Characterization of Thomsen-Friedenreich antibody subpopulations from normal human serum.
Characterization of Thomsen-Friedenreich antibody subpopulations from normal human serum.
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正常人血清中 Thomsen-Friedenreich 抗体亚群的表征。
DOI：
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发表时间：
1987
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通讯作者：
K. Schumacher
中科院分区：
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作者：
M. Wolf;U. Koerner;B. Klumpp;K. Schumacher
采用不同的富集方法从人血清中制备了Thomsen-Friedenreich （TF）抗体。这就产生了三种抗体制剂，它们都能凝集神经氨酸酶处理的红细胞。另一方面，三种抗体群体中的每一种都表现出不同的特异性模式。在血凝抑制实验中，asialfetuin、asialtransferrin、asialglycophorin和asialomucin均能抑制抗tf1抗体。这些糖蛋白的唾液化形式没有抑制作用。几种单糖或双糖都没有明显的抑制作用。这表明抗tf1识别通常被唾液酸隐藏的糖蛋白上的共同结构。抗tf2抗体对asialalfetuin、牛颌下黏液蛋白、asialomucin、asialglycophorin、二糖gal- β (1-3) n -乙酰半乳糖胺（galNAc）和nitrophenyl- β -半乳糖苷具有特异性。由于asialotransferrin或未结合的乳胺没有抑制作用，我们假设抑制剂的残留共同结构是(gal)- galac - o - ser /Thr，该结构大量存在于颌下粘蛋白中。抗tf3抗体被asialglycophorin抑制，而asialomucin和asialfetuin不受抑制。强糖抑制剂是半乳糖- β (1-3)galNAc，硝基- β -半乳糖，以及半乳糖。因此，抗tf2和抗tf3这两种抗体制剂都可以被gal- β -(1-3)galNAc抑制，但对双糖的一种或另一种糖组分表现出偏好，导致对糖缀合物抑制剂的差异识别。抗tf2和抗tf3似乎在蛋白质骨架的背景下识别碳水化合物，因为与神经酰胺骨架（GM1）连接的gal- β -(1-3)galNAc没有抑制作用。在三种人乳腺癌细胞系中，只有抗tf2识别的表位暴露在细胞表面。因此，我们得出结论，人血清中含有至少三个具有不同特异性的TF抗体亚群。只有抗tf2能检测出同样暴露在人乳腺癌细胞系上的隐性红细胞表位。
Thomsen-Friedenreich (TF) antibodies were prepared from human serum by different enrichment procedures. This resulted in three antibody preparations all of which agglutinated neuraminidase-treated erythrocytes. On the other hand, each of the three antibody populations showed a distinct specificity pattern. Anti-TF1 antibodies could be inhibited in the hemagglutination inhibition assay by asialofetuin, asialotransferrin, asialoglycophorin and asialomucin. The sialylated form of these glycoproteins showed no inhibition. No significant inhibition could be achieved with several mono- or disaccharides. This suggests that anti-TF1 recognizes common structures on glycoproteins normally hidden by sialic acid. Anti-TF2 antibodies showed specificity for asialofetuin, bovine submaxillary mucin, asialomucin, asialoglycophorin, the disaccharide gal-beta (1-3)N-acetyl-galactosamine (galNAc) and nitrophenyl-beta-galactoside. Because asialotransferrin or unbound lactosamine were not inhibitory, we suppose that the residual common structure of the inhibitors is (gal)-galNAc-O-Ser/Thr, which is present in high amounts in submaxillary mucin. Anti-TF3 antibodies were inhibited by asialoglycophorin but not by asialomucin or asialofetuin. Strong saccharide inhibitors were gal-beta (1-3)galNAc, nitrophenyl-beta-galactoside, as well as galactose. Therefore, both of the antibody preparations, anti-TF2 and anti-TF3, could be inhibited by gal-beta-(1-3)galNAc, but showed preference to one or the other sugar component of the disaccharide resulting in a differential recognition of glycoconjugate inhibitors. Anti-TF2 and anti-TF3 seem to recognize the carbohydrates in the context of a protein backbone, because gal-beta-(1-3)galNAc in connection with a ceramide backbone (GM1) was not inhibitory. When tested on three human breast cancer cell lines, only anti-TF2 recognized epitopes exposed on the cell surface. We, therefore, conclude that human serum contains at least three subpopulations of TF antibodies with distinct specificities. Only anti-TF2 can detect cryptic erythrocyte epitopes which are also exposed on human breast cancer cell lines.