QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online 5 December 2006
doi: 10.1242/jcs.03258

This Article Figures Only Full Text Full Text (PDF) All Versions of this Article: jcs.03258v1 120/1/33    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Chiu, P. C. N. Articles by Yeung, W. S. B. Search for Related Content PubMed PubMed Citation Articles by Chiu, P. C. N. Articles by Yeung, W. S. B.

Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding

¹ Department of Obstetrics and Gynaecology, University of Hong Kong, Queen Mary Hospital, Pokfulam Road, Hong Kong, China
² Department of Obstetrics and Gynaecology, University Central Hospital, 00029 HUS Helsinki, Finland
³ Department of Clinical Chemistry, University Central Hospital, 00029 HUS Helsinki, Finland

^* Author for correspondence (wsbyeung{at}hkucc.hku.hk)

Accepted 12 September 2006

Fertilization depends on successful binding of the spermatozoa to the zona pellucida of the oocyte. Glycodelin-A inhibits spermatozoa-zona pellucida binding. Previous data showed that glycodelin-A receptor(s) and zona pellucida protein receptor(s) on human spermatozoa are closely related. Using a chemical cross-linking approach, the glycodelin-A-sperm receptor complex was isolated. The receptor was identified to be fucosyltransferase-5 (FUT5) by mass spectrometry and confirmed with the use of anti-FUT5 antibodies. Sperm FUT5 was an externally oriented integral membrane protein in the acrosomal region of human spermatozoa. Biologically active FUT5 was purified from spermatozoa. Co-immunoprecipitation confirmed the interaction between glycodelin-A and sperm FUT5. Solubilized zona pellucida reduced the binding of glycodelin-A to sperm FUT5. An anti-FUT5 antibody and FUT5 acceptor blocked the binding of glycodelin-A to spermatozoa and the zona binding inhibitory activity of glycodelin-A. Sperm FUT5 bound strongly to intact and solubilized human zona pellucida. The equilibrium dissociation constant of sperm FUT5 binding to solubilized zona pellucida was 42.82 pmol/ml. These observations suggest that human sperm FUT5 is a receptor of glycodelin-A and zona pellucida proteins, and that glycodelin-A inhibits spermatozoa-zona binding by blocking the binding of sperm FUT5 to the zona pellucida.

Key words: Glycodelin, Spermatozoa, Fucosyltransferase, Zona pellucida

This article has been cited by other articles:

				H. Uchida, T. Maruyama, K. Ohta, M. Ono, T. Arase, M. Kagami, H. Oda, T. Kajitani, H. Asada, and Y. Yoshimura Histone deacetylase inhibitor-induced glycodelin enhances the initial step of implantation Hum. Reprod., October 1, 2007; 22(10): 2615 - 2622. [Abstract] [Full Text] [PDF]

				M. Seppala, H. Koistinen, R. Koistinen, P.C.N. Chiu, and W.S.B. Yeung Glycosylation related actions of glycodelin: gamete, cumulus cell, immune cell and clinical associations Hum. Reprod. Update, May 1, 2007; 13(3): 275 - 287. [Abstract] [Full Text] [PDF]