In many species of teleost, 20beta-hydroxysteroid dehydrogenase (20beta-HSD) is a key steroidogenic enzyme in the production of the oocyte maturation-inducing steroid (MIS), 17alpha, 20beta-dihydroxy-4-pregnen-3-one. In this study, 20beta-HSD in the ovary of the Japanese eel was biochemically characterized using a cell-free system. 20beta-HSD activity was located mainly in the membrane-bound fractions of the mitochondria and microsome, with lower levels detected in the cytosolic fraction. The enzymatic activity of membrane-bound 20beta-HSD was strikingly enhanced by treatment of eels with gonadotropin-rich salmon pituitary homogenate. The activity of eel ovarian mitochondrial 20beta-HSD in the presence of different solubilizing detergents was then assessed. Mitochondrial fractions solubilized by sodium deoxycholate and octhylthioglucoside retained approximately 30% of 20beta-HSD activity when compared to those of nontreated mitochondria. These results suggest that Japanese eel ovarian 20beta-HSD is composed of membrane-bound and soluble activities, and that the membrane-bound component is stimulated by gonadotropin.
Copyright 2001 Academic Press.