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Article: Increased binding of polymeric A-IgA to cultured human mesangial cells in IgA nephropathy

TitleIncreased binding of polymeric A-IgA to cultured human mesangial cells in IgA nephropathy
Authors
Issue Date1996
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/ki/index.html
Citation
Kidney International, 1996, v. 49 n. 3, p. 839-845 How to Cite?
AbstractIgA nephropathy (IgAN) is characterized by raised plasma λ-IgA1 and mesangial polymeric λ-IgA1 deposits. It remains uncertain whether the predominant glomerular λ-IgA1 deposits represent a selective uptake of polymeric IgA or a non-specific uptake due to elevated circulating λ-IgA1 levels in response to an unidentified antigen. In this study, we explored whether there is an increased binding of monomeric IgA1 (mIgA1) or polymeric IgA1 (pIgA1) from patients with IgAN to cultured human mesangial cells (HMC). Total IgA1 in plasma from patients or healthy controls was isolated by jacalin-agarose column as jacalin-bound proteins (JBP). Monomeric IgA1 and pIgA1 were distinctly separated by FPLC. HMC were incubated with IgA preparations and IgA bound to HMC was determined by flow cytometry analysis using standard curves constructed by known concentrations of κ-IgA1 or λ-IgA1. In order to avoid any increased binding of IgA to HMC due to elevated κ- or λ-IgA concentrations in JBP samples from patients, JBP samples from patients or controls were appropriately diluted to achieve comparable levels of total IgA1. No differences in the total mIgA1 or pIgA1 concentration, percentage of mIgA1 or pIgA1, or the κ/λ ratio of mIgA1 or pIgA1 were found between adjusted JBP samples from patients or healthy controls. We found a sharp rise in percentage of pIgA1 among IgA1 bound to HMC (70%), despite the fact that only 3% of the IgA1 in the adjusted JBP samples were polymeric, suggesting that pIgA1 had a higher affinity to HMC than mIgA1. Furthermore, the κ/λ ratios of pIgA1 bound to HMC were significantly lower than the κ/λ ratios of pIgA1 in adjusted JBP only with IgAN patients but not healthy controls (P = 0.0026). Our data suggest a preferential mesangial binding of polymeric λ-IgA1 from patients with IgAN. These polymeric λ-IgA immune complexes are likely to be "pathogenic" and are important in the pathogenesis of IgAN.
Persistent Identifierhttp://hdl.handle.net/10722/162133
ISSN
2015 Impact Factor: 7.683
2015 SCImago Journal Rankings: 3.181
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLai, KNen_HK
dc.contributor.authorTo, WYen_HK
dc.contributor.authorLi, PKTen_HK
dc.contributor.authorLeung, JCKen_HK
dc.date.accessioned2012-09-05T05:17:32Z-
dc.date.available2012-09-05T05:17:32Z-
dc.date.issued1996en_HK
dc.identifier.citationKidney International, 1996, v. 49 n. 3, p. 839-845en_HK
dc.identifier.issn0085-2538en_HK
dc.identifier.urihttp://hdl.handle.net/10722/162133-
dc.description.abstractIgA nephropathy (IgAN) is characterized by raised plasma λ-IgA1 and mesangial polymeric λ-IgA1 deposits. It remains uncertain whether the predominant glomerular λ-IgA1 deposits represent a selective uptake of polymeric IgA or a non-specific uptake due to elevated circulating λ-IgA1 levels in response to an unidentified antigen. In this study, we explored whether there is an increased binding of monomeric IgA1 (mIgA1) or polymeric IgA1 (pIgA1) from patients with IgAN to cultured human mesangial cells (HMC). Total IgA1 in plasma from patients or healthy controls was isolated by jacalin-agarose column as jacalin-bound proteins (JBP). Monomeric IgA1 and pIgA1 were distinctly separated by FPLC. HMC were incubated with IgA preparations and IgA bound to HMC was determined by flow cytometry analysis using standard curves constructed by known concentrations of κ-IgA1 or λ-IgA1. In order to avoid any increased binding of IgA to HMC due to elevated κ- or λ-IgA concentrations in JBP samples from patients, JBP samples from patients or controls were appropriately diluted to achieve comparable levels of total IgA1. No differences in the total mIgA1 or pIgA1 concentration, percentage of mIgA1 or pIgA1, or the κ/λ ratio of mIgA1 or pIgA1 were found between adjusted JBP samples from patients or healthy controls. We found a sharp rise in percentage of pIgA1 among IgA1 bound to HMC (70%), despite the fact that only 3% of the IgA1 in the adjusted JBP samples were polymeric, suggesting that pIgA1 had a higher affinity to HMC than mIgA1. Furthermore, the κ/λ ratios of pIgA1 bound to HMC were significantly lower than the κ/λ ratios of pIgA1 in adjusted JBP only with IgAN patients but not healthy controls (P = 0.0026). Our data suggest a preferential mesangial binding of polymeric λ-IgA1 from patients with IgAN. These polymeric λ-IgA immune complexes are likely to be "pathogenic" and are important in the pathogenesis of IgAN.en_HK
dc.languageengen_US
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/ki/index.htmlen_HK
dc.relation.ispartofKidney Internationalen_HK
dc.subject.meshAdulten_US
dc.subject.meshBiopolymers - Blood - Metabolismen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshFemaleen_US
dc.subject.meshFlow Cytometryen_US
dc.subject.meshGlomerular Mesangium - Metabolismen_US
dc.subject.meshGlomerulonephritis, Iga - Immunology - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshImmunoglobulin A - Blood - Metabolismen_US
dc.subject.meshMaleen_US
dc.subject.meshMiddle Ageden_US
dc.titleIncreased binding of polymeric A-IgA to cultured human mesangial cells in IgA nephropathyen_HK
dc.typeArticleen_HK
dc.identifier.emailLai, KN: knlai@hku.hken_HK
dc.identifier.emailLeung, JCK: jckleung@hku.hken_HK
dc.identifier.authorityLai, KN=rp00324en_HK
dc.identifier.authorityLeung, JCK=rp00448en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1038/ki.1996.116-
dc.identifier.pmid8648928en_HK
dc.identifier.scopuseid_2-s2.0-0029864366en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0029864366&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume49en_HK
dc.identifier.issue3en_HK
dc.identifier.spage839en_HK
dc.identifier.epage845en_HK
dc.identifier.isiWOS:A1996TW63700031-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridLai, KN=7402135706en_HK
dc.identifier.scopusauthoridTo, WY=36933508700en_HK
dc.identifier.scopusauthoridLi, PKT=25928016800en_HK
dc.identifier.scopusauthoridLeung, JCK=7202180349en_HK

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