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Article: Increased sialylation of polymeric γ-IgA1 in patients with IgA nephropathy

TitleIncreased sialylation of polymeric γ-IgA1 in patients with IgA nephropathy
Authors
Keywordsγ-IgA
Glycosylation
IgA nephropathy
IgA1
Polymeric IgA
Sialylation
Issue Date2002
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/36921
Citation
Journal Of Clinical Laboratory Analysis, 2002, v. 16 n. 1, p. 11-19 How to Cite?
AbstractThe mechanism of mesangial IgA deposition is poorly understood in IgA nephropathy (IgAN). Abnormal glycosylation of carbohydrate moieties in the hinge region of the IgA molecule has recently attracted much attention. In this report, we studied galactosylation and sialylation profiles in κ- and γ-IgA1 from patients with IgAN. Total serum IgA1 was isolated from patients with IgAN lgAN or healthy controls by jacalin-affinity chromatography. Six fractions of molecular weight (MW) 50-1,000 kDa were separated by fast protein liquid chromatography (FPLC). Four lectin-binding assays were used to study the sialylation and the presence of terminal galactose or N-acetylgalactosamine (GaINAc) in the O-linked carbohydrate moieties of κ- or γ-IgA1. Maackia amurensis agglutinin (MAA) and Sambucus nigra agglutinin (SNA) lectin recognize α(2,3)- and α(2,6)-linked sialic acid, respectively. Peanut agglutinin (PNA) and Helix aspersa (HA) lectin recognize terminal galactose and GaINAc, respectively. Reduced HA was demonstrated in macromolecular κ or γ-IgA1 (300-825 kDa) isolated from patients with IgAN (P < 0.05 compared with healthy controls). Lambda- but not κ-IgA1 from patients with IgAN bound less to PNA (P < 0.05). The α(2,3)-linked sialic acid content in γ- but not κ-IgA1 of MW 150-610 kDa from patients was higher than that of controls (P < 0.005). The α(2,6)-linked sialic acid content in γ-IgA1 (300-825 kDa) and κ-IgA1 (150-610 kDa) from patients was also higher than that of controls. This unusual glycosylation and sialylation pattern of the γ-IgA1 may have important implications for the pathogenesis of IgAN, as both the masking effect of sialic acid on galactose and the reduced galactosylation will hinder the clearance of macromorecular γ-IgA1 by asialoglycoprotein receptor of hepatocytes. The negative charge from sialic acid may also favor mesangial deposition of macromolecular γ-IgA1 in IgAN. © 2002 Wiley-Liss, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/162580
ISSN
2015 Impact Factor: 1.549
2015 SCImago Journal Rankings: 0.524
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLeung, JCKen_HK
dc.contributor.authorTang, SCWen_HK
dc.contributor.authorChan, DTMen_HK
dc.contributor.authorLui, SLen_HK
dc.contributor.authorLai, KNen_HK
dc.date.accessioned2012-09-05T05:21:22Z-
dc.date.available2012-09-05T05:21:22Z-
dc.date.issued2002en_HK
dc.identifier.citationJournal Of Clinical Laboratory Analysis, 2002, v. 16 n. 1, p. 11-19en_HK
dc.identifier.issn0887-8013en_HK
dc.identifier.urihttp://hdl.handle.net/10722/162580-
dc.description.abstractThe mechanism of mesangial IgA deposition is poorly understood in IgA nephropathy (IgAN). Abnormal glycosylation of carbohydrate moieties in the hinge region of the IgA molecule has recently attracted much attention. In this report, we studied galactosylation and sialylation profiles in κ- and γ-IgA1 from patients with IgAN. Total serum IgA1 was isolated from patients with IgAN lgAN or healthy controls by jacalin-affinity chromatography. Six fractions of molecular weight (MW) 50-1,000 kDa were separated by fast protein liquid chromatography (FPLC). Four lectin-binding assays were used to study the sialylation and the presence of terminal galactose or N-acetylgalactosamine (GaINAc) in the O-linked carbohydrate moieties of κ- or γ-IgA1. Maackia amurensis agglutinin (MAA) and Sambucus nigra agglutinin (SNA) lectin recognize α(2,3)- and α(2,6)-linked sialic acid, respectively. Peanut agglutinin (PNA) and Helix aspersa (HA) lectin recognize terminal galactose and GaINAc, respectively. Reduced HA was demonstrated in macromolecular κ or γ-IgA1 (300-825 kDa) isolated from patients with IgAN (P < 0.05 compared with healthy controls). Lambda- but not κ-IgA1 from patients with IgAN bound less to PNA (P < 0.05). The α(2,3)-linked sialic acid content in γ- but not κ-IgA1 of MW 150-610 kDa from patients was higher than that of controls (P < 0.005). The α(2,6)-linked sialic acid content in γ-IgA1 (300-825 kDa) and κ-IgA1 (150-610 kDa) from patients was also higher than that of controls. This unusual glycosylation and sialylation pattern of the γ-IgA1 may have important implications for the pathogenesis of IgAN, as both the masking effect of sialic acid on galactose and the reduced galactosylation will hinder the clearance of macromorecular γ-IgA1 by asialoglycoprotein receptor of hepatocytes. The negative charge from sialic acid may also favor mesangial deposition of macromolecular γ-IgA1 in IgAN. © 2002 Wiley-Liss, Inc.en_HK
dc.languageengen_US
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/36921en_HK
dc.relation.ispartofJournal of Clinical Laboratory Analysisen_HK
dc.subjectγ-IgAen_HK
dc.subjectGlycosylationen_HK
dc.subjectIgA nephropathyen_HK
dc.subjectIgA1en_HK
dc.subjectPolymeric IgAen_HK
dc.subjectSialylationen_HK
dc.subject.meshBinding Sitesen_US
dc.subject.meshCase-Control Studiesen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshFemaleen_US
dc.subject.meshGlomerulonephritis, Iga - Metabolismen_US
dc.subject.meshGlycosylationen_US
dc.subject.meshHumansen_US
dc.subject.meshImmunoglobulin A - Metabolismen_US
dc.subject.meshLectins - Metabolismen_US
dc.subject.meshMaleen_US
dc.titleIncreased sialylation of polymeric γ-IgA1 in patients with IgA nephropathyen_HK
dc.typeArticleen_HK
dc.identifier.emailLeung, JCK: jckleung@hku.hken_HK
dc.identifier.emailTang, SCW: scwtang@hku.hken_HK
dc.identifier.emailChan, DTM: dtmchan@hku.hken_HK
dc.identifier.emailLai, KN: knlai@hku.hken_HK
dc.identifier.authorityLeung, JCK=rp00448en_HK
dc.identifier.authorityTang, SCW=rp00480en_HK
dc.identifier.authorityChan, DTM=rp00394en_HK
dc.identifier.authorityLai, KN=rp00324en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1002/jcla.2035en_HK
dc.identifier.pmid11835525-
dc.identifier.scopuseid_2-s2.0-0036145758en_HK
dc.identifier.hkuros69584-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036145758&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume16en_HK
dc.identifier.issue1en_HK
dc.identifier.spage11en_HK
dc.identifier.epage19en_HK
dc.identifier.isiWOS:000173456600003-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLeung, JCK=7202180349en_HK
dc.identifier.scopusauthoridTang, SCW=7403437082en_HK
dc.identifier.scopusauthoridChan, DTM=7402687700en_HK
dc.identifier.scopusauthoridLui, SL=7102379130en_HK
dc.identifier.scopusauthoridLai, KN=7402135706en_HK

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