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dc.contributor.authorKolka, Ragnhildur
dc.contributor.authorValdimarsson, Helgi
dc.contributor.authorBodvarsson, Magnus
dc.contributor.authorHardarson, Sverrir
dc.contributor.authorJonsson, Thorbjorn
dc.date.accessioned2014-02-11T09:48:27Z
dc.date.available2014-02-11T09:48:27Z
dc.date.issued2013-09
dc.identifier.citationAPMIS 2013, 121(9):890-7en
dc.identifier.issn1600-0463
dc.identifier.pmid23398317
dc.identifier.doi10.1111/apm.12051
dc.identifier.urihttp://hdl.handle.net/2336/312600
dc.descriptionTo access publisher's full text version of this article. Please click on the hyperlink in Additional Links field.en
dc.description.abstractDefective glycosylation and immune complex (IC) formation may be of primary importance in immunoglobulin A nephropathy (IgAN) pathogenesis. The aim of this study was to determine whether defective IgA1 glycosylation might support renal deposition of IgA and disease activity. IgA was isolated from the serum of 44 IgAN patients and 46 controls and glycosylation analysed by ELISA using glycan-specific lectins. IgA was measured by immunodiffusion and immune complexes by ELISA. IgA subclasses in IC deposits in kidney glomeruli were identified by immunohistochemical methods. A significant increase in N-acetylgalactosamine (GalNAc) in terminal position (p = 0.02) observed in some of the IgAN patients, became more pronounced when sialic acid was removed from IgA1, indicating enhanced expression of α-2,6-sialyltransferase in patients compared with controls (p < 0.0001). Patients with defective galactosylation had lower serum IgA than other IgAN patients (p = 0.003). IgAN patients with both IgA1 and IgA2 glomerular deposits (21.7%) had increased GalNAc in terminal position (p = 0.003). Taken together, our results show that increased IgA glycosylation in IgAN associates with low levels of IgA, concomitant IgA1 and IgA2 glomerular deposits and poor clinical outcome.
dc.description.sponsorshipIcelandic Research Fund (RANNIS) Science Fund of Landspitali University Hospital Scandinavian Society for Immunologyen
dc.language.isoenen
dc.publisherWiley-Blackwellen
dc.relation.urlhttp://dx.doi.org/10.1111/apm.12051en
dc.relation.urlhttp://onlinelibrary.wiley.com/doi/10.1111/apm.12051/pdf
dc.rightsArchived with thanks to APMIS : acta pathologica, microbiologica, et immunologica Scandinavicaen
dc.subject.meshAcetylgalactosamine
dc.subject.meshAdolescent
dc.subject.meshAdult
dc.subject.meshAged
dc.subject.meshAntigen-Antibody Complex
dc.subject.meshCase-Control Studies
dc.subject.meshFemale
dc.subject.meshGlomerulonephritis, IGA
dc.subject.meshGlycosylation
dc.subject.meshHumans
dc.subject.meshImmunoglobulin A
dc.subject.meshKidney Glomerulus
dc.subject.meshLectins
dc.subject.meshMale
dc.subject.meshMiddle Aged
dc.subject.meshSialyltransferases
dc.titleDefective immunoglobulin A (IgA) glycosylation and IgA deposits in patients with IgA nephropathy.en
dc.typeArticleen
dc.contributor.departmentLandspitali University Hospitalen
dc.identifier.journalAPMIS : acta pathologica, microbiologica, et immunologica Scandinavicaen
html.description.abstractDefective glycosylation and immune complex (IC) formation may be of primary importance in immunoglobulin A nephropathy (IgAN) pathogenesis. The aim of this study was to determine whether defective IgA1 glycosylation might support renal deposition of IgA and disease activity. IgA was isolated from the serum of 44 IgAN patients and 46 controls and glycosylation analysed by ELISA using glycan-specific lectins. IgA was measured by immunodiffusion and immune complexes by ELISA. IgA subclasses in IC deposits in kidney glomeruli were identified by immunohistochemical methods. A significant increase in N-acetylgalactosamine (GalNAc) in terminal position (p = 0.02) observed in some of the IgAN patients, became more pronounced when sialic acid was removed from IgA1, indicating enhanced expression of α-2,6-sialyltransferase in patients compared with controls (p < 0.0001). Patients with defective galactosylation had lower serum IgA than other IgAN patients (p = 0.003). IgAN patients with both IgA1 and IgA2 glomerular deposits (21.7%) had increased GalNAc in terminal position (p = 0.003). Taken together, our results show that increased IgA glycosylation in IgAN associates with low levels of IgA, concomitant IgA1 and IgA2 glomerular deposits and poor clinical outcome.


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