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Originally published In Press as doi:10.1074/jbc.M211715200 on February 27, 2003

J. Biol. Chem., Vol. 278, Issue 19, 16675-16682, May 9, 2003
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Involvement of Histone Acetylation in Ovarian Steroid-induced Decidualization of Human Endometrial Stromal Cells*

Nozomi SakaiDagger , Tetsuo MaruyamaDagger §, Rei SakuraiDagger , Hirotaka MasudaDagger , Yurie YamamotoDagger , Aki ShimizuDagger , Ikuko KishiDagger , Hironori AsadaDagger , Satoshi Yamagoe, and Yasunori YoshimuraDagger

From the Dagger  Department of Obstetrics and Gynecology, School of Medicine, Keio University, Shinanomach 35, Shinjuku-ku, Tokyo 160-8582 and the  Department of Bioactive Molecules, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo 162-8640, Japan

Histone acetyltransferases and histone deacetylases (HDACs) determine the acetylation status of histones, regulating gene transcription. Decidualization is the progestin-induced differentiation of estrogen-primed endometrial stromal cells (ESCs), which is crucial for implantation and maintenance of pregnancy. We here show that trichostatin A (TSA), a specific HDAC inhibitor, enhances the up-regulation of decidualization markers such as insulin-like growth factor binding protein-1 (IGFBP-1) and prolactin in a dose-dependent manner that is directed by 17beta -estradiol (E2) plus progesterone (P4) in cultured ESCs, but not glandular cells, both isolated from human endometrium. Morphological changes resembling decidual transformation were also augmented by co-addition of TSA. Acid urea triton gel analysis and immunoblot using acetylated histone type-specific antibodies demonstrated that treatment with E2 plus P4 significantly increased the levels of acetylated H3 and H4 whose increment was augmented by co-treatment with TSA. Chromatin immunoprecipitation assay revealed that treatment with E2 plus P4 increased the amount of proximal progesterone-responsive region of IGFBP-1 promoter associated with acetylated H4, which was dramatically enhanced by co-addition of TSA. Taken together, our results suggest that histone acetylation is deeply involved in differentiation of human ESCs and that TSA has a potential as an enhancer of decidualization through promotion of progesterone action.

* This work was supported by the Ministry of Education, Science and Culture of Japan (Grants C1367143 to T. M. and B12470348 to Y. Y.), by Keio Gijuku Academic Development Funds (to T. M.), and by grants from the Keio Health Counseling Center (to T. M.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Tel.: 81-3-3353-1211 (ext. 62916); Fax: 81-3-3226-1667; E-mail: tetsuo@sc.itc.keio.ac.jp.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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