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Glycobiology Advance Access originally published online on August 31, 2005
Glycobiology 2006 16(1):54-64; doi:10.1093/glycob/cwj033
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org

ST6GalNAc I expression in MDA-MB-231 breast cancer cells greatly modifies their O-glycosylation pattern and enhances their tumourigenicity

S. Julien2, E. Adriaenssens3, K. Ottenberg4, A. Furlan3, G. Courtand5, A.-S. Vercoutter-Edouart2, F.-G. Hanisch4, P. Delannoy1,2 and X. Le Bourhis3

2 Unité de Glycobiologie Structurale et Fonctionnelle, UMR CNRS n° 8576, GDR CNRS n° 2590, Université des Sciences et Technologies de Lille, F-59655 Villeneuve d’Ascq, France; 3 Laboratoire de Biologie du Développement, INSERM ERI8, UPRES EA 1033, Université des Sciences et Technologies de Lille, F-59655 Villeneuve d’Ascq, France; 4 Center of Biochemistry and Center for Molecular Medicine Cologne, University of Cologne, Joseph-Stelzmann-Street 52, D-50931 Cologne, Germany; and 5 Centre Commun de Mesures Imagerie Cellulaire, Université des Sciences et Technologies de Lille, F-59655 Villeneuve d’Ascq, France

1 To whom correspondence should be addressed; e-mail: philippe.delannoy{at}univ-lille1.fr

Received on July 6, 2005; revised on August 23, 2005; accepted on August 24, 2005

Sialyl-Tn is a carbohydrate antigen overexpressed in several epithelial cancers, including breast cancer, and usually associated with poor prognosis. Sialyl-Tn is synthesized by a CMP-Neu5Ac:GalNAc{alpha}2,6-sialyltransferase: CMP-Neu5Ac: R-GalNAc{alpha}1-O-Ser/Thr {alpha}2,6-sialyltransferase (EC 2.4.99.3 [EC] ) (ST6GalNAc I), which transfers a sialic acid residue in {alpha}2,6-linkage to the GalNAc{alpha}1-O-Ser/Thr structure. However, established breast cancer cell lines express neither ST6GalNAc I nor sialyl-Tn. We have previously shown that stable transfection of MDA-MB-231, a human breast cancer cell line, with ST6GalNAc I cDNA induces sialyl-Tn antigen (STn) expression. We report here the modifications of the O-glycosylation pattern of a MUC1-related recombinant protein secreted by MDA-MB-231 sialyl-Tn positive cells. We also show that sialyl-Tn expression and concomitant changes in the overall O-glycan profiles induce a decrease of adhesion and an increase of migration of MDA-MB-231. Moreover, STn positive clones exhibit an increased tumour growth in severe combined immunodeficiency (SCID) mice. These observations suggest that modification of the O-glycosylation pattern induced by ST6GalNAc I expression are sufficient to enhance the tumourigenicity of MDA-MB-231 breast cancer cells.

Key words: breast cancer / cell adhesion / sialyl-Tn / ST6GalNAc I / tumour growth


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