Role of testosterone binding to the androgen receptor in male sexual differentiation of patients with 5α-reductase deficiency

Marc Maes, Charles Sultan, Nadia Zerhouni, Stephen W. Rothwell, Claude J. Migeon

Research output: Contribution to journalArticlepeer-review

Abstract

Testosterone (T) and dihydrotestosterone (DHT) were found to bind to a specific protein in genital skin fibroblasts of a patient with 5α-reductase deficiency. While maximum number of binding sites (Bmax) were similar for both androgens, the apparent dissociation constant (KD) of the androgen receptor for T was somewhat greater than for DHT. In competition studies of [3H]-T bound to the receptor with unlabeled T or DHT, the inhibitor constant (Ki) for T was two to three fold greater than the Ki for DHT. Also, the dissociation rate constant (kD) for [3H]-T bound to the receptor was greater than for [3H]-DHT (t 1 2 for T = 10 h and t 1 2 for DHT = 74.5 h). These results suggest that T may play a role in the sexual differentiation of male patients with 5α-reductase deficiency during their fetal life and at puberty. The low degree of masculinization during fetal life would be explained by the lower affinity and faster turnover rate of the T-reeeptor complex relative to the DHT-receptor complex. The relatively greater masculinization observed at puberty would be explained by the higher plasma T levels attained in the adult when compared to the fetus.

Original languageEnglish (US)
Pages (from-to)1385-1390
Number of pages6
JournalJournal of Steroid Biochemistry
Volume11
Issue number4
DOIs
StatePublished - Oct 1979

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

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