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Article: Increased sialylation of polymeric immunoglobulin A1: Mechanism of selective glomerular deposition in immunoglobulin A nephropathy?

TitleIncreased sialylation of polymeric immunoglobulin A1: Mechanism of selective glomerular deposition in immunoglobulin A nephropathy?
Authors
Issue Date1999
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, 1999, v. 133 n. 2, p. 152-160 How to Cite?
AbstractImmunoglobulin A nephropathy (IgAN) is characterized by raised serum IgA and predominant mesangial IgA deposits of polymeric nature. The abnormal glycosylation of the carbohydrate moieties in the hinge region of the IgA molecule has recently attracted much attention. In this study we investigated the galactosylation and sialylation of monomeric and polymeric IgA1 isolated from patients with IgAN. Total IgA1 in serum samples from patients with IgAN or from healthy controls was isolated with a jacalin-agarose column as jacalin-bound protein (JBP). Monomeric and polymeric IgA1 were distinctly separated by fast protein liquid chromatography. Lectin binding assays were designed to examine the sialylation and the expression of terminal galactose and N-acetyl galactosamine of the O-linked carbohydrate in the hinge region of the IgA molecule. Reduced terminal galactosylation was demonstrated in serum IgA and monomeric IgA1 isolated from patients with IgAN as compared with results in healthy control subjects. However, a reduction in terminal galactosylation was not found in polymeric IgA1 isolated from patients with IgAN. Instead, increased sialylation of IgA1 (α2-3 linked to galactose) was demonstrated in polymeric IgA1. This abnormality of IgA1 could bear considerable implication on the pathogenesis of IgAN, because the masking effect of sialic acid may hinder the clearance of polymeric IgA1 by the asialoglycoprotein receptor (ASGP-R) of the liver cells. An increase in the sialylated content would also render the polymeric IgA from patients with IgAN more anionic. These immunochemical properties may contribute to the selective glomerular deposition of polymeric IgA1 in IgAN.
Persistent Identifierhttp://hdl.handle.net/10722/162348
ISSN
2008 Impact Factor: 2.795
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLeung, JCKen_HK
dc.contributor.authorPoon, PYKen_HK
dc.contributor.authorLai, KNen_HK
dc.date.accessioned2012-09-05T05:19:10Z-
dc.date.available2012-09-05T05:19:10Z-
dc.date.issued1999en_HK
dc.identifier.citationJournal Of Laboratory And Clinical Medicine, 1999, v. 133 n. 2, p. 152-160en_HK
dc.identifier.issn0022-2143en_HK
dc.identifier.urihttp://hdl.handle.net/10722/162348-
dc.description.abstractImmunoglobulin A nephropathy (IgAN) is characterized by raised serum IgA and predominant mesangial IgA deposits of polymeric nature. The abnormal glycosylation of the carbohydrate moieties in the hinge region of the IgA molecule has recently attracted much attention. In this study we investigated the galactosylation and sialylation of monomeric and polymeric IgA1 isolated from patients with IgAN. Total IgA1 in serum samples from patients with IgAN or from healthy controls was isolated with a jacalin-agarose column as jacalin-bound protein (JBP). Monomeric and polymeric IgA1 were distinctly separated by fast protein liquid chromatography. Lectin binding assays were designed to examine the sialylation and the expression of terminal galactose and N-acetyl galactosamine of the O-linked carbohydrate in the hinge region of the IgA molecule. Reduced terminal galactosylation was demonstrated in serum IgA and monomeric IgA1 isolated from patients with IgAN as compared with results in healthy control subjects. However, a reduction in terminal galactosylation was not found in polymeric IgA1 isolated from patients with IgAN. Instead, increased sialylation of IgA1 (α2-3 linked to galactose) was demonstrated in polymeric IgA1. This abnormality of IgA1 could bear considerable implication on the pathogenesis of IgAN, because the masking effect of sialic acid may hinder the clearance of polymeric IgA1 by the asialoglycoprotein receptor (ASGP-R) of the liver cells. An increase in the sialylated content would also render the polymeric IgA from patients with IgAN more anionic. These immunochemical properties may contribute to the selective glomerular deposition of polymeric IgA1 in IgAN.en_HK
dc.languageengen_US
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.-
dc.subject.meshAdulten_US
dc.subject.meshAmidohydrolases - Metabolismen_US
dc.subject.meshBiopolymers - Metabolismen_US
dc.subject.meshEnzyme-Linked Immunosorbent Assayen_US
dc.subject.meshFemaleen_US
dc.subject.meshGlomerular Mesangium - Metabolismen_US
dc.subject.meshGlomerulonephritis, Iga - Metabolismen_US
dc.subject.meshGlycosylationen_US
dc.subject.meshHumansen_US
dc.subject.meshImmunoglobulin A - Metabolismen_US
dc.subject.meshLectins - Isolation & Purification - Metabolismen_US
dc.subject.meshMaleen_US
dc.subject.meshMetalloendopeptidases - Metabolismen_US
dc.subject.meshMiddle Ageden_US
dc.subject.meshN-Acetylneuraminic Acid - Metabolismen_US
dc.subject.meshPeptide-N4-(N-Acetyl-Beta-Glucosaminyl) Asparagine Amidaseen_US
dc.subject.meshPlant Lectinsen_US
dc.titleIncreased sialylation of polymeric immunoglobulin A1: Mechanism of selective glomerular deposition in immunoglobulin A nephropathy?en_HK
dc.typeArticleen_HK
dc.identifier.emailLeung, JCK: jckleung@hku.hken_HK
dc.identifier.emailLai, KN: knlai@hku.hken_HK
dc.identifier.authorityLeung, JCK=rp00448en_HK
dc.identifier.authorityLai, KN=rp00324en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/S0022-2143(99)90008-2en_HK
dc.identifier.pmid9989767-
dc.identifier.scopuseid_2-s2.0-0033082936en_HK
dc.identifier.hkuros41546-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033082936&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume133en_HK
dc.identifier.issue2en_HK
dc.identifier.spage152en_HK
dc.identifier.epage160en_HK
dc.identifier.isiWOS:000078493200008-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLeung, JCK=7202180349en_HK
dc.identifier.scopusauthoridPoon, PYK=9336837000en_HK
dc.identifier.scopusauthoridLai, KN=7402135706en_HK

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