| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
and
KATHY A. ALDERN
Department of Medicine, Division of Endocrinology/Metabolism, University of California San Diego School of Medicine La Jolla, California 92093
The activities of 3β-hydroxysteroid dehydro-genase, 17-hydroxylase, 21-hydroxylase, 11β-hydroxylase, C17,2o-lyase, and dehydroepiandrosterone sulfotransferase were measured in cultured human fetal definitive zone adrenocortical cells with and without prior exposure to 1
M ACTH for 48 h. Enzyme induction and measurements of activity were performed using serum- and lipoprotein-free conditions. ACTH induced increases of 5- to 100-fold in the activity of all of these enzymes. Although 3β-hydroxysteroid dehydrogenase activity was increased 15-fold, its activity was still an order of magnitude less than that of the hydroxylases. In contrast, when similar experiments were performed using bovine adrenocortical cells, 3β-hydroxysteroid dehydrogenase activity was similar to that of the hydroxylases after induction with ACTH. The lower activity of 3β-hydroxysteroid dehydrogenase in human cells compared to that in bovine cells resulted in different sequences of transformation of [3H]pregnenolone. The initial product in human cells, before or after induction with ACTH, was 17-hydroxypregnen-olone, which was then converted about equally to cortisol (via 17-hydroxyprogesterone and 11-deoxycortisol) and dehydro-epiandrosterone sulfate (via dehydroepiandrosterone). In contrast, bovine cells converted pregnenolone to progesterone, with or without prior exposure to ACTH, which was then converted t o 17-hydroxyprogesterone, with minimal formation of dehy-droepiandrosterone. Adrenal androgen synthesis by human ad-renocortical cells thus results from low 3β-hydroxysteroid de-hydrogenase, which is an intrinsic cell property. Since these experiments were performed using serum-free conditions, cells were not exposed to hormones other than ACTH. The results support the hypothesis that human adrenal androgen synthesis does not require a special hormone.
* This work was supported by NIH Research Grants AG-00936 from the National Institute on Aging and CA-32468 from the NCI (to P.J.H.).
To whom requests for reprints should be addressed.
Received June 13, 1983.
This article has been cited by other articles:
![]() |
K. J. Saner, T. Suzuki, H. Sasano, J. Pizzey, C. Ho, J. F. Strauss III, B. R. Carr, and W. E. Rainey Steroid Sulfotransferase 2A1 Gene Transcription Is Regulated by Steroidogenic Factor 1 and GATA-6 in the Human Adrenal Mol. Endocrinol., January 1, 2005; 19(1): 184 - 197. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. W. Aberdeen, J. S. Babischkin, W. A. Davies, G. J. Pepe, and E. D. Albrecht Decline in Adrenocorticotropin Receptor Messenger Ribonucleic Acid Expression in the Baboon Fetal Adrenocortical Zone in the Second Half of Pregnancy Endocrinology, April 1, 1997; 138(4): 1634 - 1641. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Endocrinology | Endocrine Reviews | J. Clin. End. & Metab. |
| Molecular Endocrinology | Recent Prog. Horm. Res. | All Endocrine Journals |