Modulation of Mesangial Cell Reactivity by Aberrantly Glycosylated IgA

Amore, Alessandro; Coppo, Rosanna

doi:10.1159/000045778

Cited by 11 publications

(9 citation statements)

References 27 publications

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“…By using a monoclonal antibody directed against a neoepitope on activated C3 (C3b, iC3b, C3dg), we found that GalNAc and Gal exposing glycoforms isolated form IgAN patients were significantly more active for complement activation than controls [17].…”

Section: Interaction Of Aberrantly Glycosylated Iga With Mesangial Cellsmentioning

confidence: 98%

“…The IgA receptors on mesangial cells do not exhibit properties of FcaR (CD89) or asialoglycoprotein receptors (ASGP-R) [15] and possibly belong to the transferrin receptor family [16]. Over the last years we focused particular attention on the modulation of mesangial cell reactivity by AGlyIgA, investigating the biologic effects of selected glycoforms from IgAN patients rich in terminal GalNAc or Neu5Ac2,6,GalNAc and in vitro deglycosylated IgA obtained by treating normal IgA with neuraminidase, desialylated (deSia) IgA, or neuraminidase and b-galactosidase (b-Gal) (deSia/deGal) IgA [17].…”

Section: Interaction Of Aberrantly Glycosylated Iga With Mesangial Cellsmentioning

confidence: 99%

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Aberrant glycosylation in IgA nephropathy (IgAN)

Coppo¹,

Amore

2004

Kidney International

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131

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Immunoglobulin A nephropathy (IgAN) patients exhibit circulating IgA1 with reduced galactose (Gal) and/or sialic acid (Neu5Ac) and increased exposure of N-acetylgalactosamine (GalNAc). These IgA glycoforms fix complement and in mesangial cells regulate integrin expression, enhance nitric oxide synthase (NOS) activity, decrease endothelial growth factor synthesis, meanwhile depressing proliferation and increasing apoptosis. Drugs can be targeted to the effects enhanced by aberrantly glycosylated IgA1 on mesangial cells. Recent data suggest that aberrant IgA1 glycosylation may modulate clinical expression and progression of IgAN.

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Section: Interaction Of Aberrantly Glycosylated Iga With Mesangial Cellsmentioning

confidence: 98%

Section: Interaction Of Aberrantly Glycosylated Iga With Mesangial Cellsmentioning

confidence: 99%

Aberrant glycosylation in IgA nephropathy (IgAN)

Coppo¹,

Amore

2004

Kidney International

Self Cite

160

131

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“…Each O-glycan may have variable sialylation and the hinge region glycans may contain an increased amount of N-acetylneuraminic acid (NeuNAc) residues attached to GalNac [29]. Alterations in N-glycosylation would also appear possible [30, 31]. The difference in glycosylation between patients is manifest in variable binding of IgAl to jacalin [32].…”

Section: Glycosylation Of Igamentioning

confidence: 99%

Pathogenetic Aspects of IgA Nephropathy

Rantala¹,

Mustonen

Hurme

et al. 2001

Nephron

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“…In vitro experiments as well as data from patients with IgAN indicate that degalactosylated IgA1 molecules bind C3 fragments with much higher affinity than normal IgA molecules 27 ; patients with IgAN and severe renal injury display glomerular deposition of mannose-binding lectin (a major recognition molecule of the lectin activation pathway of complement) probably as a consequence to higher affinity with aberrantly glycosylated circulating IgA1. 28 Amore and colleagues 29,30 showed that IgA glycoforms with aberrant glycosylation pattern, as well in vitro desialylated or degalactosylated normal IgA, are able to modulate several mesangial cell functions, including proliferation state, rate of apoptotic death, nitric oxide synthase activity, expression of integrins, and activation of NF-B.…”

Section: Discussionmentioning

confidence: 99%

Aberrantly Glycosylated IgA1 in Glomerular Immune Deposits of IgA Nephropathy

Giannakakis

Feriozzi

Perez

et al. 2007

Journal of the American Society of Nephrology

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In IgA nephropathy, abnormal O-glycosylation of IgA1 molecules contributes to mesangial IgA1 deposition and the development of glomerular injury; however, direct in situ demonstration of aberrantly O-glycosylated IgA1 within glomerular immune deposits has not been reported. This study investigated the presence of abnormally glycosylated IgA1 in situ and its spatial relationship with complement within the immune deposits and correlated these features with glomerular lesion severity. Immunofluorescence and confocal microscopy were used to evaluate 19 consecutive renal biopsies, and the severity of glomerular lesions were also scored. Aberrantly glycosylated IgA was observed within the immune deposits, and its amount was found to correlate with both the severity of glomerular lesions and the amount of C3c on the surface of the deposits. These results demonstrate that qualitative and quantitative evaluation of aberrantly glycosylated IgA can be performed on routine renal biopsy samples. Its presence in immune deposits likely influences the spatial organization of IgA and C3c, thereby contributing to the glomerular inflammatory response in IgA nephropathy.

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Modulation of Mesangial Cell Reactivity by Aberrantly Glycosylated IgA

Cited by 11 publications

References 27 publications

Aberrant glycosylation in IgA nephropathy (IgAN)

Aberrant glycosylation in IgA nephropathy (IgAN)

Pathogenetic Aspects of IgA Nephropathy

Aberrantly Glycosylated IgA1 in Glomerular Immune Deposits of IgA Nephropathy

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