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Immune complex formation in IgA nephropathy: a case of the ‘right’ antibodies in the ‘wrong’ place at the ‘wrong’ time?

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posted on 2010-06-22, 14:43 authored by Jonathan Barratt, Frank Eitner, John Feehally, Jürgen Floege
One of the most striking findings in IgAN is an increase in the circulating levels of poorly galactosylated IgA1 O-glycoforms (Figure 1B). This has been observed in patient populations from North America, Europe and Asia, using a variety of techniques [1–3]. Importantly, two studies of IgA1 eluted from isolated glomeruli have shown that mesangial IgA is enriched with poorly galactosylated IgA1 O-glycoforms, strongly implicating the composition of IgA1 hinge region glycans in the mechanism of IgA1 deposition [4,5]. Novak and colleagues have also reported that these poorly galactosylated IgA1 O-glycoforms are predominantly found in circulating high molecular weight IgA-IC in IgAN [6].

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Citation

Nephrology Dialysis Transplantation, 2009, 24 (12), pp. 3620-3623.

Published in

Nephrology Dialysis Transplantation

Publisher

Oxford University Press (OUP)

issn

0931-0509

Copyright date

2009

Available date

2010-06-22

Publisher version

http://ndt.oxfordjournals.org/content/24/12/3620

Notes

Comment on: Suzuki H, Fan R, Zhang Z, Brown R, Hall S, Julian BA, Chatham WW, Suzuki Y, Wyatt RJ, Moldoveanu Z, Lee JY, Robinson J, Tomana M, Tomino Y, Mestecky J, Novak J. Aberrantly glycosylated IgA1 in IgA nephropathy patients is recognized by IgG antibodies with restricted heterogeneity. J Clin Invest. 2009 Jun;119(6):1668-77. doi: 10.1172/JCI38468. Epub 2009 May 26

Language

en

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