Mass spectrometry proves under-O-glycosylation of glomerular IgA1 in IgA nephropathy.

@article{Hiki2001MassSP,
  title={Mass spectrometry proves under-O-glycosylation of glomerular IgA1 in IgA nephropathy.},
  author={Yoshiyuki Hiki and Hiroko Odani and Masaaki Takahashi and Yoshinari Yasuda and A Nishimoto and Hitoo Iwase and Toru Shinzato and Y. Kobayashi and Kenji Maeda},
  journal={Kidney international},
  year={2001},
  volume={59 3},
  pages={
          1077-85
        }
}
BACKGROUND The IgA1 molecule, which is predominantly deposited in glomeruli in IgA nephropathy (IgAN), is a unique serum glycoprotein because it has O-glycan side chains in its hinge region. Our study was conducted to investigate the O-glycan structure in the glomerular IgA1 in IgAN. METHODS The IgA1 was separated from 290 renal biopsy specimens of 278 IgAN patients and from four serum IgA1 samples (IgAN, 2; control, 2). The variety of O-glycan glycoform was determined by estimating the… 
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O- and N-Glycosylation of Serum Immunoglobulin A is Associated with IgA Nephropathy and Glomerular Function.

High-resolution data suggest that IgA O- and N-glycopeptides are promising targets for future investigations on the pathophysiology of IgAN and as potential noninvasive biomarkers for disease prediction and deteriorating kidney function.

O-glycosylation of serum IgD in IgA nephropathy.

Observations show that abnormal IgA1 O-glycosylation in IgAN is not due to an inherent defect in glycosylations mechanisms but arises only at a later stage in B cell development and may be secondary to aberrant immunoregulation.

Clustered O-Glycans of IgA1

The results represent a new clinically relevant approach that requires ECD/electron transfer dissociation-type fragmentation to define the molecular events leading to pathogenesis of a chronic kidney disease and offers generally applicable principles for the analysis of clustered sites of O-glycosylation.

Identification of Distinct Glycoforms of IgA1 in Plasma from Patients with Immunoglobulin A (IgA) Nephropathy and Healthy Individuals*

It is demonstrated that undergalactosylation of O-glycans in IgA1 is not restricted to IgAN and suggested that in vivo inefficiency of T-synthase toward IgA 1 in a subpopulation of B or plasma cells, as well as overall elevation of IgA, may contribute to IgAn pathogenesis.

Quantitative change of IgA hinge O-glycan composition is a novel marker of therapeutic responses of IgA nephropathy.

Analysis of O-glycan heterogeneity in IgA1 myeloma proteins by Fourier transform ion cyclotron resonance mass spectrometry: implications for IgA nephropathy

The results suggest that future analysis of IgA1 HR from IgAN patients and normal healthy controls should be feasible, and the first AI-ECD fragmentation on an individual IgA 1 O-glycopeptide from an IgA2 HR preparation that is reproducible for each IgA3 myeloma protein is reported.

Diagnostic Potential of Plasma IgA1 O-Glycans in Discriminating IgA Nephropathy From Other Glomerular Diseases and Healthy Participants

The amount of GalNAc and galactose in plasma IgA1 hinge region identified by glycoproteomics could be used as a diagnostic biomarker for IgA nephropathy and is promising for practical clinical applications.

IgA1 molecules produced by tonsillar lymphocytes are under-O-glycosylated in IgA nephropathy.

  • A. HorieY. Hiki K. Maeda
  • Medicine, Biology
    American journal of kidney diseases : the official journal of the National Kidney Foundation
  • 2003

O-glycosylation of serum IgA1 antibodies against mucosal and systemic antigens in IgA nephropathy.

It is demonstrated that IgA 1 O-glycosylation normally varies in different immune responses and that patients produce the full spectrum of IgA1 O- glycoforms.

Serum under-galactosylated IgA1 is increased in Japanese patients with IgA nephropathy.

HAA-IgA binding is significantly increased in Japanese IgAN patients and the O-glycan structure of IgA1 hinge glycopeptides was shifted to smaller molecular weights in high HAA- IgA-binding IgAN Patients.
...

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