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

Regulation of synthesis and activity of bovine adrenocortical NADPH-cytochrome P-450 reductase by ACTH.

Dee A, Carlson G, Smith C, Masters BS, Waterman MR
Biochem Biophys Res Commun. 1985 128 (2): 650-6

PMID: 2986621 · DOI:10.1016/0006-291x(85)90095-6

Primary, monolayer cultures of bovine adrenocortical cells have been utilized to demonstrate that ACTH regulates the synthesis and thus the activity of NADPH-cytochrome P-450 reductase. The temporal pattern of induction correlates well with that previously reported for cytochromes P-45017 alpha and P-450 C21, microsomal steroid hydroxylases serviced by P-450 reductase. Results of in vitro translation studies suggest that ACTH regulates P-450 reductase synthesis at the transcriptional level and show that the adrenocortical enzyme is synthesized as the mature form. The action of ACTH to induce P-450 reductase synthesis in the adrenal cortex can be mimicked by dibutyryl cAMP, but not by phenobarbital which induces P-450 reductase synthesis in liver.

MeSH Terms (11)

Adrenal Cortex Adrenocorticotropic Hormone Animals Cattle Cells, Cultured Immunosorbent Techniques Liver NADPH-Ferrihemoprotein Reductase Phenobarbital Swine Time Factors

Connections (1)

This publication is referenced by other Labnodes entities: