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Article: Size-dependent binding of IgA to HepG2, U937, and human mesangial cells

TitleSize-dependent binding of IgA to HepG2, U937, and human mesangial cells
Authors
Issue Date2002
PublisherMosby, Inc. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/709553/description#description
Citation
Journal Of Laboratory And Clinical Medicine, 2002, v. 140 n. 6, p. 398-406 How to Cite?
AbstractIgA nephropathy (IgAN) is characterized by increased circulating IgA and mesangial IgA deposition. The mechanism of mesangial IgA deposition remains poorly understood in IgAN. In this report, we studied the binding characteristics of serum IgA from patients with IgAN and healthy controls to different cell types, including a liver-cell line (HepG2), a monocytic cell line (U937), and human mesangial cells (HMCs). Jacalin-bound proteins (JBPs) were purified from serum IgA by means of jacalin affinity chromatography. Total IgA concentrations were significantly higher in patients with IgAN than in controls (P < .001). JBPs were further separated by means of size exclusion chromatography, and six pooled fractions with molecular weight ranging from 50 to 1000 kD were obtained. The concentration of low-molecular-weight (LMW) IgA complexes (150-300 kD) and high-molecular-weight (HMW) IgA complexes (300-1000 kD) were significantly higher in patients than in healthy controls (P < .001 and .05, respectively). Cultured human mesangial cells bound more IgA of 300 to 610 kD in IgA isolated from patients with IgAN (P < .01). The binding of IgA (LMW and HMW) from patients with IgAN to HepG2 was significantly higher than that of IgA preparations from controls. U937 significantly bound more IgA of 150 to 825 kD in IgA isolated from patients with IgAN (P < .01). Different and distinct binding patterns were observed in the three cell types for IgA with different molecular weights. HMCs bound more HMW than LMW IgA. We noted preferential binding of LMW (150 to 300 kDa) and intermediate (350-710 kDa) IgA to HepG2 than of IgA complexes of more than 710 kDa. U937 mainly bound LMW and intermediate size IgA (150 to 710 kDa) with no binding of IgA with size greater than 710 kD. Our findings suggest that monocytes, hepatocytes, and mesangial cells have unique properties with regard to their binding to different forms of IgA. These characteristic properties may alter the catabolism of circulating IgA and, hence, predispose their deposition in the kidney mesangium in IgAN.
Persistent Identifierhttp://hdl.handle.net/10722/77073
ISSN
2008 Impact Factor: 2.795
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLeung, JCKen_HK
dc.contributor.authorTsang, AWLen_HK
dc.contributor.authorChan, LYYen_HK
dc.contributor.authorTang, SCWen_HK
dc.contributor.authorLam, MFen_HK
dc.contributor.authorLai, KNen_HK
dc.date.accessioned2010-09-06T07:27:58Z-
dc.date.available2010-09-06T07:27:58Z-
dc.date.issued2002en_HK
dc.identifier.citationJournal Of Laboratory And Clinical Medicine, 2002, v. 140 n. 6, p. 398-406en_HK
dc.identifier.issn0022-2143en_HK
dc.identifier.urihttp://hdl.handle.net/10722/77073-
dc.description.abstractIgA nephropathy (IgAN) is characterized by increased circulating IgA and mesangial IgA deposition. The mechanism of mesangial IgA deposition remains poorly understood in IgAN. In this report, we studied the binding characteristics of serum IgA from patients with IgAN and healthy controls to different cell types, including a liver-cell line (HepG2), a monocytic cell line (U937), and human mesangial cells (HMCs). Jacalin-bound proteins (JBPs) were purified from serum IgA by means of jacalin affinity chromatography. Total IgA concentrations were significantly higher in patients with IgAN than in controls (P < .001). JBPs were further separated by means of size exclusion chromatography, and six pooled fractions with molecular weight ranging from 50 to 1000 kD were obtained. The concentration of low-molecular-weight (LMW) IgA complexes (150-300 kD) and high-molecular-weight (HMW) IgA complexes (300-1000 kD) were significantly higher in patients than in healthy controls (P < .001 and .05, respectively). Cultured human mesangial cells bound more IgA of 300 to 610 kD in IgA isolated from patients with IgAN (P < .01). The binding of IgA (LMW and HMW) from patients with IgAN to HepG2 was significantly higher than that of IgA preparations from controls. U937 significantly bound more IgA of 150 to 825 kD in IgA isolated from patients with IgAN (P < .01). Different and distinct binding patterns were observed in the three cell types for IgA with different molecular weights. HMCs bound more HMW than LMW IgA. We noted preferential binding of LMW (150 to 300 kDa) and intermediate (350-710 kDa) IgA to HepG2 than of IgA complexes of more than 710 kDa. U937 mainly bound LMW and intermediate size IgA (150 to 710 kDa) with no binding of IgA with size greater than 710 kD. Our findings suggest that monocytes, hepatocytes, and mesangial cells have unique properties with regard to their binding to different forms of IgA. These characteristic properties may alter the catabolism of circulating IgA and, hence, predispose their deposition in the kidney mesangium in IgAN.en_HK
dc.languageengen_HK
dc.publisherMosby, Inc. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/709553/description#descriptionen_HK
dc.relation.ispartofJournal of Laboratory and Clinical Medicineen_HK
dc.rightsJournal of Laboratory and Clinical Medicine. Copyright © Mosby, Inc.en_HK
dc.subject.meshAntigen-Antibody Complex - metabolismen_HK
dc.subject.meshChromatography, Affinityen_HK
dc.subject.meshGlomerular Mesangium - cytology - metabolismen_HK
dc.subject.meshGlomerulonephritis - metabolismen_HK
dc.subject.meshHepatocytes - cytology - metabolismen_HK
dc.subject.meshHumansen_HK
dc.subject.meshImmunoglobulin A - classification - isolation & purification - metabolismen_HK
dc.subject.meshMaleen_HK
dc.subject.meshMolecular Weighten_HK
dc.subject.meshMonocytes - cytology - metabolismen_HK
dc.subject.meshParticle Sizeen_HK
dc.subject.meshTumor Cells, Cultureden_HK
dc.subject.meshU937 Cellsen_HK
dc.titleSize-dependent binding of IgA to HepG2, U937, and human mesangial cellsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0022-2143&volume=140&spage=398&epage=406&date=2002&atitle=Size-dependent+Binding+of+IgA+to+HepG2,+U937,+and+Human+Mesangial+Cells.en_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.doi10.1067/mlc.2002.129338en_HK
dc.identifier.pmid12486407en_HK
dc.identifier.scopuseid_2-s2.0-0036918517en_HK
dc.identifier.hkuros81133en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036918517&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume140en_HK
dc.identifier.issue6en_HK
dc.identifier.spage398en_HK
dc.identifier.epage406en_HK
dc.identifier.isiWOS:000180023500005-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLeung, JCK=7202180349en_HK
dc.identifier.scopusauthoridTsang, AWL=7006979244en_HK
dc.identifier.scopusauthoridChan, LYY=8108378300en_HK
dc.identifier.scopusauthoridTang, SCW=7403437082en_HK
dc.identifier.scopusauthoridLam, MF=35300050600en_HK
dc.identifier.scopusauthoridLai, KN=7402135706en_HK

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