File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Glycosylation profile of differently charged IgA1 and their binding characteristics to cultured mesangial cells in IgA nephropathy

TitleGlycosylation profile of differently charged IgA1 and their binding characteristics to cultured mesangial cells in IgA nephropathy
Authors
KeywordsIgA nephropathy
IgA1
Mesangial cell
Polymeric IgA
Issue Date2007
PublisherS Karger AG. The Journal's web site is located at http://www.karger.com/NEE
Citation
Nephron - Experimental Nephrology, 2007, v. 107 n. 3, p. e107-e118 How to Cite?
AbstractBackground: IgA nephropathy (IgAN) is characterized by mesangial deposition of polymeric IgA1 (pIgA1), yet the pathogeneic mechanism remains unresolved. In the present study, we examined the glycosylation profile of differently charged IgA1 from IgAN patients. The binding characteristics of these IgA1 fractions to cultured human mesangial cells (HMC) and hepatoma cell lines (HepG2) were studied. Methods: Differently charged IgA1 were isolated by ion exchange chromatography. The glycosylation profile in the carbohydrate moieties of these differently charged IgA1 was analyzed by galactose (Gal)-, galactose- acetylgalactosamine (Gal-GalNAc)-, or sialic acid-specific enzyme-linked lectin binding assays (ELLA). The binding characteristic of these IgA1 to HMC was examined by flow cytometry and competitive binding assay. Results: Anionic pIgA from IgAN patients showed less reactivity in (Gal)- and (Gal-GalNAc)-specific ELLA (p < 0.01). There was higher reactivity for anionic pIgA1 in α(2,6)-linked sialic acid-specific ELLA (p < 0.01). Anionic pIgA1 from IgAN patients exhibited increased binding to cultured HMC and the binding was significantly reduced after neuraminidase treatment (p < 0.05). In contrast, anionic pIgA1 from IgAN patients bound less to cultured HepG2 cells and the binding was enhanced following neuraminidase treatment (p < 0.05). Conclusions: We demonstrated an unusual glycosylation and sialylation pattern of anionic pIgA1 in IgAN which may have an important effect on its pathogenesis. Copyright © 2007 S. Karger AG.
Persistent Identifierhttp://hdl.handle.net/10722/77395
ISSN
2015 Impact Factor: 1.531
2015 SCImago Journal Rankings: 1.030
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLeung, JCKen_HK
dc.contributor.authorChan, LYYen_HK
dc.contributor.authorTang, SCWen_HK
dc.contributor.authorTam, PCen_HK
dc.contributor.authorFenn, Jen_HK
dc.contributor.authorLai, KNen_HK
dc.date.accessioned2010-09-06T07:31:26Z-
dc.date.available2010-09-06T07:31:26Z-
dc.date.issued2007en_HK
dc.identifier.citationNephron - Experimental Nephrology, 2007, v. 107 n. 3, p. e107-e118en_HK
dc.identifier.issn1660-2129en_HK
dc.identifier.urihttp://hdl.handle.net/10722/77395-
dc.description.abstractBackground: IgA nephropathy (IgAN) is characterized by mesangial deposition of polymeric IgA1 (pIgA1), yet the pathogeneic mechanism remains unresolved. In the present study, we examined the glycosylation profile of differently charged IgA1 from IgAN patients. The binding characteristics of these IgA1 fractions to cultured human mesangial cells (HMC) and hepatoma cell lines (HepG2) were studied. Methods: Differently charged IgA1 were isolated by ion exchange chromatography. The glycosylation profile in the carbohydrate moieties of these differently charged IgA1 was analyzed by galactose (Gal)-, galactose- acetylgalactosamine (Gal-GalNAc)-, or sialic acid-specific enzyme-linked lectin binding assays (ELLA). The binding characteristic of these IgA1 to HMC was examined by flow cytometry and competitive binding assay. Results: Anionic pIgA from IgAN patients showed less reactivity in (Gal)- and (Gal-GalNAc)-specific ELLA (p < 0.01). There was higher reactivity for anionic pIgA1 in α(2,6)-linked sialic acid-specific ELLA (p < 0.01). Anionic pIgA1 from IgAN patients exhibited increased binding to cultured HMC and the binding was significantly reduced after neuraminidase treatment (p < 0.05). In contrast, anionic pIgA1 from IgAN patients bound less to cultured HepG2 cells and the binding was enhanced following neuraminidase treatment (p < 0.05). Conclusions: We demonstrated an unusual glycosylation and sialylation pattern of anionic pIgA1 in IgAN which may have an important effect on its pathogenesis. Copyright © 2007 S. Karger AG.en_HK
dc.languageengen_HK
dc.publisherS Karger AG. The Journal's web site is located at http://www.karger.com/NEEen_HK
dc.relation.ispartofNephron - Experimental Nephrologyen_HK
dc.rightsNephron Experimental Nephrology . Copyright © S Karger AG.en_HK
dc.subjectIgA nephropathyen_HK
dc.subjectIgA1en_HK
dc.subjectMesangial cellen_HK
dc.subjectPolymeric IgAen_HK
dc.subject.meshAcetylgalactosamine - analysisen_HK
dc.subject.meshAdulten_HK
dc.subject.meshAnionsen_HK
dc.subject.meshBinding, Competitiveen_HK
dc.subject.meshCationsen_HK
dc.subject.meshCell Line, Tumor - metabolismen_HK
dc.subject.meshCells, Cultured - metabolism - pathologyen_HK
dc.subject.meshFemaleen_HK
dc.subject.meshGalactose - analysisen_HK
dc.subject.meshGlomerulonephritis, IGA - metabolismen_HK
dc.subject.meshGlycosylation - drug effectsen_HK
dc.subject.meshHumansen_HK
dc.subject.meshImmunoglobulin A - chemistry - metabolismen_HK
dc.subject.meshMaleen_HK
dc.subject.meshMesangial Cells - metabolism - pathologyen_HK
dc.subject.meshMiddle Ageden_HK
dc.subject.meshN-Acetylneuraminic Acid - analysisen_HK
dc.subject.meshNeuraminidase - pharmacologyen_HK
dc.subject.meshProtein Bindingen_HK
dc.subject.meshProtein Processing, Post-Translational - drug effectsen_HK
dc.titleGlycosylation profile of differently charged IgA1 and their binding characteristics to cultured mesangial cells in IgA nephropathyen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1660-2129&volume=107&spage=107&epage=118&date=2007&atitle=Glycosylation+profile+of+differently+charged+IgA1+and+their+binding+characteristics+to+cultured+mesangial+cells+in+IgA+nephropathyen_HK
dc.identifier.emailLeung, JCK: jckleung@hku.hken_HK
dc.identifier.emailTang, SCW: scwtang@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.authorityLai, KN=rp00324en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1159/000109980en_HK
dc.identifier.pmid17957128-
dc.identifier.scopuseid_2-s2.0-35948950673en_HK
dc.identifier.hkuros138346en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-35948950673&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume107en_HK
dc.identifier.issue3en_HK
dc.identifier.spagee107en_HK
dc.identifier.epagee118en_HK
dc.identifier.isiWOS:000251439300003-
dc.publisher.placeSwitzerlanden_HK
dc.identifier.scopusauthoridLeung, JCK=7202180349en_HK
dc.identifier.scopusauthoridChan, LYY=55182644100en_HK
dc.identifier.scopusauthoridTang, SCW=7403437082en_HK
dc.identifier.scopusauthoridTam, PC=7202539419en_HK
dc.identifier.scopusauthoridFenn, J=17534025300en_HK
dc.identifier.scopusauthoridLai, KN=7402135706en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats