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Article: Effects of glycodelins on functional competence of spermatozoa

TitleEffects of glycodelins on functional competence of spermatozoa
Authors
KeywordsAcrosome reaction
Capacitation
Glycodelin
Spermatozoa
Zona pellucida binding
Issue Date2009
PublisherElsevier Ireland Ltd. The Journal's web site is located at http://www.elsevier.com/locate/jri
Citation
Journal Of Reproductive Immunology, 2009, v. 83 n. 1-2, p. 26-30 How to Cite?
AbstractGlycodelin is a glycoprotein with 4 known glycoforms, namely glycodelin-S, glycodelin-A, glycodelin-F and glycodelin-C. The glycoforms are present in the female reproductive tract which the spermatozoa must pass through before fertilizing the oocyte. Thus the spermatozoa interact with each of these glycoforms in succession. The glycoforms have different effects on sperm function. Glycodelin-S in the seminal plasma suppresses albumin-induced cholesterol efflux from the spermatozoa and thereby regulates the initiation of capacitation. Glycodelin-A in the oviductal fluid suppresses extracellular signal-regulated kinase making the spermatozoa more sensitive to zona pellucida-induced acrosome reaction. Follicular fluid glycodelin-F suppresses progesterone-induced acrosome reaction and prevents premature acrosome reaction. Glycodelin-A and glycodelin-F also inhibit spermatozoa-zona pellucida binding by interacting with sperm surface fucosyltransferase-5, which also binds to zona pellucida glycoproteins. The physiological implication of this phenomenon remains to be determined. The inhibitory activities of glycodelin-A and glycodelin-F on spermatozoa-zona pellucida binding is removed by glycodelin-C in the cumulus matrix. Glycodelin-C not only displaces sperm-bound glycodelin-A and glycodelin-F, it also enhances spermatozoa-zona pellucida binding. These different biological activities of the glycodelin isoforms are determined by glycosylation of the proteins. Deglycosylation abolishes the binding and therefore the action of the glycodelins on spermatozoa. Knowledge of the mechanism of actions of glycodelins may enable development of novel strategies for fertility regulation. © 2009 Elsevier Ireland Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/142247
ISSN
2015 Impact Factor: 3.202
2015 SCImago Journal Rankings: 1.233
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYeung, WSBen_HK
dc.contributor.authorLee, KFen_HK
dc.contributor.authorKoistinen, Ren_HK
dc.contributor.authorKoistinen, Hen_HK
dc.contributor.authorSeppälä, Men_HK
dc.contributor.authorChiu, PCNen_HK
dc.date.accessioned2011-10-21T07:54:40Z-
dc.date.available2011-10-21T07:54:40Z-
dc.date.issued2009en_HK
dc.identifier.citationJournal Of Reproductive Immunology, 2009, v. 83 n. 1-2, p. 26-30en_HK
dc.identifier.issn0165-0378en_HK
dc.identifier.urihttp://hdl.handle.net/10722/142247-
dc.description.abstractGlycodelin is a glycoprotein with 4 known glycoforms, namely glycodelin-S, glycodelin-A, glycodelin-F and glycodelin-C. The glycoforms are present in the female reproductive tract which the spermatozoa must pass through before fertilizing the oocyte. Thus the spermatozoa interact with each of these glycoforms in succession. The glycoforms have different effects on sperm function. Glycodelin-S in the seminal plasma suppresses albumin-induced cholesterol efflux from the spermatozoa and thereby regulates the initiation of capacitation. Glycodelin-A in the oviductal fluid suppresses extracellular signal-regulated kinase making the spermatozoa more sensitive to zona pellucida-induced acrosome reaction. Follicular fluid glycodelin-F suppresses progesterone-induced acrosome reaction and prevents premature acrosome reaction. Glycodelin-A and glycodelin-F also inhibit spermatozoa-zona pellucida binding by interacting with sperm surface fucosyltransferase-5, which also binds to zona pellucida glycoproteins. The physiological implication of this phenomenon remains to be determined. The inhibitory activities of glycodelin-A and glycodelin-F on spermatozoa-zona pellucida binding is removed by glycodelin-C in the cumulus matrix. Glycodelin-C not only displaces sperm-bound glycodelin-A and glycodelin-F, it also enhances spermatozoa-zona pellucida binding. These different biological activities of the glycodelin isoforms are determined by glycosylation of the proteins. Deglycosylation abolishes the binding and therefore the action of the glycodelins on spermatozoa. Knowledge of the mechanism of actions of glycodelins may enable development of novel strategies for fertility regulation. © 2009 Elsevier Ireland Ltd. All rights reserved.en_HK
dc.languageeng-
dc.publisherElsevier Ireland Ltd. The Journal's web site is located at http://www.elsevier.com/locate/jrien_HK
dc.relation.ispartofJournal of Reproductive Immunologyen_HK
dc.subjectAcrosome reactionen_HK
dc.subjectCapacitationen_HK
dc.subjectGlycodelinen_HK
dc.subjectSpermatozoaen_HK
dc.subjectZona pellucida bindingen_HK
dc.subject.meshAcrosome Reaction-
dc.subject.meshEndometrium - metabolism-
dc.subject.meshFallopian Tubes - metabolism-
dc.subject.meshGlycoproteins - physiology-
dc.subject.meshPregnancy Proteins - physiology-
dc.titleEffects of glycodelins on functional competence of spermatozoaen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0165-0378&volume=83&issue=1-2&spage=26&epage=30&date=2009&atitle=Effects+of+glycodelins+on+functional+competence+of+spermatozoa-
dc.identifier.emailYeung, WSB:wsbyeung@hkucc.hku.hken_HK
dc.identifier.emailLee, KF:ckflee@hku.hken_HK
dc.identifier.emailChiu, PCN:pchiucn@hku.hken_HK
dc.identifier.authorityYeung, WSB=rp00331en_HK
dc.identifier.authorityLee, KF=rp00458en_HK
dc.identifier.authorityChiu, PCN=rp00424en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.jri.2009.04.012en_HK
dc.identifier.pmid19857900-
dc.identifier.scopuseid_2-s2.0-70449708925en_HK
dc.identifier.hkuros173273-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-70449708925&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume83en_HK
dc.identifier.issue1-2en_HK
dc.identifier.spage26en_HK
dc.identifier.epage30en_HK
dc.identifier.isiWOS:000273024800006-
dc.publisher.placeIrelanden_HK
dc.identifier.scopusauthoridYeung, WSB=7102370745en_HK
dc.identifier.scopusauthoridLee, KF=26643097500en_HK
dc.identifier.scopusauthoridKoistinen, R=7006574669en_HK
dc.identifier.scopusauthoridKoistinen, H=7003612125en_HK
dc.identifier.scopusauthoridSeppälä, M=35475165300en_HK
dc.identifier.scopusauthoridChiu, PCN=25959969200en_HK
dc.identifier.citeulike6051500-

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