Regulation of synthesis and activity of bovine adrenocortical NADPH-cytochrome P-450 reductase by ACTH.
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.
Dee
A
A
Carlson
G
G
Smith
C
C
Masters
B S
BS
Waterman
M R
MR
D000302:Adrenal Cortex / Q000187:drug effects / Q000201:enzymology*; D000324:Adrenocorticotropic Hormone / Q000494:pharmacology*; D000818:Animals; D002417:Cattle; D002478:Cells, Cultured; D007163:Immunosorbent Techniques; D008099:Liver / Q000201:enzymology; D009251:NADPH-Ferrihemoprotein Reductase / Q000276:immunology / Q000378:metabolism*; D010634:Phenobarbital / Q000494:pharmacology; D013552:Swine; D013997:Time Factors
D000324:Adrenocorticotropic Hormone; D009251:NADPH-Ferrihemoprotein Reductase; D010634:Phenobarbital