KINETIC-ANALYSIS OF RAT STEROID 5-ALPHA-REDUCTASE ACTIVITY IN PROSTATE AND EPIDIDYMIS HOMOGENATES AT NEUTRAL PH - EVIDENCE FOR TYPE-I ACTIVITY IN EPIDIDYMIS
Pn. Span et al., KINETIC-ANALYSIS OF RAT STEROID 5-ALPHA-REDUCTASE ACTIVITY IN PROSTATE AND EPIDIDYMIS HOMOGENATES AT NEUTRAL PH - EVIDENCE FOR TYPE-I ACTIVITY IN EPIDIDYMIS, Journal of steroid biochemistry and molecular biology, 57(1-2), 1996, pp. 95-101
Immunocytochemical studies and mRNA measurements have shown that the r
at epididymis-like the rat prostate-expresses both rat steroid 5 alpha
-reductase isozymes, i.e. type I and II. So far, enzyme activity measu
rements in rat epididymis homogenates, however, do not support the pre
sence of type I 5 alpha-reductase activity. Incubating homogenates of
both tissues with a wide range of substrate concentrations, we were ab
le to detect activity of both isozymes in rat prostate and epididymis
tissues at neutral pH. In rat prostate the amount of type I activity,
as measured by the V-max at pH 7.0, exceeds that of type II 5 alpha-re
ductase 50-fold. The efficiency ratio, V-max/K-m, of the type I isozym
e accounts for 25% of the total in vivo potential activity. A possible
anabolic role for the type I isozyme in rat prostate was thus surmise
d. In rat epididymis the V-max of type I and type II 5 alpha-reductase
at pH 7.0 were similar. Comparison of the efficiency ratio V-max/K-m
of either isozyme in the rat epididymis, however, suggested that the t
ype II isozyme would play the major role in the 5 alpha-reduction of t
estosterone at physiological concentrations and at neutral pH. The spe
cific localization of the isozymes should be considered to allow for c
orrect quantification of their in vivo contribution to dihydrotestoste
rone formation. (C) 1996 Elsevier Science Ltd.