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BOR - Papers in Press, published online ahead of print June 25, 2003.
Biol Reprod 2003, 10.1095/biolreprod.103.017830
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BIOLOGY OF REPRODUCTION 69, 1545–1551 (2003)
DOI: 10.1095/biolreprod.103.017830
© 2003 by the Society for the Study of Reproduction, Inc.


Female Reproductive Tract

Differences in Glycosylation and Sperm-Egg Binding Inhibition of Pregnancy-Related Glycodelin1

Hannu Koistinen3, Richard L. Easton5, Philip C.N. Chiu6, Sara Chalabi5, Mervi Halttunen3, Anne Dell5, Howard R. Morris5, William S.B. Yeung6, Markku Seppälä4, and Riitta Koistinen2,3

Department of Obstetrics and Gynecology3 Department of Clinical Chemistry,4 Helsinki University Central Hospital, 00029 HUS, Finland Department of Biological Sciences,5 Imperial College, London SW7 2AZ, United Kingdom Department of Obstetrics and Gynecology,6 University of Hong Kong, Queen Mary Hospital, Hong Kong, China

Glycodelin is a glycoprotein produced in many glands, particularly those of reproductive tissues. It appears as different glycoforms in amniotic fluid (glycodelin-A) and seminal plasma (glycodelin-S), but only glycodelin-A inhibits gamete adhesion. In the present study, glycodelin from secretory-phase endometrium, first-trimester pregnancy decidua, and midtrimester amniotic fluid was studied with respect to physicochemical properties, including glycosylation patterns and inhibitory activity of sperm-egg binding. Purified glycodelins from all these sources were similar in isoelectric focusing and in lectin immunoassays using lectins from Wisteria floribunda and Sambucus nigra. Likewise, the glycodelins inhibited sperm-egg binding in a dose-dependent manner, as measured by hemizona-binding assay. However, subtle quantitative physicochemical and biological differences were found between glycodelins from different sources as well as within the same tissue/fluid between different individuals. Differences were most pronounced between endometrial glycodelins from nonpregnancy and first-trimester pregnancy. The glycan structures studied by fast-atom bombardment mass spectrometry of individual amniotic fluid glycodelin-A samples also showed interindividual quantitative differences. In conclusion, glycodelins from different female reproductive tract tissues and amniotic fluid share substantial similarity, allowing all of them to be called glycodelin-A. However, these glycodelins exhibit quantitative physicochemical and functional differences between different sources and individuals.

1 Supported by grants from the University of Helsinki, the Academy of Finland, the Helsinki University Hospital Research Funds, Federation of the Finnish Life and Pension Insurance Companies, the Finnish Cancer Foundation, the Biotechnology and Biological Sciences Research Council, the Wellcome Trust, and the Research Grant Council, Hong Kong (HKU 7188/99M, HKU 7261/01M).

2 Correspondence: Riitta Koistinen, Department of Obstetrics and Gynecology, Helsinki University Central Hospital, Biomedicum Helsinki, P.O. Box 700, Haartmaninkatu 8, 00029 HUS, Finland. FAX: 358 9 47171731; riitta.koistinen{at}hus.fi




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