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Vol. 287, Issue 2, 504-507, November 1998

20beta -Hydroxysteroid Dehydrogenase Catalyzes Ketone-Reduction of Acetohexamide, an Oral Antidiabetic Drug, in Liver Microsomes of Adult Male Rats

Hidenori Takada, Masaki Otagiri and Yorishige Imamura

Faculty of Pharmaceutical Sciences, Kumamoto University, 5-1, Oe-honmachi, Kumamoto 862-0973, Japan

We examined the catalytic properties and physiological function of an enzyme responsible for the ketone-reduction of acetohexamide, an oral antidiabetic drug, in liver microsomes of adult male rats. Progesterone, 17alpha -hydroxyprogesterone, cortisone and cortisol, which have a ketone group at 20-position of C21-steroids, were potent inhibitors for ketone-reduction of acetohexamide in liver microsomes of adult male rats. Progesterone was also found to inhibit competitively the ketone-reduction of acetohexamide, suggesting that the ketone-reduction of acetohexamide and progesterone is catalyzed by the same enzyme. When progesterone was used as a substrate, 20beta -hydroxysteroid dehydrogenase present in liver microsomes of adult rats, such as acetohexamide reductase, exhibited a male-specific and androgen-dependent activity. Furthermore, a significant correlation was observed between the activities of 20beta -hydroxysteroid dehydrogenase and acetohexamide reductase in liver microsomes of individual male rats at various ages. Based on all results, we conclude that 20beta -hydroxysteroid dehydrogenase catalyzes the ketone-reduction of acetohexamide in liver microsomes of adult male rats.

0022-3565/98/2872-0504$03.00/0
THE JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS
Copyright © 1998 by The American Society for Pharmacology and Experimental Therapeutics


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