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2002 | 49 | 4 | 991-998
Article title

Carbohydrate moieties of N-cadherin from human melanoma cell lines.

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Expression of N-cadherin an adhesion molecule of the cadherin family, in tumor cells is associated with their increased invasive potential. Many studies suggested the role of N-linked oligosaccharides as important factors that contribute to metastasis by influencing tumor cell invasion and adhesion. N-cadherin is a heavily glycosylated protein. We have analysed the carbohydrate profile of this protein synthesized in human melanoma cell lines: WM35 from the primary tumor site and WM239, WM9, and A375 from different metastatic sites. N-cadherin was immunoprecipitated with anti-human N-cadherin polyclonal antibodies. Characterisation of its carbohydrate moieties was carried out by SDS/PAGE electrophoresis and blotting, followed by immunochemical identification of the N-cadherin polypeptides and analysis of their glycans using highly specific digoxigenin or biotin labelled lectins. The positive reaction of N-cadherin from the WM35 cell line with Galanthus nivalis agglutinin (GNA), Datura stramonium agglutinin (DSA) and Sambucus nigra agglutinin (SNA) indicated the presence of high-mannose type glycans and biantennary complex type oligosaccharides with α2-6 linked sialic acid. N-cadherin from WM239, WM9, and A375 cell lines gave a positive reaction with Phaseolus vulgaris leukoagglutinin (L-PHA) and lotus Tetragonolobus purpureas agglutinin (LTA). This indicated the presence of tri- or tetra-antennary complex type glycans with α-fucose. In addition, N-cadherin from WM9 (lymphomodus metastatic site) and A375 (solid tumor metastatic site) contained complex type chains with α2-3 sialic acid (positive reaction with Maackia amurensis agglutinin - MAA). The results demonstrated that N-glycans of N-cadherin are altered in metastatic melanomas in a way characteristic for invasive tumor cells.
Physical description
  • Institute of Medical Biochemistry, Medical College, Jagiellonian University, Kraków, Poland
  • Institute of Medical Biochemistry, Medical College, Jagiellonian University, Kraków, Poland
  • Institute of Zoology, Department of Animal Physiology, Jagiellonian University, Kraków, Poland
  • Institute of Zoology, Department of Animal Physiology, Jagiellonian University, Kraków, Poland
  • Institute of Medical Biochemistry, Medical College, Jagiellonian University, Kraków, Poland
  • Aplin AE, Howe AK, Juliano RL. (1999) Cell adhesion molecules, signal transduction and cell growth. Curr Opin Cell Biol.; 11: 737-44.
  • Bradford M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem.; 72: 248-54.
  • Bussemakers MJ, Van Bokhoven A, Tomita K, Jansen CF, Schalken JA. (2000) Complex cadherin expression in human prostate. Int J Cancer.; 85: 446-50.
  • Dall'Olio F. (1996) Protein glycosylation in cancer biology: an overview. J Clin Pathol.; 49: 126M-35M.
  • Dall'Olio F, Chiricolo M, Ceccarelli C, Minni F, Marrano D, Santini D. (2000) beta-Galactoside alpha2,6-sialyltransferase in human colon cancer: contribution of multiple transcripts to regulation of enzyme activity and reactivity with Sambucus nigra agglutinin. Int J Cancer.; 88: 58-65.
  • Datti A, Donovan R, Korczak B, Dennis JW. (2000) A homogeneous cell-based assay to identify N-liked carbohydrate processing inhibitors. Anal Biochem.; 280: 137-42.
  • Demetriou M, Nabi I, Coppolino M, Dedhar S, Denis J. (1995) Reduced contract-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V. J Cell Biol.; 130: 383-92.
  • Dennis JW, Granovsky M, Warren ChE. (1999) Glycoprotein glycosylation and cancer progression. Biochim Biophys Acta.; 1473: 21-34.
  • Dennis JW, Granovsky M, Warren ChE. (1999) Protein glycosylation in development and disease. BioEssays.; 21: 412-21.
  • Dimitroff Ch, Pera P, Dall'Olio F, Matta K, Chandrasekaran EV, Lau J, Bernacki R. (1999) Cell surface N-acetylneuraminic acid 2,3alpha-galactoside-dependent intercellular adhesion of human colon cancer cells. Biochem Biophys Res Commun.; 256: 631-6.
