IgA interaction with the asialoglycoprotein receptor.
IgA interaction with the asialoglycoprotein receptor.
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DOI：
10.1073/pnas.79.20.6229
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发表时间：
1982-10
影响因子：
11.1
通讯作者：
R. Stockert;M. Kressner;J. Collins;I. Sternlieb;A. Morell
中科院分区：
文献类型：
--
作者：
R. Stockert;M. Kressner;J. Collins;I. Sternlieb;A. Morell
正常人血清中存在的免疫球蛋白与去唾液酸糖蛋白的肝脏受体发生反应，这表现为对受体介导的红细胞凝集的抑制。通过用半乳糖氧化酶氧化IgA的半乳糖或N-乙酰半乳糖胺残基，可逆地取消抑制作用。受体识别的部位似乎是存在于IgAI亚型IgA铰链区的O-糖基连接的寡糖。在体外，肝脏受体对IgA的特异性结合表明，体内肝脏对聚合的IgA的摄取可能是由这一反应介导的。
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.