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

3 Beta-hydroxysteroid dehydrogenase-isomerase activity in bovine adrenocortical cells in culture: lack of response to ACTH treatment.

Marston SA, Waterman MR, McCarthy JL
J Steroid Biochem. 1985 22 (6): 789-94

PMID: 2991660 · DOI:10.1016/0022-4731(85)90287-0

Primary cultures of bovine adrenocortical cells (BAC) were used to determine whether the adrenal microsomal 3 beta-hydroxysteroid dehydrogenase-isomerase complex (3 beta-HSD), like the 17 alpha-hydroxylase (17-OHase), responded to ACTH treatment with an increase in activity. Both enzymes influence the steroidogenic path leading to 17 alpha-hydroxyprogesterone formation and thus could affect adrenal androgen biosynthesis. 3 beta-HSD Activity in postmitochondrial supernatant fluid, homogenates or cell monolayers remained unchanged after cells had been maintained in 1 microM ACTH up to 48 h. Since ACTH exposure led to a marked increase in 17-OHase activity over the same time period, it is concluded that, under the conditions used, the 3 beta-HSD-isomerase complex in BAC is nonresponsive to tropic hormone treatment.

MeSH Terms (10)

3-Hydroxysteroid Dehydrogenases Adrenal Cortex Adrenocorticotropic Hormone Animals Cattle Cells, Cultured Kinetics Progesterone Progesterone Reductase Steroid 17-alpha-Hydroxylase

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