Abstract
Our objective was to evaluate a convenient in vitro model for measuring steroid affinities to the human androgen receptor. The ability3 of unlabeled analogues of dihydrotestosterone (DHT) to compete with [3H]DHT for binding to the receptor in human fibroblasts was measured and expressed relative to DHT. The C-3 ketone group and the planar configuration of the A and B rings were critical for binding. Absence of the 10β-methyl group increased affinity of the androstane compounds for the receptor. The 17β-hydroxyl group was also essential for high affinity binding and addition of a 17α -methyl group enhanced binding. Binding of steroids with a Δ4 double bond was consistently less than that of the 5α-reduced steroids. This was true of both the androstene and estrene series. We conclude that human foreskin fibroblasts offer a useful model for in vitro studies characterizing the effects of steroid structural modifications on binding to the human androgen receptor.
Original language | English (US) |
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Pages (from-to) | 617-626 |
Number of pages | 10 |
Journal | Steroids |
Volume | 41 |
Issue number | 5 |
DOIs | |
State | Published - May 1983 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Endocrinology
- Pharmacology
- Clinical Biochemistry
- Organic Chemistry