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Article: Effects of differential glycosylation of glycodelins on lymphocyte survival

TitleEffects of differential glycosylation of glycodelins on lymphocyte survival
Authors
Issue Date2009
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2009, v. 284 n. 22, p. 15084-15096 How to Cite?
AbstractGlycodelin is a human glycoprotein with four reported glycoforms, namely glycodelin-A (GdA), glycodelin-F (GdF), glycodelin-C (GdC), and glycodelin-S (GdS). These glycoforms have the same protein core and appear to differ in their N-glycosylation. The glycosylation of GdA is completely different from that of GdS.GdAinhibits proliferation and induces cell death of T cells. However, the glycosylation and immunomodulating activities of GdF and GdC are not known. This study aimed to use ultra-high sensitivity mass spectrometry to compare the glycomes of GdA, GdC, and GdF and to study the relationship between the immunological activity and glycosylation pattern among glycodelin glycoforms. Using MALDI-TOF strategies, the glycoforms were shown to contain an enormous diversity of bi-, tri-, and tetraantennary complex-type glycans carrying Galβ1-4GlcNAc (lacNAc) and/or GalNAcβ1-4GlcNAc (lacdiNAc) antennae backbones with varying levels of fucose and sialic acid substitution. Interestingly, they all carried a family of Sda (NeuAcα2-3(GalNAcβ1-4)Gal)-containing glycans, which were not identified in the earlier study because of less sensitive methodologies used. Among the three glycodelins, GdA is the most heavily sialylated. Virtually all the sialic acid on GdC is located on the Sda antennae. With the exception of the Sda epitope, the GdC N-glycome appears to be the asialylated counterpart of the GdA/GdF glycomes. Sialidase activity, which may be responsible for transforming GdA/GdF to GdC, was detected in cumulus cells. Both GdA and GdF inhibited the proliferation, induced cell death, and suppressed interleukin-2 secretion of Jurkat cells and peripheral blood mono-nuclear cells. In contrast, no immunosuppressive effect was observed for GdS and GdC. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/58312
ISSN
2014 Impact Factor: 4.573
2014 SCImago Journal Rankings: 2.734
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
Research Grants Council (RGC)HKU 764706M
HKU 764007M
Biotechnology and Biological Sciences Research Council (BBSRC)B19088
SF19107
Imperial College London Scholarships
Malaysian Institute of Strategic and International Studies (ISIS) Perdana Scholarship
Funding Information:

This study was supported by Research Grants Council (RGC) Grants HKU 764706M and HKU 764007M, by Grants B19088 and SF19107 from the Biotechnology and Biological Sciences Research Council (BBSRC), including a BBSRC Professorial Fellowship (to A. D.), and by Imperial College London Scholarships and the Malaysian Institute of Strategic and International Studies (ISIS) Perdana Scholarship (to P.-C. P.).

References
Grants

 

