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Article: Glycosylation related actions of glycodelin: Gamete, cumulus cell, immune cell and clinical associations

TitleGlycosylation related actions of glycodelin: Gamete, cumulus cell, immune cell and clinical associations
Authors
KeywordsCumulus cells
Fertilization
Immunosuppression
Issue Date2007
PublisherOxford University Press. The Journal's web site is located at http://humupd.oxfordjournals.org
Citation
Human Reproduction Update, 2007, v. 13 n. 3, p. 275-287 How to Cite?
AbstractGlycodelin is an example of a glycoprotein whose complex-type glycans mediate biological actions in human reproduction and immune reactions. Being attached to an identical protein backbone, glycodelin oligosaccharides vary significantly from one reproductive tissue to another and have an effect on its own secretion and role in cell communication. For instance, uterine glycodelin-A inhibits sperm-oocyte interaction by binding on the sperm head. This is a glycosylation-dependent phenomenon, in which fucosyltransferase-5 plays a key role. Glycodelin-S from seminal plasma binds evenly around the sperm head and maintains an uncapacitated state in the spermatozoa, until the isoform is detached during sperm passage through the cervix. Glycodelin-F from follicular fluid and Fallopian tube binds to the acrosomal region of the sperm head, thereby inhibiting both the sperm-oocyte binding and premature progesterone-induced acrosome reaction. The cumulus cells surrounding the oocyte can capture glycodelin-A and -F from the surrounding environment and convert these isoforms to a cumulus cell isoform, glycodelin-C. It differs by glycosylation from the other isoforms, and it too attaches on the sperm head, with the highest density in the equatorial region. Glycodelin-C is capable of detaching the sperm-bound inhibitory isoforms so that the sperm-oocyte binding is enhanced. Glycodelin-A also has immunosuppressive actions directed to cellular, humoral and innate immunity. Although these actions depend mainly on the protein backbone, glycosylation also plays a part. Glycosylated glycodelin may be involved in the protection of spermatozoa against maternal immune reactions, and glycodelin also has apoptogenic activity. Some glycosylation patterns of glycodelin may mask its apoptogenic domain. This review updates the recent research and clinical associations of glycodelin, highlighting the role of glycosylation. © The Author 2007. Published by Oxford University Press.
Persistent Identifierhttp://hdl.handle.net/10722/87360
ISSN
2015 Impact Factor: 11.194
2015 SCImago Journal Rankings: 4.678
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSeppälä, Men_HK
dc.contributor.authorKoistinen, Hen_HK
dc.contributor.authorKoistinen, Ren_HK
dc.contributor.authorChiu, PCNen_HK
dc.contributor.authorYeung, WSBen_HK
dc.date.accessioned2010-09-06T09:28:39Z-
dc.date.available2010-09-06T09:28:39Z-
dc.date.issued2007en_HK
dc.identifier.citationHuman Reproduction Update, 2007, v. 13 n. 3, p. 275-287en_HK
dc.identifier.issn1355-4786en_HK
dc.identifier.urihttp://hdl.handle.net/10722/87360-
dc.description.abstractGlycodelin is an example of a glycoprotein whose complex-type glycans mediate biological actions in human reproduction and immune reactions. Being attached to an identical protein backbone, glycodelin oligosaccharides vary significantly from one reproductive tissue to another and have an effect on its own secretion and role in cell communication. For instance, uterine glycodelin-A inhibits sperm-oocyte interaction by binding on the sperm head. This is a glycosylation-dependent phenomenon, in which fucosyltransferase-5 plays a key role. Glycodelin-S from seminal plasma binds evenly around the sperm head and maintains an uncapacitated state in the spermatozoa, until the isoform is detached during sperm passage through the cervix. Glycodelin-F from follicular fluid and Fallopian tube binds to the acrosomal region of the sperm head, thereby inhibiting both the sperm-oocyte binding and premature progesterone-induced acrosome reaction. The cumulus cells surrounding the oocyte can capture glycodelin-A and -F from the surrounding environment and convert these isoforms to a cumulus cell isoform, glycodelin-C. It differs by glycosylation from the other isoforms, and it too attaches on the sperm head, with the highest density in the equatorial region. Glycodelin-C is capable of detaching the sperm-bound inhibitory isoforms so that the sperm-oocyte binding is enhanced. Glycodelin-A also has immunosuppressive actions directed to cellular, humoral and innate immunity. Although these actions depend mainly on the protein backbone, glycosylation also plays a part. Glycosylated glycodelin may be involved in the protection of spermatozoa against maternal immune reactions, and glycodelin also has apoptogenic activity. Some glycosylation patterns of glycodelin may mask its apoptogenic domain. This review updates the recent research and clinical associations of glycodelin, highlighting the role of glycosylation. © The Author 2007. Published by Oxford University Press.en_HK
dc.languageengen_HK
dc.publisherOxford University Press. The Journal's web site is located at http://humupd.oxfordjournals.orgen_HK
dc.relation.ispartofHuman Reproduction Updateen_HK
dc.rightsHuman Reproduction Update. Copyright © Oxford University Press.en_HK
dc.subjectCumulus cellsen_HK
dc.subjectFertilizationen_HK
dc.subjectImmunosuppressionen_HK
dc.titleGlycosylation related actions of glycodelin: Gamete, cumulus cell, immune cell and clinical associationsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1355-4786&volume=13&spage=275&epage=287&date=2007&atitle=Glycosylation+related+actions+of+glycodelin:+gamete,+cumulus+cell,+immune+cell+and+clinical+associationsen_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.doi10.1093/humupd/dmm004en_HK
dc.identifier.pmid17329396-
dc.identifier.scopuseid_2-s2.0-34347233136en_HK
dc.identifier.hkuros126360en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34347233136&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume13en_HK
dc.identifier.issue3en_HK
dc.identifier.spage275en_HK
dc.identifier.epage287en_HK
dc.identifier.isiWOS:000246122700006-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridSeppälä, M=35475165300en_HK
dc.identifier.scopusauthoridKoistinen, H=7003612125en_HK
dc.identifier.scopusauthoridKoistinen, R=7006574669en_HK
dc.identifier.scopusauthoridChiu, PCN=25959969200en_HK
dc.identifier.scopusauthoridYeung, WSB=7102370745en_HK
dc.identifier.citeulike1252161-

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