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J. Biol. Chem., Vol. 280, Issue 27, 25580-25589, July 8, 2005

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Glycodelin-S in Human Seminal Plasma Reduces Cholesterol Efflux and Inhibits Capacitation of Spermatozoa^*

Philip C. N. Chiu, Man-Kin Chung, Heng-Yan Tsang, Riitta Koistinen¶, Hannu Koistinen¶, Markku Seppala¶, Kai-Fai Lee, and William S.B. Yeung||

From the Department of Obstetrics and Gynaecology, University of Hong Kong, Queen Mary Hospital, Pokfulam Road, Hong Kong, China and the Departments of Obstetrics and Gynaecology and ^¶Clinical Chemistry, University Central Hospital, 00029 HUS Helsinki, Finland

Tight control of sperm capacitation is important for successful fertilization. Glycodelin-S is one of the most abundant glycoproteins in the human seminal plasma. However, its function is unclear. We investigated the role of glycodelin-S on capacitation of human spermatozoa. Binding kinetics experiments demonstrated the presence of two saturable and reversible binding sites of glycodelin-S on human spermatozoa. Differently glycosylated other isoforms of glycodelin, glycodelin-A and -F, did not compete with glycodelin-S for these binding sites, suggesting that the glycodelin-S binding sites are different from those of the other isoforms. Indirect immunofluorescent staining revealed specific binding of glycodelin-S around the sperm head. This immunoreactivity was greatly reduced in spermatozoa that had migrated through the cervical mucus surrogates. Glycodelin-S at physiological concentrations significantly reduced the bovine serum albumin and cyclodextrin-induced cholesterol efflux and down-regulated the adenylyl cyclase/protein kinase A/tyrosine kinase signaling pathway, resulting in suppression of capacitation. Deglycosylation abolished glycodelin-S binding and the effect of glycodelin-S on bovine serum albumin-induced capacitation. This indicates that the carbohydrate moiety of glycodelin-S is critical for the function of the molecule. It is concluded that glycodelin-S in seminal plasma maintains the uncapacitated state of human spermatozoa.

Received for publication, April 15, 2005 , and in revised form, May 9, 2005.

^* This work was supported by the Research Grant Council, Hong Kong (Grants HKU7261/01M and HKU7614/05M), Committee on Research and Conference Grants, University of Hong Kong, Helsinki University Central Hospital Research Funds, Federation of the Finnish Life and Pension Insurance Companies, the Cancer Society of Finland, the Academy of Finland, and the University of Helsinki.The costs of publication of this article were defrayed in part by the payment of page charges. This 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.: 852-285-53405; Fax: 852-281-75374; E-mail: wsbyeung{at}hkucc.hku.hk.

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