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IgA肾病中IgA1分子铰链区O 连接糖基半乳糖基化的水平降低 ,该糖基化异常可通过多种途径引起IgA1分子在肾小球的沉积和肾小球的炎性损伤。B细胞内β1、3半乳糖基转移酶活性的缺乏可能是IgA1分子异常糖基化的原因。对该糖基化异常的深入研究将有利于进一步阐明IgA肾病的发病机制并有望对IgA肾病的治疗提供新的思路。
In IgA nephropathy, the level of O-linked glycosylgalactosylation in the hinge region of IgA1 is decreased. Abnormal glycosylation may induce the deposition of IgA1 in glomeruli and the glomerular inflammatory injury through a variety of pathways. The lack of β1,3 galactosyltransferase activity in B cells may be responsible for the abnormal glycosylation of IgA1 molecules. In-depth study of this abnormal glycosylation will help further elucidate the pathogenesis of IgA nephropathy and is expected to provide new ideas for the treatment of IgA nephropathy.