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- Title
Galactose-deficient IgA1 in sera of IgA nephropathy patients is present in complexes with IgG.
- Authors
Tomana, Milan; Matousovic, Karel; Julian, Bruce A.; Radl, Jiri; Konecny, Karel; Mestecky, Jiri
- Abstract
IgA1 proteins from sera of patients with IgA nephropathy (IgAN) are galactosylated to a lesser degree than those from healthy controls. The increased reactivity of intact or de-sialylated serum IgA1 with N-acetylgalactosamine (GalNAc)-specific lectins, <em>Helix aspersa</em> (HAA) and <em>Caragana arborescens</em> (CAA) and de-sialylated IgA1 with <em>Helix pomatia</em> (HPA) and <em>Bauhinia purpurea</em> (BPA) indicated that the Gal deficiency is in glycans located in the hinge region of IgA1 molecules. De-sialylated IgA from sera of 81 IgAN patients bound biotin-labeled lectin HAA more effectively than did de-sialylated IgA from 56 healthy controls (<em>P</em> < 0,0001). Similar results were observed for 67 IgAN patients and 52 controls with second lectin, CAA (<em>P</em> < 0.001). The binding patterns for 9 patients with mesangial proliferative glomerulonephritis of non-IgA origin were similar to those for controls. Incompletely galactosylated IgA1 capable of binding GalNAc-specific lectins was detected in complexes with IgG as demonstrated by ELISA, size-exclusion chromatography and sucrose gradient ultracentrifugation. The formation of IgA1-IgG complexes may affect the serum level of IgM by reducing the rate of its elimination and catabolic degradation by the liver.
- Subjects
KIDNEY diseases; HEMAGGLUTININ; ENZYME-linked immunosorbent assay; SERUM; LECTINS; BLOOD plasma
- Publication
Kidney International, 1997, Vol 52, Issue 2, p509
- ISSN
0085-2538
- Publication type
Article
- DOI
10.1038/ki.1997.361