  • Dufour S, Beauvais-Jauneau A, Delouvee A, Thiery JP. (1999) Differential function of N-cadherin and cadherin-7 in the control of embryonic cells motility. J Cell Biol.; 146: 501-16.
  • Freemont AJ, Hoyland JA. (1996) Cell adhesion molecules. J Clin Pathol.; 49: 321M-30M.
  • Giard DJ, Aaronson SA, Todaro GJ, Amstein P, Kersey JH, Dosik H, Parks WP. (1973) In vitro cultivation of human tumors: establishment of cell lines derived from a series of solid tumors. J Natl Cancer Inst.; 51: 1417-23.
  • Hazan RB, Phillips GR, Qiao RF, Norton L, Aaronson SA. (2000) Exogenous expression of N-cadherin in breast cancer cell induces cell migration, invasion and metastasis. J Cell Biol.; 148: 779-90.
  • 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: 303-11.
  • Hirohashi S. (1998) Inactivation of the E-cadherin-mediated cell adhesion system in human cancers. Am J Pathol.; 153: 333-9.
  • Hsu MY, Wheelock MJ, Johnson KR, Herlyn M. (1996) Shifts in cadherin profiles between human normal melanocytes and melanomas. J Investig Dermatol Symp Proc.; 1: 188-94.
  • Hsu MY, Meier FE, Nesbit M, Hsu JY, Belle P, Elder DE, Herlyn M. (2000) E-cadherin expression in melanoma cells restores keratinocyte-mediated growth control and down-regulates expression of invasion-related adhesion receptors. Am J Pathol.; 156: 1515-25.
  • Johnson J. (1999) Cell adhesion molecules in the development and progression of malignant melanoma. Cancer Metastasis Rev.; 18: 345-57.
  • Laemmli UK. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature.; 227: 680-5.
  • Laidler P, Litynska A. (1997) Tumor cell N-glycans in metastasis. Acta Biochim Polon.; 44: 343-58.
  • Laidler P, Gil D, Pituch-Noworolska A, Ciolczyk D, Ksiazek D, Przybylo M, Litynska A. (2000) Expression of beta1-integrins and N-cadherin in bladder cancer and melanoma cell lines. Acta Biochim Polon.; 47: 1159-70.
  • Litynska A, Przybylo M, Pochea E, Hoja-Lukowicz D, Ciolczyk D, Laidler P, Gil D. (2001) Comparison of the lectin-binding pattern between different human melanoma cell lines. Melanoma Res.; 11: 205-12.
  • Menger MD, Vollmar B. (1996) Adhesion molecules as determinants of disease: from molecular biology to surgical research. Br J Surg.; 83: 588-601.
  • Nieman M, Prudoff R, Johnson K, Wheelock M. (1999) N-cadherin promotes motility in human breast cancer cells regardless of their E-cadherin expression. J Cell Biol.; 147: 631-43.
  • Petretti T, Kemmer W, Schulze W, Schlag PM. (2000) Altered mRNA expression of glycosyltransferases in human colorectal carcinomas and liver metastases. Gut.; 46: 359-66.
  • Pierce M, Buckhaults P, Chen L, Fregien N. (1997) Regulation of N-acetylglukosaminyltransferase V and Asn-linked oligosaccharide beta(1,6)-branching by a growth factor signaling pathway and effects on cell adhesion and metastatic potential. Glycoconj J.; 14: 623-30.
  • Pousset D, Piller V, Bureaud, Monsigny M, Piller F. (1997) Increased alpha2-6 sialylation of N-glycans in a transgenic mouse model of hepatocellular carcinoma. Cancer Res.; 57: 4249-56.
  • Prokopishyn N, Puzon-McLaughlin W, Takada Y, Laferte S. (1999) Integrin alpha3beta1 expressed by human colon cancer cells is a major carrier of oncodevelopmental carbohydrate epitopes. J Cell Biochem.; 72: 189-209.
  • 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: 151-7.
  • Tang A, Eller M, Hara M, Yaar M, Hirohashi S, Gilchrest B. (1994) E-cadherin is the major mediator of human melanocyte adhesion to keratinocytes in vitro. J Cell Sci.; 107: 983-92.
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