Cell surface carbohydrate differences were observed between two human cell lines initiated from primary melanoma and metastasis of the same patient. Although total sialic acid content was similar in both cell lines, neuraminidase-released sialic acid was twice as high in metastatic cells than that of primary cells. One class of Concanavalin A binding sites with similar affinity constant was found in untreated and neuraminidasetreated cells in both cell lines. Before surface sialic acid release, the primary cell line expressed two classes ofRicinus lectin binding sites with high and low affinity; the cell line of metastatic origin had only one class ofRicinus lectin binding sites with low affinity. After neuraminidase treatment, the number ofRicinus lectin binding sites with low affinity increased two- or three-fold in both cell lines, whereas the high-affinity binding sites were not observed in primary cells. The present data indicated that differences in surface sialic acid level modified theRicinus lectin binding in two human melanoma cell lines. However, the ability of the cells to bind Concanavalin A was not changed.
This is a preview of subscription content, log in to check access.
Buy single article
Instant access to the full article PDF.
Price includes VAT for USA
Subscribe to journal
Immediate online access to all issues from 2019. Subscription will auto renew annually.
This is the net price. Taxes to be calculated in checkout.
Van Beek W P, Smets L A, Emmelot P: Increased sialic acid density in surface glycoprotein of transformed and malignant cells. A general phenomenon?Cancer Res 33, 2913 (1973).
Hakomori S I: Structures and organization of cell surface glycolipids. Dependency on cell growth and malignant transformation.Biochim biophys Acta 417, 55 (1975).
Nicolson G L: Transmembrane control of the receptors on normal and tumor cells. II. Surface changes associated with transformation and malignancy.Biochim biophys Acta 458, 1 (1976).
Gahmberg C G: Membrane glycoproteins and glycolipids: structure, localization and function of the carbohydrate, in Funean J B and Michel R H (eds):Membrane Structure, New Comprehensive Biochemistry, vol. 1, pp. 127–160. Amsterdam, Elsevier (1981).
Warren L, Zeidman I, Buch C A: The surface glycoproteins of a mouse melanoma growing in culture and as a solid tumorin vivo.Cancer Res 35, 2186 (1975).
Yogeeswaren G, Stein B S, Sebastian H: Altered cell surface organisation of gangliosides and sialyglycoproteins of mouse metastatic melanoma variant lines selectedin vivo for enhanced lung implantation.Cancer Res 38, 1336 (1978).
Finne J, Tao T W, Burger M M: Carbohydrate changes in glycoproteins of a poorly metastasizing wheat germ agglutinin-resistant melanoma clone.Cancer Res 40, 2580 (1980).
Irimura T, Gonzales R, Nicolson G L: Effects of tunicamycin on B16 metastatic melanoma cell surface glycoproteins and blood-borne arrest and survival properties.Cancer Res 41, 3411 (1980).
Jumblatt J E, Tao T W, Schlup V, Finne J, Burger M M: Altered surface glycoproteins in melanoma cell variants with reduced metastasing capacity selected for resistance to wheat germ agglutinin.Biochem Biophys Res Commun 95, 111 (1980).
Raz A, McLellan W L, Hart I R, Bucana C D, Hoyer L C, Sela B A, Dragsten P, Fidler I J: Cell surface properties of B16 melarioma with differing metastatic potential.Cancer Res 40, 1645 (1980).
Roberts G P: Lactoperoxidase-catalysed iodination of surface proteins on human melanoma cells.Br J Cancer 38, 114 (1978).
Lloyd K O, Travassos L R, Takahashi T, Old L J: Cell surface glycoproteins of human tumor cell lines: unusual characteristics of malignant melanoma.J Natl Cancer Inst 63, 623 (1979).
Albino A P, Lloyd K O, Houghton A N, Oettgen H F, Old L J: Heterogeneity in surface antigen and glycoprotein expression of cell lines derived from different melanoma metastases of the same patient.J exp Med 154, 1764 (1981).
Romani N, Schuler G, Fritsch P: Identical lectin binding patterns of human melanocytes and melanoma cellsin vitro.J Invest Dermatol 80, 272 (1981).
Nicolson G L, Blaustein J: The interaction ofRicinus communis agglutinin with normal and tumor cell surfaces.Biochim biophys Acta 266, 543 (1972).
Goldstein I J, So L L: Protein-carbohydrate interaction. III. Agar gel-diffusion studies in the interaction of concanavalin A, a lectin isolated from jack bean, with polysaccharides.Arch Biochem Biophys 111, 407 (1965).
Aubert C, Rougé F, Galindo J R: Tumorigenicity of human malignant melanocytes in nude mice in relation to their differentiationin vitro.J Natl Cancer Inst 64, 1029 (1980).
Warren L: The thiobarbituric acid assay of sialic acids.J biol Chem 234, 1971 (1959).
Miller I R, Great H: Protein labeling by acetylation.Biopolymers 11, 2533 (1972).
Aubery M, Guillouzo A, Bernard B, Font J: Changes inRicinus communis lectin binding to the cell surface of human liver cells in culture.Exp Cell Res 129, 273 (1980).
Scatchard G: The attractions of proteins for small molecules and ions.Ann N Y Acad Sci 51, 660 (1949).
Zentz C, Frenoy J P, Bourrillon R: Interaction entre l'hémaglutinine de Ricin et ses ligands, galactose et lactose. Etude par microcalorimétrie et dialyse à l'équilibre.Biochimie 61, 1 (1979).
Levitzki A, Koshland D E Jr: Negative cooperativity in regulatory enzymes.Proc Natl Acad Sci USA 69, 1121 (1969).
Adair W L, Kornfel S: Isolation of the receptors for wheat germ agglutinin and theRicinus communis lectins from human erythrocytes using affinity chromatography.J biol Chem 249, 4696 (1974).
About this article
Cite this article
Reynier, M., Aubery, M., Lebec, S. et al. Differences in surface sialic acid and galactosyl residues of two autologous human melanoma cell lines. Med. Oncol. & Tumor Pharmacother. 1, 157–161 (1984). https://doi.org/10.1007/BF02934137
- Concanavalin A
- Ricinus lectin
- Sialic acid
- Human melanoma cell lines