Kelemen J, Lacki J K, Müller W
Hochrheininstitut für Rehabilitationsforschung, Bad Säckingen, Németország.
Orv Hetil. 1997 Jun 15;138(24):1577-8.
Glycosylation is the main posttranslational modification of protein molecules. Human immunoglobulin G (IgG) is unique among serum glycoproteins because it is associated with at least 30 different biantennary oligosaccharide moieties. Elevated ratio of circulating IgG molecules lacking galactose from the oligosaccharides on the CH2 domain correlates with severity of the disease in a number of different autoimmune illnesses. Moreover, it may be helpful in differential diagnosis of rheumatoid arthritis (RA). By that we may try to predict outcome of RA. Its seems that agalactosyl IgG is distinctively connected with rheumatoid arthritis and may be involved in its immunopathogenesis.
糖基化是蛋白质分子主要的翻译后修饰。人免疫球蛋白G(IgG)在血清糖蛋白中独具特色,因为它与至少30种不同的双天线型寡糖部分相关联。循环中缺乏CH2结构域寡糖半乳糖的IgG分子比例升高,与多种不同自身免疫性疾病的病情严重程度相关。此外,它可能有助于类风湿关节炎(RA)的鉴别诊断。借此我们可以尝试预测RA的预后。似乎去半乳糖基IgG与类风湿关节炎有独特关联,可能参与其免疫发病机制。