 17-alpha-Hydroxylase Steroid 21-Hydroxylase

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