Are matrix - immoblized neoglycoproteins, plant and human lectins and carbohydrate- binding antibodies from human serum mediators of adhesion in vitro for carcinoma and lymphosarcoma cells?

Journal/Book: Anticancer Res. 15 (1), 169-174. 1995;

Abstract: Mediation of cell adhesion by defined molecules can be studied by theirimmobilization onto a nitrocellulose matrix and incubation with cells.In order to infer the capacity of deliberately selectedprotein-carbohydrate interactions to establish sugar-inhibitable celladhesion, a panel of immobilized neoglycoproteins was employed for themurine lymphosarcoma lines RAW-117 with low (P) and high (H10)metastatic capacity, a human mammary carcinoma line (DU4475) and threehuman colon carcinoma lines (C205, SW480, SW620). Exhibiting anotherwise rather similar behavior relative to the line with lowmetastatic potential, the murine line RAW117-H10 bound strongly to thematrix with carboxyl group-bearing N-acetylneuraminic acid andglucuronic acid as well as rhamnose. Whereas the analysis ofcarbohydrate-mediated adhesion yielded comparable results for the threecolon carcinoma lines, a markedly reduced number of adherent cells wascounted for matrix-attached alpha- and beta-galactosyl, alpha-mannosyland alpha-glucosyl moieties in the case of the mammary carcinoma line,raising evidence for cell lineage-dependent alterations of thisproperty. From the carbohydrate-binding proteins, the plant lectin,concanavalin A and Viscum album agglutinin almost invariably served wellas 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 immobilizedhuman beta-galactoside-binding lectin (Mr 14kDa) caused adhesion of themurine lines and one colon carcinoma line (SW480). Neither C-reactiveprotein under conditions that induce its activity as lectin nor serumamyloid P component nor a lactose-binding immunoglobulin G fraction fromhuman serum were reactive. However, cell adhesion to thealpha-galactoside-binding immunoglobulin G fraction of human serum wasseen with the murine line of low metastatic capacity and the mammarycarcinoma line. Cells of this line adhered also to the mannan-bindingprotein from human serum, supporting the view for its potential role inhost defence against aberrantly glycosylated tumor cells. Author.

Keyword(s): ADENOCARCINOMA

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