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Article: Differences in Glycosylation and Sperm-Egg Binding Inhibition of Pregnancy-Related Glycodelin

TitleDifferences in Glycosylation and Sperm-Egg Binding Inhibition of Pregnancy-Related Glycodelin
Authors
KeywordsDecidua
Ovum
Pregnancy
Sperm
Issue Date2003
PublisherSociety for the Study of Reproduction. The Journal's web site is located at http://www.biolreprod.org/
Citation
Biology Of Reproduction, 2003, v. 69 n. 5, p. 1545-1551 How to Cite?
AbstractGlycodelin 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.
Persistent Identifierhttp://hdl.handle.net/10722/87399
ISSN
2015 Impact Factor: 3.471
2015 SCImago Journal Rankings: 1.646
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorKoistinen, Hen_HK
dc.contributor.authorEaston, RLen_HK
dc.contributor.authorChiu, PCNen_HK
dc.contributor.authorChalabi, Sen_HK
dc.contributor.authorHalttunen, Men_HK
dc.contributor.authorDell, Aen_HK
dc.contributor.authorMorris, HRen_HK
dc.contributor.authorYeung, WSBen_HK
dc.contributor.authorSeppälä, Men_HK
dc.contributor.authorKoistinen, Ren_HK
dc.date.accessioned2010-09-06T09:29:10Z-
dc.date.available2010-09-06T09:29:10Z-
dc.date.issued2003en_HK
dc.identifier.citationBiology Of Reproduction, 2003, v. 69 n. 5, p. 1545-1551en_HK
dc.identifier.issn0006-3363en_HK
dc.identifier.urihttp://hdl.handle.net/10722/87399-
dc.description.abstractGlycodelin 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.en_HK
dc.languageengen_HK
dc.publisherSociety for the Study of Reproduction. The Journal's web site is located at http://www.biolreprod.org/en_HK
dc.relation.ispartofBiology of Reproductionen_HK
dc.subjectDeciduaen_HK
dc.subjectOvumen_HK
dc.subjectPregnancyen_HK
dc.subjectSpermen_HK
dc.titleDifferences in Glycosylation and Sperm-Egg Binding Inhibition of Pregnancy-Related Glycodelinen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0006-3363&volume=69&spage=1545&epage=1551&date=2003&atitle=Differences+in+glycosylation+and+sperm-egg+binding+inhibition+of+pregnancy-related+glycodelinen_HK
dc.identifier.emailChiu, PCN:pchiucn@hku.hken_HK
dc.identifier.emailYeung, WSB:wsbyeung@hkucc.hku.hken_HK
dc.identifier.authorityChiu, PCN=rp00424en_HK
dc.identifier.authorityYeung, WSB=rp00331en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1095/biolreprod.103.017830en_HK
dc.identifier.pmid12826581-
dc.identifier.scopuseid_2-s2.0-0242361762en_HK
dc.identifier.hkuros87757en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0242361762&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume69en_HK
dc.identifier.issue5en_HK
dc.identifier.spage1545en_HK
dc.identifier.epage1551en_HK
dc.identifier.isiWOS:000186147700013-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridKoistinen, H=7003612125en_HK
dc.identifier.scopusauthoridEaston, RL=7004476498en_HK
dc.identifier.scopusauthoridChiu, PCN=25959969200en_HK
dc.identifier.scopusauthoridChalabi, S=6507840158en_HK
dc.identifier.scopusauthoridHalttunen, M=6701710914en_HK
dc.identifier.scopusauthoridDell, A=7103412653en_HK
dc.identifier.scopusauthoridMorris, HR=7401534652en_HK
dc.identifier.scopusauthoridYeung, WSB=7102370745en_HK
dc.identifier.scopusauthoridSeppälä, M=35475165300en_HK
dc.identifier.scopusauthoridKoistinen, R=7006574669en_HK

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