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NDT Advance Access published online on May 12, 2008
Nephrology Dialysis Transplantation, doi:10.1093/ndt/gfn203
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© The Author [2008]. Published by Oxford University Press on behalf of ERA-EDTA. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org


Is sialylation of IgA the agent provocateur of IgA nephropathy?*

Alice Smith1,2, Karen Molyneux1,2, John Feehally1,2 and Jonathan Barratt1,2

1 Department of Infection, Immunity and Inflammation, University of Leicester 2 John Walls Renal Unit, University Hospitals of Leicester NHS Trust, Leicester, UK

Correspondence and offprint requests to: John Feehally, Department of Infection, Immunity and Inflammation, John Walls Renal Unit, Leicester General Hospital, Gwendolen Road, Leicester, LE5 4 PW, UK. Tel: +44-0116-258-8043; Fax: +44-0116-258-4764; E-mail: jf27@le.ac.uk

Keywords: IgA glycosylation; IgA nephropathy; sialyltransferases

The first 10% of the full text of this article appears below.



   Review of field
 
Altered O-glycosylation of IgA1 has been recognized as a potentially pathogenic abnormality in IgAN for ~20 years [1]. The 17-amino acid hinge region of IgA1 can carry from 0 to 6 O-glycan moieties, each of which is a relatively short and simple sugar chain, but there are up to six different potential forms [2]. The variability in the number and location of occupied O-glycosylation sites, and the different possible forms of each of these chains (Figure 2) result in a vast array of potential IgA1 O-glycoforms, and this immense diversity has hindered the precise structural definition of the abnormality in IgAN.


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  		Fig. 2 The major O-glycan forms of human . . . [Full Text of this Article]

 


   Clinical implications
 


   Take home message
 

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