Abstract
The regulation of steroid 17αhydroxylase in human and bovine adrenocortical cells in culture is reviewed. It is shown that (i) the long-term growth and cloning of normal human fetal adrenocortical cells in culture is feasible; (ii) the phorbol ester 12-O-tetradecanoyl phorbol 13-acetate (TPA) is an effective mitogen in both clonal cultures and non-clonal early cultures of human adrenocortical cells, and shows a selective action in promoting adrenocortical cell growth and inhibiting fibroblast growth; (iii) the key steroidogenic enzymes, 17αhydroxylase and 3βhydroxysteroid dehydrogenase (3βHSD), are under dual regulation by the cyclic AMP and protein kinase C second messenger systems; (iv) for 17αhydroxylase, this dual regulation is mediated by changes in 17αhydroxylase mRNA levels; (v) bovine adrenocortical cells can be transfected with SV40 T antigen, producing lines with elevated differentiated functions, including stabilized high expression of 17αhydroxylase; (vi) human adrenocortical cells can also be transfected with SV40 large T antigen, giving rise to functional cell lines which may be useful in future studies of 17αhydroxylase regulation.
Original language | English (US) |
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Pages (from-to) | 159-182 |
Number of pages | 24 |
Journal | Endocrine Research |
Volume | 15 |
Issue number | 1-2 |
DOIs | |
State | Published - Jan 1 1989 |
Externally published | Yes |
ASJC Scopus subject areas
- Endocrinology