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

J Steroid Biochem. 1985 Jun;22(6):789-94. doi: 10.1016/0022-4731(85)90287-0.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 3-Hydroxysteroid Dehydrogenases / metabolism*
  • Adrenal Cortex / drug effects
  • Adrenal Cortex / enzymology*
  • Adrenocorticotropic Hormone / pharmacology*
  • Animals
  • Cattle
  • Cells, Cultured
  • Kinetics
  • Progesterone / biosynthesis
  • Progesterone Reductase / metabolism*
  • Steroid 17-alpha-Hydroxylase / metabolism

Substances

  • Progesterone
  • Adrenocorticotropic Hormone
  • 3-Hydroxysteroid Dehydrogenases
  • Progesterone Reductase
  • Steroid 17-alpha-Hydroxylase