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Mol. Hum. Reprod. Advance Access published online on October 11, 2005

Molecular Human Reproduction, doi:10.1093/molehr/gah215
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© The Author 2005. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org
Received May 5, 2005
Revised June 26, 2005
Accepted July 19, 2005

Article

Characterization of 17{beta}-hydroxysteroid dehydrogenase type 4 in human ovarian surface epithelial cells

Y. Nagayoshi 1*, T. Ohba 1, H. Yamamoto 2, Y. Miyahara 1, H. Tashiro 3, H. Katabuchi 3, and H. Okamura 1

1 Department of Reproductive Medicine and Surgery, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan
2 Department of Molecular Pharmacology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan
3 Department of Gynecology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan

* To whom correspondence should be addressed.
Y. Nagayoshi, E-mail: yumikonagayoshi{at}fc.kuh.kumamoto-u.ac.jp


   Abstract

The human ovarian surface epithelium (hOSE) is a single layer of mesothelial-type primitive epithelial cells that are potential estrogen targets. It has been reported that hOSE cells can produce estrogen. However, the mechanisms that regulate estrogen level(s) in hOSE cells are not yet known. To elucidate the enzymes involved in these reactions, we examined gene expression of 17{beta}-hydroxysteroid dehydrogenases (17{beta}-HSDs) in primary hOSE (POSE) and OSE2a cells using RT-PCR. We found that POSE cells and cells of the immortalized hOSE line, OSE2a, bidirectionally converted estrone (E1) and 17{beta}-estradiol (E2). Both cell types expressed mRNA for 17{beta}-HSD type 1 (17{beta}-HSD1), suggesting that the enzyme is involved in the E1 to E2 conversion. Interestingly, both cells expressed 17{beta}-HSD4 mRNA but not 17{beta}-HSD2 mRNA. We prepared an antibody against the carboxyl terminal of 17{beta}-HSD4 (anti-17{beta}-HSD4 antibody), which recognized the 80 and 48 kDa proteins in POSE and OSE2a cells based on immunoblot analysis. Furthermore, immunohistochemical study revealed the presence of 17{beta}-HSD4 in hOSE cells in the human ovary. These results suggest that 17{beta}-HSD4 is involved in estrogen inactivation and may protect against an excessive accumulation of E2 in hOSE cells.

Keywords: estrogen/ovarian surface epithelial cells/ovary/17{beta}-HSD4.
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