PT  - JOURNAL ARTICLE
AU  - Hidenori Takada
AU  - Masaki Otagiri
AU  - Yorishige Imamura
TI  - 20β-Hydroxysteroid Dehydrogenase Catalyzes Ketone-Reduction of Acetohexamide, an Oral Antidiabetic Drug, in Liver Microsomes of Adult Male Rats
DP  - 1998 Nov 01
TA  - Journal of Pharmacology and Experimental Therapeutics
PG  - 504--507
VI  - 287
IP  - 2
4099  - http://jpet.aspetjournals.org/content/287/2/504.short
4100  - http://jpet.aspetjournals.org/content/287/2/504.full
SO  - J Pharmacol Exp Ther1998 Nov 01; 287
AB  - 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, 17α-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, 20β-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 20β-hydroxysteroid dehydrogenase and acetohexamide reductase in liver microsomes of individual male rats at various ages. Based on all results, we conclude that 20β-hydroxysteroid dehydrogenase catalyzes the ketone-reduction of acetohexamide in liver microsomes of adult male rats. The American Society for Pharmacology and Experimental Therapeutics