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Cancer Immunology, Immunotherapy
Published in: Cancer Immunology, Immunotherapy 1/2006

01-01-2006 | Symposium Paper

Characterization of glycosylation and adherent properties of melanoma cell lines

Authors: Piotr Laidler, Anna Lityńska, Dorota Hoja-Łukowicz, Maria Łabędz, Małgorzata Przybyło, Dorota Ciołczyk-Wierzbicka, Ewa Pocheć, Ewa Trębacz, Elżbieta Kremser

Published in: Cancer Immunology, Immunotherapy | Issue 1/2006

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Abstract

The repertoire of oligosaccharide components of cellular glycoproteins significantly contributes to cell adhesion and communication. In tumor cells, alteration in cellular glycosylation may play a key role in giving rise to invasive and metastatic potential. Over 100 melanoma cell lines deposited in the ESTDAB Melanoma Cell Bank (Tubingen, Germany) were studied for the characteristic glycan composition related to tumor progression. Analysis of: (1) cell adhesion to extracellular matrix proteins—fibronectin, laminin, and collagen; (2) the expression of selected glycosyltransferases—α2,3(Galβ1,3)- and α2,3(Galβ1,4)-sialyltransferases, α1,2- and α1,3-fucosyltransferases, and N-acetylglucosaminyltransferase V; (3) characterization of N-glycans was carried out on uveal (4), primary cutaneous (6), and metastatic (96) melanoma cell lines. Results showed that uveal cells did not adhere to any of the substrates and, in general, possessed less glycans containing α-2,6- and α-2,3-linked sialic acid. The average number of polypeptides bearing β-1,6-branched tri- and tetra antennary glycans(characteristic of the metastatic phenotype)were similar in uveal, primary cutaneous, and metastatic melanoma cell lines. Characterization of N-glycans may open a new perspective in the search for specific glycoproteins that could become targets for the therapeutic modulation of melanoma.
Literature
1.
Aplin A, Howe A, Juliano RL (1999) Cell adhesion molecules, signal transduction and cell growth. Curr Option Cell Biol 11:737–744CrossRef
2.
Bani MR, Giavazzi R (2000) Invasion and metastasis. In: Bronchud MH, Foote MA, Peters WP, Robinson MO (eds) Principles of molecular oncology. Humana Press, Totawa, pp 298–320
3.
Bellis SL (2004) Variant glycosylation an underappreciated regulatory mechanism for β1 integrins. Biochim Biophys Acta 1663:52–60PubMedCrossRef
4.
Ciołczyk-Wierzbicka D, Gil D, Hoja-Łukowicz D, Lityńska A, Laidler P (2002) Carbohydrate moieties of N-cadherin from human melanoma cell lines. Acta Biochim Pol 4:991–998
5.
Ciołczyk-Wierzbicka D, Amoresano A, Casbarra A, Hoja-Łukowicz D, Lityńska A, Laidler P (2004) The structure of the oligosaccharides of N-cadherin from human melanoma cell lines. Glycoconjugate J 20:483–492CrossRef
6.
Chakraborty AK, Pawelek J, Ikeda Y, Miyoshi E, Kolesnikova N, Funasaka Y, Ichihashi M, Taniguchi N (2001) Fusion hybrids with macrophage and melanoma cells up-regulate N-acetylglucosaminyltransferase V, β 1-6 branching and metastasis. Cell Growth Differ 12:623–630PubMed
7.
Chandrasekaran EV, Chawda R, Locke RD, Piskorz CF, Matta KL (2002) Biosynthesis of the carbohydrate antigenic determinants, globo H, blood group H and Lewis b: a role for prostate cancer cell alpha 1,2-L-fucosyltransferase. Glycobiology 12:153–162CrossRefPubMed
8.
Dall’Olio F (1996) Protein glycosylation in cancer biology: an overview. J Clin Pathol 49:126M–135MCrossRef
9.
Demetriou M, Nabi I, Coppolino M, Dedhar S, Dennis JW (1995) Reduced contract-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-Transferase V. J Cell Biol 130:383–392CrossRefPubMed
10.
Dennis JW (1991) N-linked oligosaccharides processing and tumor cell biology. Cancer Biol 2:411–420
11.
Dennis JW, Granovsky M, Warren CE (1999) Glycoprotein glycosylation and cancer progression. Biochim Biophys Acta 1473:21–34PubMed
12.
Granovsky M, Fata J, Pawling J, Muller W, Khokha R, Dennis JW (2000) Suppression of tumor growth and metastasis in Mgat-5 deficient mice. Nat Med 6:306–312CrossRefPubMed
13.
Goupille C, Marionneau S, Bureau V, Hallouin F, Meichenin M, Rocher J, Le Pendu J (2000) α1,2 Fucosyltransferase increase resistance to apoptosis of rat colon carcinoma cells. Glycobiology 10:375–382CrossRefPubMed
14.
Gu J, Taniguchi N (2004) Regulation of integrin function by N-glycans. Glycoconjugate J 21:9–15CrossRef
15.
