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Article: Serologic study of immunoglobulin A-fibronectin aggregates in immunoglobulin A nephropathy

TitleSerologic study of immunoglobulin A-fibronectin aggregates in immunoglobulin A nephropathy
Authors
Keywordsenzyme-linked immunosorbent assay
Immunoglobulin A nephropathy
immunoglobulin A-fibronectin aggregates
specificity
Issue Date1996
PublisherWB Saunders Co. The Journal's web site is located at http://www.elsevier.com/locate/ajkd
Citation
American Journal Of Kidney Diseases, 1996, v. 27 n. 5, p. 622-630 How to Cite?
AbstractThe immunoglobulin A (IgA)-fibronectin aggregates, detected by enzyme- linked immunosorbent assay using either antifibronectin or collagen I as binding protein, were previously found to be raised in the circulation of patients with IgA nephropathy (IgAN). It has been suggested that IgA- fibronectin aggregates are involved in the pathogenesis and that the plasma IgA-fibronectin level may even be of diagnostic value in IgAN. Nevertheless, a recent report has questioned the specificity of these assays as plasma IgA may interact with immobilized IgG and these assays detect not only IgA- fibronectin, but also total plasma IgA. These doubts render the interpretation of raised IgA-fibronectin aggregates in IgAN impossible. We isolated total IgA 1 in plasma by jacalin-agarose. Monomeric and polymeric IgA 1 were distinctly separated by fast protein liquid chromatography. When the fast protein liquid chromatography fractions were analyzed for IgA- fibronectin using the antifibronectin capture assay, increased optical density values were predominantly observed in polymeric IgA but not in monomeric IgA. Similar findings were found when the fast protein liquid chromatography fractions were studied using a novel gelatin-anti-IgA assay that avoided nonspecific interaction between plasma IgA and immobilized IgG used as the capture antibody in antifibronectin capture assay. Using our gelatin-anti-IgA assay, we failed to demonstrate a diagnostic increase in IgA-fibronectin aggregates in polymeric IgA from patients with IgAN compared with controls. Our finding of circulating IgA-fibronectin aggregates in patients with IgAN comparable to those of healthy controls did not support the notion that these aggregates may have a pathogenetic role or diagnostic value in IgAN.
Persistent Identifierhttp://hdl.handle.net/10722/162149
ISSN
2015 Impact Factor: 6.269
2015 SCImago Journal Rankings: 2.313
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorKar Neng Laien_HK
dc.contributor.authorWah Yuen Toen_HK
dc.contributor.authorLeung, JCKen_HK
dc.contributor.authorYu, AWYen_HK
dc.contributor.authorLi, PKTen_HK
dc.date.accessioned2012-09-05T05:17:39Z-
dc.date.available2012-09-05T05:17:39Z-
dc.date.issued1996en_HK
dc.identifier.citationAmerican Journal Of Kidney Diseases, 1996, v. 27 n. 5, p. 622-630en_HK
dc.identifier.issn0272-6386en_HK
dc.identifier.urihttp://hdl.handle.net/10722/162149-
dc.description.abstractThe immunoglobulin A (IgA)-fibronectin aggregates, detected by enzyme- linked immunosorbent assay using either antifibronectin or collagen I as binding protein, were previously found to be raised in the circulation of patients with IgA nephropathy (IgAN). It has been suggested that IgA- fibronectin aggregates are involved in the pathogenesis and that the plasma IgA-fibronectin level may even be of diagnostic value in IgAN. Nevertheless, a recent report has questioned the specificity of these assays as plasma IgA may interact with immobilized IgG and these assays detect not only IgA- fibronectin, but also total plasma IgA. These doubts render the interpretation of raised IgA-fibronectin aggregates in IgAN impossible. We isolated total IgA 1 in plasma by jacalin-agarose. Monomeric and polymeric IgA 1 were distinctly separated by fast protein liquid chromatography. When the fast protein liquid chromatography fractions were analyzed for IgA- fibronectin using the antifibronectin capture assay, increased optical density values were predominantly observed in polymeric IgA but not in monomeric IgA. Similar findings were found when the fast protein liquid chromatography fractions were studied using a novel gelatin-anti-IgA assay that avoided nonspecific interaction between plasma IgA and immobilized IgG used as the capture antibody in antifibronectin capture assay. Using our gelatin-anti-IgA assay, we failed to demonstrate a diagnostic increase in IgA-fibronectin aggregates in polymeric IgA from patients with IgAN compared with controls. Our finding of circulating IgA-fibronectin aggregates in patients with IgAN comparable to those of healthy controls did not support the notion that these aggregates may have a pathogenetic role or diagnostic value in IgAN.en_HK
dc.languageengen_US
dc.publisherWB Saunders Co. The Journal's web site is located at http://www.elsevier.com/locate/ajkden_HK
dc.relation.ispartofAmerican Journal of Kidney Diseasesen_HK
dc.subjectenzyme-linked immunosorbent assayen_HK
dc.subjectImmunoglobulin A nephropathyen_HK
dc.subjectimmunoglobulin A-fibronectin aggregatesen_HK
dc.subjectspecificityen_HK
dc.subject.meshAntibodies - Diagnostic Useen_US
dc.subject.meshBiological Markers - Blooden_US
dc.subject.meshCarrier Proteins - Diagnostic Useen_US
dc.subject.meshChromatography, Liquiden_US
dc.subject.meshCollagen - Diagnostic Useen_US
dc.subject.meshEnzyme-Linked Immunosorbent Assayen_US
dc.subject.meshFemaleen_US
dc.subject.meshFibronectins - Blood - Immunologyen_US
dc.subject.meshGelatin - Diagnostic Useen_US
dc.subject.meshGlomerulonephritis, Iga - Blooden_US
dc.subject.meshHumansen_US
dc.subject.meshImmunoglobulin A - Blooden_US
dc.subject.meshImmunoglobulin G - Diagnostic Useen_US
dc.subject.meshLectins - Diagnostic Useen_US
dc.subject.meshMaleen_US
dc.subject.meshPlant Lectinsen_US
dc.subject.meshSensitivity And Specificityen_US
dc.subject.meshSepharose - Diagnostic Useen_US
dc.titleSerologic study of immunoglobulin A-fibronectin aggregates in immunoglobulin A nephropathyen_HK
dc.typeArticleen_HK
dc.identifier.emailKar Neng Lai: knlai@hku.hken_HK
dc.identifier.emailLeung, JCK: jckleung@hku.hken_HK
dc.identifier.authorityKar Neng Lai=rp00324en_HK
dc.identifier.authorityLeung, JCK=rp00448en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/S0272-6386(96)90095-5-
dc.identifier.pmid8629620-
dc.identifier.scopuseid_2-s2.0-0029960066en_HK
dc.identifier.volume27en_HK
dc.identifier.issue5en_HK
dc.identifier.spage622en_HK
dc.identifier.epage630en_HK
dc.identifier.isiWOS:A1996UJ49700002-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridKar Neng Lai=7402135706en_HK
dc.identifier.scopusauthoridWah Yuen To=16752471800en_HK
dc.identifier.scopusauthoridLeung, JCK=7202180349en_HK
dc.identifier.scopusauthoridYu, AWY=7401478900en_HK
dc.identifier.scopusauthoridLi, PKT=25928016800en_HK

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