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Estrogen Mediates Phosphorylation of Histone H3 in Ovarian Follicle and Mammary Epithelial Tumor Cells via the Mitotic Kinase, Aurora B

Grupo de Fisiología y Biotecnología de la Reproducción (Z.T.R.-C.), Facultad de Ciencias Agrarias, Universidad de Antioquia, Medellín, Colombia; Centre de recherche en reproduction animale (Z.T.R.-C., B.D.M.), Faculté de médecine vétérinaire, Université de Montréal, St-Hyacinthe, Quebec, Canada J2S 7C6; Institut de génétique et biologie moléculaire et cellulaire (S.K, L.M., P.S.-C.), Université Louis Pasteur, 67404 Illkirch-Strasbourg, France; and Department of Pathology (K.H.B.), Baylor College of Medicine, Houston, Texas 77030

Address all correspondence and requests for reprints to: Bruce D. Murphy, Centre de recherche en reproduction animale, Faculté de médecine vétérinaire, Université de Montréal, St-Hyacinthe, Quebec, Canada J2S 7C6.

Cells of the ovarian follicle undergo extensive proliferation and differentiation from the time that the follicle escapes from the primordial state to its acquisition of ovulatory capacity. We examined the dynamic modification of the phosphorylation state of the histone H3 N-terminal tail in granulosa cells during follicular development. In rodent follicles, the granulosa cell H3 phosphorylation on Ser10 peaks during proestrus. This epigenetic mark is induced by both FSH and 17ß-estradiol (E2), acting independently. E2-induced H3 phosphorylation fails to occur in mice with inactivated -isoform of the nuclear estrogen receptor. E2 induction of histone phosphorylation is attenuated by cell cycle inhibition. Further, E2 induces the activity of the mitotic kinase, Aurora B, in a mammary tumor cell model where mitosis is estrogen receptor- dependent. These results provide evidence for mitotic regulation in follicle development by estrogen and demonstrate a previously undiscovered mechanism for induction of cell proliferation in ovarian and mammary gland cells.

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Ligands:   17β-Estradiol

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