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- Title
TGF-β1 mimics the effect of IL-4 on the glycosylation of IgA1 by downregulating core 1 β1, 3-galactosyltransferase and Cosmc.
- Authors
Jun Xiao; Manting Wang; Dawei Xiong; Ying Wang; Qiuyue Li; Jing Zhou; Qinkai Chen
- Abstract
The aberrant glycosylation of IgA1 is pivotal in the pathogenesis of IgA nephropathy (IgAN). The aim of the present study was to investigate the effect of transforming growth factor-β1 (TGF-β1) on the glycosylation of IgA1 and the associated mechanism. The mRNA levels of core1 β1, 3-galactosyltransferase (C1GalT1) and its molecular chaperone, Cosmc, were analyzed, as was the subsequent O-glycosylation of IgA1, in a human B-cell line stimulated with TGF-β1. The IgA1-positive human B-cell line was cultured with different concentrations of recombinant human TGF-β1 (5, 10, 15 and 30 ng/ml). The production and glycosylation of IgA1 were assayed using sandwich ELISA and enzyme-linked lectin binding assays, respectively, and the mRNA levels of C1GalT1 and Cosmc were quantified using reverse transcription-quantitative polymerase chain reaction analysis. The results showed that the production of IgA1 was stimulated by low concentrations of TGF-β1 (5 or 10 ng/ml) and was suppressed by high concentrations (15 or 30 ng/ml). The terminal glycosylation of secreted IgA1 was altered in response to TGF-β1. TGF-β1 stimulation significantly decreased the mRNA levels of C1GalT1 and Cosmc. TGF-β1 may be key in controlling the glycosylation of IgA1, in part via the downregulation of C1GalT1 and Cosmc.
- Subjects
GLYCOSYLATION; IMMUNOGLOBULIN A; IGA glomerulonephritis; TRANSFORMING growth factors-beta; GALACTOSYLTRANSFERASES
- Publication
Molecular Medicine Reports, 2017, Vol 15, Issue 2, p969
- ISSN
1791-2997
- Publication type
Article
- DOI
10.3892/mmr.2016.6084