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- Publisher Website: 10.1093/humupd/dmm004
- Scopus: eid_2-s2.0-34347233136
- PMID: 17329396
- WOS: WOS:000246122700006
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Article: Glycosylation related actions of glycodelin: Gamete, cumulus cell, immune cell and clinical associations
Title | Glycosylation related actions of glycodelin: Gamete, cumulus cell, immune cell and clinical associations |
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Authors | |
Keywords | Cumulus cells Fertilization Immunosuppression |
Issue Date | 2007 |
Publisher | Oxford 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? |
Abstract | Glycodelin 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 Identifier | http://hdl.handle.net/10722/87360 |
ISSN | 2023 Impact Factor: 14.8 2023 SCImago Journal Rankings: 4.074 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Seppälä, M | en_HK |
dc.contributor.author | Koistinen, H | en_HK |
dc.contributor.author | Koistinen, R | en_HK |
dc.contributor.author | Chiu, PCN | en_HK |
dc.contributor.author | Yeung, WSB | en_HK |
dc.date.accessioned | 2010-09-06T09:28:39Z | - |
dc.date.available | 2010-09-06T09:28:39Z | - |
dc.date.issued | 2007 | en_HK |
dc.identifier.citation | Human Reproduction Update, 2007, v. 13 n. 3, p. 275-287 | en_HK |
dc.identifier.issn | 1355-4786 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/87360 | - |
dc.description.abstract | Glycodelin 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.language | eng | en_HK |
dc.publisher | Oxford University Press. The Journal's web site is located at http://humupd.oxfordjournals.org | en_HK |
dc.relation.ispartof | Human Reproduction Update | en_HK |
dc.rights | Human Reproduction Update. Copyright © Oxford University Press. | en_HK |
dc.subject | Cumulus cells | en_HK |
dc.subject | Fertilization | en_HK |
dc.subject | Immunosuppression | en_HK |
dc.title | Glycosylation related actions of glycodelin: Gamete, cumulus cell, immune cell and clinical associations | en_HK |
dc.type | Article | en_HK |
dc.identifier.openurl | http://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+associations | en_HK |
dc.identifier.email | Chiu, PCN:pchiucn@hku.hk | en_HK |
dc.identifier.email | Yeung, WSB:wsbyeung@hkucc.hku.hk | en_HK |
dc.identifier.authority | Chiu, PCN=rp00424 | en_HK |
dc.identifier.authority | Yeung, WSB=rp00331 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1093/humupd/dmm004 | en_HK |
dc.identifier.pmid | 17329396 | - |
dc.identifier.scopus | eid_2-s2.0-34347233136 | en_HK |
dc.identifier.hkuros | 126360 | en_HK |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-34347233136&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 13 | en_HK |
dc.identifier.issue | 3 | en_HK |
dc.identifier.spage | 275 | en_HK |
dc.identifier.epage | 287 | en_HK |
dc.identifier.isi | WOS:000246122700006 | - |
dc.publisher.place | United Kingdom | en_HK |
dc.identifier.scopusauthorid | Seppälä, M=35475165300 | en_HK |
dc.identifier.scopusauthorid | Koistinen, H=7003612125 | en_HK |
dc.identifier.scopusauthorid | Koistinen, R=7006574669 | en_HK |
dc.identifier.scopusauthorid | Chiu, PCN=25959969200 | en_HK |
dc.identifier.scopusauthorid | Yeung, WSB=7102370745 | en_HK |
dc.identifier.citeulike | 1252161 | - |
dc.identifier.issnl | 1355-4786 | - |