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Article: Characteristics of polymeric λ-IgA binding to leukocytes in IgA nephropathy

TitleCharacteristics of polymeric λ-IgA binding to leukocytes in IgA nephropathy
Authors
Issue Date2002
PublisherAmerican Society of Nephrology. The Journal's web site is located at http://www.jasn.org
Citation
Journal Of The American Society Of Nephrology, 2002, v. 13 n. 9, p. 2309-2319 How to Cite?
AbstractIgA nephropathy (IgAN) is characterized by predominant mesangial polymeric IgA1 (pIgA1) deposits, with increased plasma IgA1 levels. Plasma IgA levels are determined by the rate of IgA production, uptake by leukocytes, and removal by hepatocytes. Fcα receptor 1 (FcαR1) is a candidate molecule for the regulation of IgA levels, but reports of its expression in leukocytes in IgAN are conflicting. Increased binding of endogenous IgA to circulating granulocytes and monocytes in IgAN was demonstrated in this study. FcαR1 expression on leukocytes was increased, independently of plasma IgA levels. FcαR1 was not saturated in leukocytes, because of internalization of IgA after uptake. Further binding of exogenous IgA isolated from individual subjects was observed with leukocytes from the same subjects. Compared with cells from control subjects, granulocytes but not monocytes from patients with IgAN exhibited a greater binding capacity for exogenous IgA, predominantly pIgA. To circumvent the possibility that endogenous IgA might alter FcαR1 expression, granulocytes or monocytes derived from the HL-60 or U937 cell lines were used to explore the nature of IgA binding. A higher affinity for pIgA was demonstrated. Inhibition studies using unlabeled IgA, other serum proteins, or a specific FcαR1-blocking antibody suggested binding mechanisms other than FcαR1 for pIgA uptake by leukocytes. This study also suggested the migration and/or sequestration of "activated" leukocytes with predominant λ-IgA in the mononuclear phagocytic system or inflammatory tissues, after the initial binding of A-pIgA. These immunologic abnormalities might contribute to the glomerulointerstitial injury in IgAN, in the presence of leukocytic infiltration.
Persistent Identifierhttp://hdl.handle.net/10722/162627
ISSN
2015 Impact Factor: 8.491
2015 SCImago Journal Rankings: 4.699
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLai, KNen_HK
dc.contributor.authorChan, LYYen_HK
dc.contributor.authorTang, SCWen_HK
dc.contributor.authorTsang, AWLen_HK
dc.contributor.authorGuo, Hen_HK
dc.contributor.authorTse, KCen_HK
dc.contributor.authorYip, Ten_HK
dc.contributor.authorLeung, JCKen_HK
dc.date.accessioned2012-09-05T05:21:49Z-
dc.date.available2012-09-05T05:21:49Z-
dc.date.issued2002en_HK
dc.identifier.citationJournal Of The American Society Of Nephrology, 2002, v. 13 n. 9, p. 2309-2319en_HK
dc.identifier.issn1046-6673en_HK
dc.identifier.urihttp://hdl.handle.net/10722/162627-
dc.description.abstractIgA nephropathy (IgAN) is characterized by predominant mesangial polymeric IgA1 (pIgA1) deposits, with increased plasma IgA1 levels. Plasma IgA levels are determined by the rate of IgA production, uptake by leukocytes, and removal by hepatocytes. Fcα receptor 1 (FcαR1) is a candidate molecule for the regulation of IgA levels, but reports of its expression in leukocytes in IgAN are conflicting. Increased binding of endogenous IgA to circulating granulocytes and monocytes in IgAN was demonstrated in this study. FcαR1 expression on leukocytes was increased, independently of plasma IgA levels. FcαR1 was not saturated in leukocytes, because of internalization of IgA after uptake. Further binding of exogenous IgA isolated from individual subjects was observed with leukocytes from the same subjects. Compared with cells from control subjects, granulocytes but not monocytes from patients with IgAN exhibited a greater binding capacity for exogenous IgA, predominantly pIgA. To circumvent the possibility that endogenous IgA might alter FcαR1 expression, granulocytes or monocytes derived from the HL-60 or U937 cell lines were used to explore the nature of IgA binding. A higher affinity for pIgA was demonstrated. Inhibition studies using unlabeled IgA, other serum proteins, or a specific FcαR1-blocking antibody suggested binding mechanisms other than FcαR1 for pIgA uptake by leukocytes. This study also suggested the migration and/or sequestration of "activated" leukocytes with predominant λ-IgA in the mononuclear phagocytic system or inflammatory tissues, after the initial binding of A-pIgA. These immunologic abnormalities might contribute to the glomerulointerstitial injury in IgAN, in the presence of leukocytic infiltration.en_HK
dc.languageengen_US
dc.publisherAmerican Society of Nephrology. The Journal's web site is located at http://www.jasn.orgen_HK
dc.relation.ispartofJournal of the American Society of Nephrologyen_HK
dc.subject.meshGlomerulonephritis, IGA - immunology-
dc.subject.meshImmunoglobulin gamma-Chains - immunology - metabolism-
dc.subject.meshImmunoglobulin kappa-Chains - immunology - metabolism-
dc.subject.meshLeukocytes - immunology - metabolism-
dc.subject.meshImmunoglobulin A - blood - immunology - pharmacology-
dc.titleCharacteristics of polymeric λ-IgA binding to leukocytes in IgA nephropathyen_HK
dc.typeArticleen_HK
dc.identifier.emailLai, KN: knlai@hku.hken_HK
dc.identifier.emailTang, SCW: scwtang@hku.hken_HK
dc.identifier.emailLeung, JCK: jckleung@hku.hken_HK
dc.identifier.authorityLai, KN=rp00324en_HK
dc.identifier.authorityTang, SCW=rp00480en_HK
dc.identifier.authorityLeung, JCK=rp00448en_HK
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1097/01.ASN.0000026497.82930.73en_HK
dc.identifier.pmid12191975-
dc.identifier.scopuseid_2-s2.0-0036707884en_HK
dc.identifier.hkuros81646-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036707884&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume13en_HK
dc.identifier.issue9en_HK
dc.identifier.spage2309en_HK
dc.identifier.epage2319en_HK
dc.identifier.isiWOS:000177687000013-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLai, KN=7402135706en_HK
dc.identifier.scopusauthoridChan, LYY=8108378300en_HK
dc.identifier.scopusauthoridTang, SCW=7403437082en_HK
dc.identifier.scopusauthoridTsang, AWL=7006979244en_HK
dc.identifier.scopusauthoridGuo, H=55468645700en_HK
dc.identifier.scopusauthoridTse, KC=7102609864en_HK
dc.identifier.scopusauthoridYip, T=7004283977en_HK
dc.identifier.scopusauthoridLeung, JCK=7202180349en_HK

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