Wawotzny R, André S, Dong X, Joshi S S, Gabius H J
Institut für Physiologische Chemie, Tierärztliche Fakultät, Ludwig-Maximilians-Universität, München, Germany.
Anticancer Res. 1995 Jan-Feb;15(1):169-74.
Mediation of cell adhesion by defined molecules can be studied by their immobilization onto a nitrocellulose matrix and incubation with cells. In order to infer the capacity of deliberately selected protein-carbohydrate interactions to establish sugar-inhibitable cell adhesion, a panel of immobilized neoglycoproteins was employed for the murine lymphosarcoma lines RAW-117 with low (P) and high (H10) metastatic capacity, a human mammary carcinoma line (DU4475) and three human colon carcinoma lines (C205, SW480, SW620). Exhibiting an otherwise rather similar behavior relative to the line with low metastatic potential, the murine line RAW117-H10 bound strongly to the matrix with carboxyl group-bearing N-acetylneuraminic acid and glucuronic acid as well as rhamnose. Whereas the analysis of carbohydrate-mediated adhesion yielded comparable results for the three colon carcinoma lines, a markedly reduced number of adherent cells was counted for matrix-attached alpha- and beta-galactosyl, alpha-mannosyl and alpha-glucosyl moieties in the case of the mammary carcinoma line, raising evidence for cell lineage-dependent alterations of this property. From the carbohydrate-binding proteins, the plant lectin, concanavalin A and Viscum album agglutinin almost invariably served well as cell adhesion molecules. Appropriate cell surface sugar receptors, probed with neoglycoproteins, and glycoconjugates, probed with lectins, thus can contribute to adhesion in this model system. The immobilized human beta-galactoside-binding lectin (Mr 14kDa) caused adhesion of the murine lines and one colon carcinoma line (SW480). Neither C-reactive protein under conditions that induce its activity as lectin nor serum amyloid P component nor a lactose-binding immunoglobulin G fraction from human serum were reactive. However, cell adhesion to the alpha-galactoside-binding immunoglobulin G fraction of human serum was seen with the murine line of low metastatic capacity and the mammary carcinoma line. Cells of this line adhered also to the mannan-binding protein from human serum, supporting the view for its potential role in host defence against aberrantly glycosylated tumor cells.
通过将特定分子固定在硝酸纤维素基质上并与细胞孵育，可以研究其对细胞黏附的介导作用。为了推断特意选择的蛋白质 - 碳水化合物相互作用建立糖抑制性细胞黏附的能力，一组固定化的新糖蛋白被用于具有低转移能力（P）和高转移能力（H10）的小鼠淋巴肉瘤细胞系RAW - 117、人乳腺癌细胞系（DU4475）以及三个人结肠癌细胞系（C205、SW480、SW620）。与低转移潜能的细胞系相比，表现出其他相当相似行为的小鼠细胞系RAW117 - H10与带有羧基的N - 乙酰神经氨酸、葡萄糖醛酸以及鼠李糖的基质强烈结合。虽然对碳水化合物介导的黏附分析在三个结肠癌细胞系中产生了可比的结果，但在乳腺癌细胞系的情况下，计数到附着在基质上的α - 和β - 半乳糖基、α - 甘露糖基和α - 葡萄糖基部分的黏附细胞数量明显减少，这为该特性的细胞谱系依赖性改变提供了证据。从碳水化合物结合蛋白来看，植物凝集素刀豆球蛋白A和欧洲槲寄生凝集素几乎总是作为良好的细胞黏附分子起作用。因此，用新糖蛋白探测的合适细胞表面糖受体以及用凝集素探测的糖缀合物可以在这个模型系统中促进黏附。固定化的人β - 半乳糖苷结合凝集素（Mr 14kDa）导致小鼠细胞系和一个结肠癌细胞系（SW480）黏附。在诱导其作为凝集素活性的条件下，C反应蛋白、血清淀粉样P成分以及人血清中的乳糖结合免疫球蛋白G组分均无反应。然而，低转移能力的小鼠细胞系和乳腺癌细胞系出现了对人血清α - 半乳糖苷结合免疫球蛋白G组分的细胞黏附。该细胞系的细胞也黏附于人血清中的甘露聚糖结合蛋白，支持了其在宿主抵御异常糖基化肿瘤细胞中的潜在作用的观点。
