Format

Send to

Choose Destination
See comment in PubMed Commons below
J Nephrol. 1999 Mar-Apr;12(2):76-84.

Methodological approaches to the analysis of IgA1 O-glycosylation in IgA nephropathy.

Author information

1
Department of Nephrology, Leicester General Hospital, UK. aa50@le.ac.uk

Abstract

IgA nephropathy (IgAN) is a common form of glomerulonephritis in which IgA1 molecules deposit in the renal mesangium, leading to progressive glomerular inflammatory injury in a significant proportion of patients. The mechanisms underlying the pathogenesis of IgAN remain poorly understood, but altered O-glycosylation, a physicochemical abnormality of IgA1 observed in these patients, may be a contributory factor. Although many studies have reported aberrant IgA1 O-glycosylation in IgAN, the precise structural nature of the defect remains to be fully characterised, and analysis of IgA1 O-glycans has proved technically challenging. Three main strategies have been employed: lectin binding to the O-glycans in situ on the whole IgA1 molecule; mass spectroscopy of isolated O-glycosylated glycopeptides; and size/charge separation of free O-glycans released from IgA1. In this review, the basic principles, strengths and weaknesses of each of these methodological approaches are considered, together with a summary of the data obtained from their use. One of the common criticisms of many studies of IgA1 O-glycosylation is the method of IgA1 purification employed, and therefore, this issue is also critically discussed.

PMID:
10378662
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Loading ...
    Support Center