Abnormal IgA glycosylation in Henoch-Schönlein purpura restricted to patients with clinical nephritis
Autor: | F R Willis, A C Allen, T J Beattie, John Feehally |
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Rok vydání: | 1998 |
Předmět: |
Immunoglobulin A
Adult Male Henoch-Schonlein purpura Glycosylation Adolescent IgA Vasculitis Molecular Sequence Data chemical and pharmacologic phenomena Nephropathy fluids and secretions stomatognathic system immune system diseases hemic and lymphatic diseases Lectins medicine Humans Amino Acid Sequence Child Aged Transplantation Kidney biology business.industry Glomerulonephritis Glomerulonephritis IGA Middle Aged medicine.disease Purpura medicine.anatomical_structure Nephrology Child Preschool Immunology biology.protein Female medicine.symptom Plant Lectins business Nephritis Kidney disease |
Zdroj: | Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association. 13(4) |
ISSN: | 0931-0509 |
Popis: | Background. Glomerular deposition of IgA1 is a common feature of Henoch-Schonlein 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 Methods. To investigate whether IgA1 is abnormally glycosylated in Henoch-Schonlein purpura, the binding of Vicia villosa lectin to serum IgA1 was studied in the following subject groups: IgA nephropathy; adults and children with Henoch-Schonlein purpura and nephritis; children with clinically diagnosed Henoch-Schonlein 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-Schonlein purpura with nephritis. However, the lectin binding of serum IgA1 from children with Henoch-Schonlein 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-Schonlein 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. |
Databáze: | OpenAIRE |
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