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Low Expression of 3β-Hydroxy-5-Ene Steroid Dehydrogenase Gene in Human Fetal Adrenals in Vivo; Adrenocorticotropin and Protein Kinase C-Dependent Regulation in Adrenocortical Cultures

Departments of Pediatrics (R.V., P.J.M.) and Pathology (R.V., V.I., P.J.M.), University of Helsinki SF-00290 Helsinki, Finland

Address correspondence and requests for reprints to: Raimo Voutilainen, M.D., Department of Pediatrics, University of Helsinki, SF-00290 Helsinki, Finland.

Human fetal adrenals are very active in steroid production. They make large amounts of dehydroepiandrosterone sulfate which is further converted to estrogens in placenta. Fetal adrenals cannot make cortisol efficiently from cholesterol or pregnenolone, but they can convert progesterone to cortisol. To clarify the molecular basis of the very low activity of 3β-hydroxy-5-ene steroid dehydrogenase (3βHSD) in human fetal adrenals we studied the expression of 3βHSD gene in fetal adrenals in vivo and in culture conditions. Human adult adrenals, placenta and a testicular Leydig cell tumor clearly expressed 3βHSD gene when studied by Northern blotting, but fetal adrenals and ovaries had no detectable 3βHSD mRNA by this method. Polymerase chain reaction analysis of cDNA samples derived from different human tissues revealed 3βHSD gene expression in placenta, adult adrenal and adult ovarian granulosa cells after 25 cycles of amplification. Fetal adrenal samples became positive only after additional amplification cycles, which verifies the very low expression of 3βHSD gene in fetal adrenals. In cell culture conditions both ACTH and a protein kinase C regulator 12-O-tetradecanoyl phorbol-13-acetate induced 3βHSD gene expression. We conclude: 1) the very low activity of 3βHSD in human fetal adrenals is due to the low expression of this gene; 2) both cAMP and protein kinase C-dependent mechanisms regulate 3βHSD gene expression in adrenocortical cells. (J Clin Endocrinol Metab 72: 761–767, 1991)

Received February 20, 1900.

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