Hakomori S (1996) Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism. Cancer Res 56:5309–5318PubMed
16.
Hakomori S (2002) Glycosylation defining cancer malignancy: new wine in an old bottle. Proc Natl Acad Sci USA 99:10231–10233CrossRefPubMed
17.
Herlyn M, Berking C, Li G, Satyamoorthy K (2000) Lessons from melanocyte development for understanding the biological events in naevus and melanoma formation. Melanoma Res 10:303–312CrossRefPubMed
18.
Humphries MJ, Matsumoto K, White SL, Olden K (1986) Inhibition of experimental metastasis by castanospermine in mice: blockage of two distinct stages of tumor colonization by oligosacharide processing inhibitors. Cancer Res 46:5215–5222PubMed
19.
Kim YJ, Varki A (1997) Perspectives on the significance of altered glycosylation of glycoprotein in cancer. Glycoconjugate J 14:569–576CrossRef
20.
Kobata A (1992) Structures and functions of the sugar chains of glycoproteins. Eur J Biochem 209:483–501CrossRefPubMed
21.
Laemmli UK (1970) Cleavage of structural proteins during assembly of the head bacteriophage T4. Nature 227:680–685CrossRefPubMed
22.
Li G, Satyamoorthy K, Herlyn M (2001) N-cadherin-mediated intercellular interactions promote survival and migration of melanoma cells. Cancer Res 61:3819–3825PubMed
23.
Li G, Satyamoorthy K, Herlyn M (2002) Dynamic of cell interactions and communications during melanoma development. Crit Rev Oral Biol Med 13:62–70PubMedCrossRef
24.
Lityńska A, Przybyło M, Pocheć E, Hoja-Łukowicz D, Ciołczyk D, Laidler P (2001) Comparison of the lectin-binding pattern in different human melanoma cell lines. Melanoma Res 11:1–8CrossRefPubMed
25.
Marionneau S, Le Moullac-Vaidye B, Le Pendu J (2002) Expression of histo-blood group A antigen increase resistance to apoptosis and facilitates escape from immune control of rat colon carcinoma cells. Glycobiology 12:851–856CrossRefPubMed
26.
Nangia-Makker P, Conklin J, Hogan V, Raz A (2002) Carbohydrate-binding proteins in cancer, and their ligands as therapeutic agents. Trends Mol Med 8:187–192CrossRefPubMed
27.
Ochwat D, Hoja-Łukowicz D, Lityńska A (2004) N-glycoproteins bearing β1-6 branched oligosaccharides from the A375 human melanoma cell line analysed by tandem mass spectrometry. Melanoma Res 14:479–485CrossRefPubMed
28.
Orntoft TF, Vestergaard EM (1999) Clinical aspect of altered glycosylation of glycoproteins in cancer. Electrophoresis 20:362–371CrossRefPubMed
29.
Ozaki Y, Kontani K, Teramoto K, Fujita T, Tezuka N, Sawai S, Watanabe H, Fujino S, Asai T, Ohkubo I (2004) Identification of antigenic epitopes recognized by Mac-2 binding protein-specific cytotoxic T lymphocytes for use in cancer immunotherapy. Biochim Biophys Res Commun 317:1089–1095CrossRef
30.
Peterson GL (1977) A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem 83:346–356CrossRefPubMed
31.
Petretti T, Kemmner W, Schulze B, Schlag PM (2000) Altered mRNA expression of glycosyltransferases in human colorectal carcinomas and liver metastases. Gut 46:359–366CrossRefPubMed
32.
Pierce M, Buckhaults P, Chen L, Fregien N (1997) Regulation of N-acetylglucosaminyltransferase V and Asn-linked oligosaccharide β(1,6)-branching by a growth factor signalling pathway and effects on cell adhesion and metastatic potential. Glycoconjugate J 14:623–630CrossRef
33.
Pocheć E, Lityńska A, Amoresano A, Casbarra A (2003) Glycosylation profile of integrin α3β1 changes with melanoma progression. Biochim Biophys Acta 1644:113–123
34.
Sanders DS, Blessing K, Hassan GA, Bruton R, Marsden JR, Jankowski J (1999) Alterations in cadherin and catenin expression during the biological progression of melanocytic tumours. Mol Pathol 52:151–157PubMedCrossRef
35.
Yoshimura M, Ihara Y, Matsuzawa Y, Taniguchi N (1996) Aberrent glycosylation of E-cadherin enhanced cell-cell binding to suppress metastasis. J Biol Chem 271:13811–13815CrossRefPubMed
Metadata
Title
Characterization of glycosylation and adherent properties of melanoma cell lines
Authors
Piotr Laidler
Anna Lityńska
Dorota Hoja-Łukowicz
Maria Łabędz
Małgorzata Przybyło
Dorota Ciołczyk-Wierzbicka
Ewa Pocheć
Ewa Trębacz
Elżbieta Kremser
Publication date
01-01-2006
Publisher
Springer-Verlag
Published in
Cancer Immunology, Immunotherapy / Issue 1/2006
Print ISSN: 0340-7004
Electronic ISSN: 1432-0851
DOI
https://doi.org/10.1007/s00262-005-0019-4

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