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Glycobiology, 2001, Vol. 11, No. 3 183-194
© 2001 Oxford University Press

Anticoagulant heparan sulfate proteoglycans expression in the rat ovary peaks in preovulatory granulosa cells

Marc Princivalle2, Shereen Hasan, Ghamartaj Hosseini and Ariane I. de Agostini1

Infertility Clinic, Department of Gynaecology and Obstetrics, Geneva University Hospital, 1211 Geneva 14, Switzerland and 2Fondation pour Recherches Médicales, 64, avenue de la Roseraie, University of Geneva, 1205 Geneva, Switzerland

Ovarian granulosa cells synthesize anticoagulant heparan sulfate proteoglycans (aHSPGs), which bind and activate antithrombin III. To determine if aHSPGs could contribute to the control of proteolytic activities involved in follicular development and ovulation, we studied the pattern of expression of these proteoglycans during the ovarian cycle. aHSPGs were localized on cells and tissues by 125I-labeled antithrombin III binding followed by microscopic autoradiography. Localization of aHSPGs has shown that cultured granulosa cells, hormonally stimulated by gonadotropins to differentiate in vitro, up-regulate their synthesis and release of aHSPGs. In vivo, during gonadotropin-stimulated cycle, aHSPGs are present on granulosa cells of antral follicles and are strongly labeled in preovulatory follicles. These data demonstrate that aHSPG expression in the ovarian follicle is hormonally induced to culminate in preovulatory follicles. Moreover, we have shown that five heparan sulfate core proteins mRNA (perlecan; syndecan-1, -2, and -4; and glypican-1) are synthesized by granulosa cells, providing attachment for anticoagulant heparan sulfate chains on the cell surface and in the extracellular matrix. These core proteins are constantly expressed during the cycle, indicating that modulations of aHSPG levels observed in the ovary are likely controlled at the level of the biosynthesis of anticoagulant heparan sulfate glycosaminoglycan chains. This expression pattern enables aHSPGs to focus serine protease inhibitors in the developing follicle to control proteolysis and fibrin formation at ovulation.

1 To whom correspondence should be addressed


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