Qin K N, Rosenfield R L
Pritzker School of Medicine, University of Chicago Children's Hospital, University of Chicago, Illinois 60637-1470, USA.
J Soc Gynecol Investig. 2000 Jan-Feb;7(1):61-4. doi: 10.1016/s1071-5576(99)00067-2.
Conversion of androstenedione to testosterone, the most potent androgen secreted by the ovary, is carried out by androgenic 17 beta-hydroxysteroid dehydrogenase (17 beta-HSD) activity. The molecular basis for this is unclear. We tested the hypothesis that type 5 17 beta-HSD (17 beta-HSD5) is responsible for testosterone formation from androstenedione in the human ovary.
We used primers specific for each type of 17 beta-HSD to identify quantitatively and directly sequence the polymerase chain reaction products of a human ovary library.
17 beta-HSD1, 17 beta-HSD4, and 17 beta-HSD5 were detected in the library lysate, but not 17 beta-HSD2 or 17 beta-HSD3. 17 beta-HSD5 was the predominant androgenic form of 17 beta-HSD expressed in human ovary.
These data suggest that 17 beta-HSD5 may play a major role in testosterone biosynthesis by the human ovary. Further investigation of the regulation of 17 beta-HSD5 gene expression is warranted with regard to ovarian testosterone secretion in normal and abnormal states of ovarian function, such as polycystic ovary syndrome.