Abstract
The inhibition of human prostatic 5α-reductase by androstenedione (A), 4-hydroxyandrostenedione (4-OH-A), and 4-methoxyandrostenedione (4-MeO-A) was studied. All three steroids inhibited 5α-reductase in a concentration-dependent manner. The inhibition was competitive with respect to testosterone and non-competitive with respect to NADPH, indicating that these compounds inhibit 5α-reductase by acting as alternative substrates. K j values obtained were in the range 0.21–0.3 μM (A), 1.01–2.04 μM (4-OH-A), and 10.2–28.3 μM (4-MeO-A). Thus the two derivatives of androstenedione are poor inhibitors of 5α-reductase and appear to have limited clinical potential.
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