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Article: Effects of differential glycosylation of glycodelins on lymphocyte survival
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TitleEffects of differential glycosylation of glycodelins on lymphocyte survival
 
AuthorsLee, CL1 1
Pang, PC3
Yeung, WSB1
Tissot, B3
Panico, M3
Lao, TTH4
Chu, IK1
Lee, KF1
Chung, MK1
Lam, KKW1
Koistinen, R5 5
Koistinen, H5
Seppälä, M5
Morris, HR3 2
Dell, A3
Chiu, PCN1
 
Issue Date2009
 
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
 
CitationJournal Of Biological Chemistry, 2009, v. 284 n. 22, p. 15084-15096 [How to Cite?]
DOI: http://dx.doi.org/10.1074/jbc.M807960200
 
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.
 
ISSN0021-9258
2012 Impact Factor: 4.651
2012 SCImago Journal Rankings: 2.723
 
DOIhttp://dx.doi.org/10.1074/jbc.M807960200
 
PubMed Central IDPMC2685690
 
ISI Accession Number IDWOS:000266288200044
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.).

 
ReferencesReferences in Scopus
 
GrantsStructural Characterization and Quantification of Diabetes-Associated Glycosylation Changes in Glycodelins Using Mass Spectrometry
 
DC FieldValue
dc.contributor.authorLee, CL
 
dc.contributor.authorPang, PC
 
dc.contributor.authorYeung, WSB
 
dc.contributor.authorTissot, B
 
dc.contributor.authorPanico, M
 
dc.contributor.authorLao, TTH
 
dc.contributor.authorChu, IK
 
dc.contributor.authorLee, KF
 
dc.contributor.authorChung, MK
 
dc.contributor.authorLam, KKW
 
dc.contributor.authorKoistinen, R
 
dc.contributor.authorKoistinen, H
 
dc.contributor.authorSeppälä, M
 
dc.contributor.authorMorris, HR
 
dc.contributor.authorDell, A
 
dc.contributor.authorChiu, PCN
 
dc.date.accessioned2010-05-31T03:28:06Z
 
dc.date.available2010-05-31T03:28:06Z
 
dc.date.issued2009
 
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.
 
dc.description.naturelink_to_OA_fulltext
 
dc.identifier.citationJournal Of Biological Chemistry, 2009, v. 284 n. 22, p. 15084-15096 [How to Cite?]
DOI: http://dx.doi.org/10.1074/jbc.M807960200
 
dc.identifier.doihttp://dx.doi.org/10.1074/jbc.M807960200
 
dc.identifier.eissn1083-351X
 
dc.identifier.epage15096
 
dc.identifier.hkuros171466
 
dc.identifier.isiWOS:000266288200044
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.).

 
dc.identifier.issn0021-9258
2012 Impact Factor: 4.651
2012 SCImago Journal Rankings: 2.723
 
dc.identifier.issue22
 
dc.identifier.openurl
 
dc.identifier.pmcidPMC2685690
 
dc.identifier.pmid19240032
 
dc.identifier.scopuseid_2-s2.0-67649386171
 
dc.identifier.spage15084
 
dc.identifier.urihttp://hdl.handle.net/10722/58312
 
dc.identifier.volume284
 
dc.languageeng
 
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
 
dc.publisher.placeUnited States
 
dc.relation.ispartofJournal of Biological Chemistry
 
dc.relation.projectStructural Characterization and Quantification of Diabetes-Associated Glycosylation Changes in Glycodelins Using Mass Spectrometry
 
dc.relation.referencesReferences in Scopus
 
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 survival
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong
  2. M-SCAN Ltd.
  3. Imperial College London
  4. Chinese University of Hong Kong
  5. Helsinki University Central Hospital