Galactose-deficient IgA1 in sera of IgA nephropathy patients is present in complexes with IgG.

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, Helix aspersa (HAA) and Caragana arborescens (CAA) and de-sialylated IgA1 with Helix pomatia (HPA) and Bauhinia purpurea (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 (P < 0.0001). Similar results were observed for 67 IgAN patients and 52 controls with second lectin, CAA (P < 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 IgA1 by reducing the rate of its elimination and catabolic degradation by the liver.

journal_name

Kidney Int

journal_title

Kidney international

authors

Tomana M,Matousovic K,Julian BA,Radl J,Konecny K,Mestecky J

doi

10.1038/ki.1997.361

subject

Has Abstract

pub_date

1997-08-01 00:00:00

pages

509-16

issue

2

eissn

0085-2538

issn

1523-1755

pii

S0085-2538(15)60201-0

journal_volume

52

pub_type

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