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: Abnormal IgA glycosylation in Henoch-Schönlein purpura restricted to patients with clinical nephritis.
    Author: Allen AC, Willis FR, Beattie TJ, Feehally J.
    Journal: Nephrol Dial Transplant; 1998 Apr; 13(4):930-4. PubMed ID: 9568852.
    Abstract:
    BACKGROUND: Glomerular deposition of IgA1 is a common feature of Henoch-Schönlein purpura, and is indistinguishable from that seen in IgA nephropathy. Serum IgA1 is abnormally O-glycosylated in IgA nephropathy, and this may contribute to mesangial IgA1 deposition and the development of glomerular injury. This altered O-glycosylation of IgA1 can be detected by its increased binding to the lectin Vicia villosa. METHODS: To investigate whether IgA1 is abnormally glycosylated in Henoch-Schönlein purpura, the binding of Vicia villosa lectin to serum IgA1 was studied in the following subject groups: IgA nephropathy; adults and children with Henoch-Schönlein purpura and nephritis; children with clinically diagnosed Henoch-Schönlein purpura but no renal involvement; adults and children with non-IgA associated glomerulonephritis; and matched controls. RESULTS: The abnormality of lectin binding seen in IgA nephropathy was also found in both adults and children with Henoch-Schönlein purpura with nephritis. However, the lectin binding of serum IgA1 from children with Henoch-Schönlein purpura lacking renal involvement did not differ from controls, and similarly, no abnormality of lectin binding was seen in patients with non-IgA associated glomerulonephritis. CONCLUSIONS: These data indicate that the abnormality of IgA1 O-glycosylation seen in IgA nephropathy is also found in Henoch-Schönlein purpura, but only in those subjects with renal involvement, while IgA1 O-glycosylation is normal in patients with other forms of renal disease. These findings lend strong support to a role for altered IgA1 O-glycosylation in the pathogenesis of IgA-associated glomerular disease.
    [Abstract] [Full Text] [Related] [New Search]