免疫球蛋白A与去唾液酸糖蛋白受体的相互作用。
IgA interaction with the asialoglycoprotein receptor.
作者信息
Stockert R J, Kressner M S, Collins J C, Sternlieb I, Morell A G
出版信息
Proc Natl Acad Sci U S A. 1982 Oct;79(20):6229-31. doi: 10.1073/pnas.79.20.6229.
Abstract
IgA present in normal human serum reacts with the hepatic receptor specific for asialoglycoproteins as demonstrated by inhibition of receptor-mediated erythroagglutination. Inhibition is reversibly abolished by the oxidation of the galactose or N-acetylgalactosamine residues of IgA with galactose oxidase. The site of receptor recognition appears to be the O-glycosidically linked oligosaccharides present on the hinge region of the IgAI subtype of IgA. The demonstration of a specific binding, in vitro, of IgA by the hepatic receptor suggests that the uptake of polymeric IgA by the liver in vivo may be mediated by this reaction.
摘要
正常人体血清中的IgA可与去唾液酸糖蛋白的肝特异性受体发生反应，这一点可通过受体介导的红细胞凝集抑制实验得到证明。用半乳糖氧化酶氧化IgA的半乳糖或N-乙酰半乳糖胺残基后，抑制作用可被可逆性消除。受体识别位点似乎是IgA的IgA1亚型铰链区存在的O-糖苷键连接的寡糖。肝受体在体外对IgA的特异性结合表明，肝脏在体内对聚合IgA的摄取可能是由该反应介导的。
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