Schlepper-Schäfer J, Kolb-Bachofen V, Kolb H
Biochem J. 1980 Mar 15;186(3):827-31. doi: 10.1042/bj1860827.
Kupffer cells isolated from the rat liver are able to bind neuraminidase-treated rat erythrocytes via a D-galactose-specific receptor on the cell surface. Binding of desialylated erythrocytes was inhibited by several mono- and oligo-saccharides related to D-galactose, but not by unrelated sugars. However, after phosphorylation at position 6 D-glucose was as good an inhibitor as D-galactose. Two synthetic glycoproteins, D-galactosyl-albumin and, at a higher concentration, D-glucosyl-albumin, strongly inhibit cell contacts. Lectin-mediated binding of desialylated erythrocytes is dependent on the presence of Ca2'ons, but independent of ATP formation and cell motility. It is concluded that binding of desialylated erythrocytes by rat Kupffer cells is mediated by a Ca2-dependent D-galactosyl/D-glucosyl-recognition system.
从大鼠肝脏分离出的库普弗细胞能够通过细胞表面的D-半乳糖特异性受体结合经神经氨酸酶处理的大鼠红细胞。去唾液酸红细胞的结合受到几种与D-半乳糖相关的单糖和寡糖的抑制，但不受无关糖类的抑制。然而，6位磷酸化后的D-葡萄糖与D-半乳糖一样是良好的抑制剂。两种合成糖蛋白，D-半乳糖基白蛋白以及在较高浓度下的D-葡萄糖基白蛋白，强烈抑制细胞接触。凝集素介导的去唾液酸红细胞结合依赖于Ca2+离子的存在，但与ATP形成和细胞运动无关。得出的结论是，大鼠库普弗细胞对去唾液酸红细胞的结合是由Ca2+依赖性D-半乳糖基/D-葡萄糖基识别系统介导的。
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