Dicyclohexane derivatives that bind to androgen-binding protein (ABP) also inhibit hormone stimulated aromatase activity in rat Sertoli cells.

Dicyclohexane derivatives are known to inhibit testosterone binding to rat androgen-binding protein (ABP) a secretory product of Sertoli cells. In this paper we show that these compounds also inhibit the aromatization of testosterone by Sertoli cells in response to cyclic AMP and to hormones that act via this nucleotide. The inhibitory activity of the nonsteroidal androgen analogues is dose-dependent and roughly parallels their ability to interfere with the aromatase activity in human placental microsomes and their affinity for ABP. Diethylstilbestrol and mesohexestrol--two nonsteroidal estrogens which resemble the dicyclohexane derivatives--also inhibit aromatase activity in Sertoli cells and placental microsomes. The effects of the synthetic estrogens on Sertoli cells, however, are less specific. Unlike the dicyclohexane derivatives they also block hormone induced activation of the adenylate cyclase. We conclude that dicyclohexane derivatives are representative of a novel series of inhibitors of aromatase activity.