DC FieldValueLanguage
dc.contributor.authorLee, CLen_HK
dc.contributor.authorPang, PCen_HK
dc.contributor.authorYeung, WSBen_HK
dc.contributor.authorTissot, Ben_HK
dc.contributor.authorPanico, Men_HK
dc.contributor.authorLao, TTHen_HK
dc.contributor.authorChu, IKen_HK
dc.contributor.authorLee, KFen_HK
dc.contributor.authorChung, MKen_HK
dc.contributor.authorLam, KKWen_HK
dc.contributor.authorKoistinen, Ren_HK
dc.contributor.authorKoistinen, Hen_HK
dc.contributor.authorSeppälä, Men_HK
dc.contributor.authorMorris, HRen_HK
dc.contributor.authorDell, Aen_HK
dc.contributor.authorChiu, PCNen_HK
dc.date.accessioned2010-05-31T03:28:06Z-
dc.date.available2010-05-31T03:28:06Z-
dc.date.issued2009en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2009, v. 284 n. 22, p. 15084-15096en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/58312-
dc.description.abstractGlycodelin is a human glycoprotein with four reported glycoforms, namely glycodelin-A (GdA), glycodelin-F (GdF), glycodelin-C (GdC), and glycodelin-S (GdS). These glycoforms have the same protein core and appear to differ in their N-glycosylation. The glycosylation of GdA is completely different from that of GdS.GdAinhibits proliferation and induces cell death of T cells. However, the glycosylation and immunomodulating activities of GdF and GdC are not known. This study aimed to use ultra-high sensitivity mass spectrometry to compare the glycomes of GdA, GdC, and GdF and to study the relationship between the immunological activity and glycosylation pattern among glycodelin glycoforms. Using MALDI-TOF strategies, the glycoforms were shown to contain an enormous diversity of bi-, tri-, and tetraantennary complex-type glycans carrying Galβ1-4GlcNAc (lacNAc) and/or GalNAcβ1-4GlcNAc (lacdiNAc) antennae backbones with varying levels of fucose and sialic acid substitution. Interestingly, they all carried a family of Sda (NeuAcα2-3(GalNAcβ1-4)Gal)-containing glycans, which were not identified in the earlier study because of less sensitive methodologies used. Among the three glycodelins, GdA is the most heavily sialylated. Virtually all the sialic acid on GdC is located on the Sda antennae. With the exception of the Sda epitope, the GdC N-glycome appears to be the asialylated counterpart of the GdA/GdF glycomes. Sialidase activity, which may be responsible for transforming GdA/GdF to GdC, was detected in cumulus cells. Both GdA and GdF inhibited the proliferation, induced cell death, and suppressed interleukin-2 secretion of Jurkat cells and peripheral blood mono-nuclear cells. In contrast, no immunosuppressive effect was observed for GdS and GdC. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.subject.meshApoptosis-
dc.subject.meshCarbohydrate Conformation-
dc.subject.meshGlycoproteins - isolation and purification - metabolism-
dc.subject.meshLymphocytes - cytology - metabolism - secretion-
dc.subject.meshPregnancy Proteins - isolation and purification - metabolism-
dc.titleEffects of differential glycosylation of glycodelins on lymphocyte survivalen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9258&volume=284&issue=22&spage=15084&epage=15096&date=2009&atitle=Effects+of+differential+glycosylation+of+glycodelins+on+lymphocyte+survivalen_HK
dc.identifier.emailYeung, WSB:wsbyeung@hkucc.hku.hken_HK
dc.identifier.emailChu, IK:ivankchu@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.authorityChu, IK=rp00683en_HK
dc.identifier.authorityLee, KF=rp00458en_HK
dc.identifier.authorityChiu, PCN=rp00424en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1074/jbc.M807960200en_HK
dc.identifier.pmid19240032en_HK
dc.identifier.pmcidPMC2685690-
dc.identifier.scopuseid_2-s2.0-67649386171en_HK
dc.identifier.hkuros171466en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-67649386171&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume284en_HK
dc.identifier.issue22en_HK
dc.identifier.spage15084en_HK
dc.identifier.epage15096en_HK
dc.identifier.eissn1083-351X-
dc.identifier.isiWOS:000266288200044-
dc.publisher.placeUnited Statesen_HK
dc.relation.projectStructural Characterization and Quantification of Diabetes-Associated Glycosylation Changes in Glycodelins Using Mass Spectrometry-
dc.identifier.scopusauthoridLee, CL=9277221100en_HK
dc.identifier.scopusauthoridPang, PC=23028555800en_HK
dc.identifier.scopusauthoridYeung, WSB=7102370745en_HK
dc.identifier.scopusauthoridTissot, B=14621721100en_HK
dc.identifier.scopusauthoridPanico, M=7005321077en_HK
dc.identifier.scopusauthoridLao, TTH=35327208900en_HK
dc.identifier.scopusauthoridChu, IK=7103327484en_HK
dc.identifier.scopusauthoridLee, KF=26643097500en_HK
dc.identifier.scopusauthoridChung, MK=8964203600en_HK
dc.identifier.scopusauthoridLam, KKW=25637362300en_HK
dc.identifier.scopusauthoridKoistinen, R=7006574669en_HK
dc.identifier.scopusauthoridKoistinen, H=7003612125en_HK
dc.identifier.scopusauthoridSeppälä, M=35475165300en_HK
dc.identifier.scopusauthoridMorris, HR=7401534652en_HK
dc.identifier.scopusauthoridDell, A=7103412653en_HK
dc.identifier.scopusauthoridChiu, PCN=25959969200en_HK

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