These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Methodological approaches to the analysis of IgA1 O-glycosylation in IgA nephropathy.
    Author: Allen AC.
    Journal: J Nephrol; 1999; 12(2):76-84. PubMed ID: 10378662.
    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.
    [Abstract] [Full Text] [Related] [New Search]