Imperial College London
Alternate

ProfessorMatthewPickering

Faculty of Medicine, Department of Immunology and Inflammation

Centre Director, Professor of Rheumatology
 
 
 
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Contact

 

matthew.pickering Website

 
 
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Assistant

 

Miss Claudia Rocchi +44 (0)20 3313 2315

 
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Location

 

9N12Commonwealth BuildingHammersmith Campus

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Summary

 

Publications

Citation

BibTex format

@article{Dotz:2021:10.1681/ASN.2020081208,
author = {Dotz, V and Visconti, A and Lomax-Browne, HJ and Clerc, F and Hipgrave, Ederveen AL and Medjeral-Thomas, NR and Cook, HT and Pickering, MC and Wuhrer, M and Falchi, M},
doi = {10.1681/ASN.2020081208},
journal = {Journal of the American Society of Nephrology},
pages = {1--12},
title = {O- and N-glycosylation of serum immunoglobulin A is associated with IgA nephropathy and glomerular function.},
url = {http://dx.doi.org/10.1681/ASN.2020081208},
volume = {32},
year = {2021}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - BACKGROUND: IgA nephropathy (IgAN) is the most common primary glomerular disease worldwide and is a leading cause of renal failure. The disease mechanisms are not completely understood, but a higher abundance of galactose-deficient IgA is recognized to play a crucial role in IgAN pathogenesis. Although both types of human IgA (IgA1 and IgA2) have several N-glycans as post-translational modification, only IgA1 features extensive hinge-region O-glycosylation. IgA1 galactose deficiency on the O-glycans is commonly detected by a lectin-based method. To date, limited detail is known about IgA O- and N-glycosylation in IgAN. METHODS: To gain insights into the complex O- and N-glycosylation of serum IgA1 and IgA2 in IgAN, we used liquid chromatography-mass spectrometry (LC-MS) for the analysis of tryptic glycopeptides of serum IgA from 83 patients with IgAN and 244 age- and sex-matched healthy controls. RESULTS: Multiple structural features of N-glycosylation of IgA1 and IgA2 were associated with IgAN and glomerular function in our cross-sectional study. These features included differences in galactosylation, sialylation, bisection, fucosylation, and N-glycan complexity. Moreover, IgA1 O-glycan sialylation was associated with both the disease and glomerular function. Finally, glycopeptides were a better predictor of IgAN and glomerular function than galactose-deficient IgA1 levels measured by lectin-based ELISA. CONCLUSIONS: Our 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.
AU  - Dotz,V
AU  - Visconti,A
AU  - Lomax-Browne,HJ
AU  - Clerc,F
AU  - Hipgrave,Ederveen AL
AU  - Medjeral-Thomas,NR
AU  - Cook,HT
AU  - Pickering,MC
AU  - Wuhrer,M
AU  - Falchi,M
DO  - 10.1681/ASN.2020081208
EP  - 12
PY  - 2021///
SN  - 1046-6673
SP  - 1
TI  - O- and N-glycosylation of serum immunoglobulin A is associated with IgA nephropathy and glomerular function.
T2  - Journal of the American Society of Nephrology
UR  - http://dx.doi.org/10.1681/ASN.2020081208
UR  - https://www.ncbi.nlm.nih.gov/pubmed/34127537
UR  - https://jasn.asnjournals.org/content/early/2021/08/13/ASN.2020081208
UR  - http://hdl.handle.net/10044/1/91595
VL  - 32
ER  -
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