Okada H, Tanaka H
Mol Immunol. 1983 Nov;20(11):1233-6. doi: 10.1016/0161-5890(83)90148-7.
Glycophorin, one of the major glycoproteins of erythrocytes (E), was extracted from human E (glycophorin-Hu) and guinea pig E (glycophorin-GP) and adsorbed to rabbit-E. The adsorption of glycophorin-Hu and glycophorin-GP to rabbit-E made the E resistant to hemolysis by human serum and guinea pig serum, respectively, via the alternative complement pathway (ACP). However, it did not make the rabbit-E resistant to hemolysis by serum heterologous to the glycophorin adsorbed. This species-specific inhibition by glycophorin of ACP activation should play a role in restricting ACP activation on self cell membranes. By recognizing the self-cell surface as the place where the complement reaction must be prevented, ACP will be able to accomplish the discrimination of non-self constituents without diversity of recognition sites for a variety of foreign substances.
血型糖蛋白是红细胞（E）的主要糖蛋白之一，从人红细胞（血型糖蛋白-Hu）和豚鼠红细胞（血型糖蛋白-GP）中提取，并吸附到兔红细胞上。血型糖蛋白-Hu和血型糖蛋白-GP吸附到兔红细胞上，分别通过替代补体途径（ACP）使红细胞对人血清和豚鼠血清的溶血具有抗性。然而，它并没有使兔红细胞对与吸附的血型糖蛋白异源的血清溶血具有抗性。血型糖蛋白对ACP激活的这种物种特异性抑制作用应在限制自身细胞膜上的ACP激活中发挥作用。通过将自身细胞表面识别为必须防止补体反应的部位，ACP将能够在没有针对多种外来物质的识别位点多样性的情况下完成对非自身成分的区分。
