Breast Cancer Research and Treatment

, Volume 90, Issue 1, pp 77–84

Stable expression of sialyl-Tn antigen in T47-D cells induces a decrease of cell adhesion and an increase of cell migration

  • Sylvain Julien
  • Chann Lagadec
  • Marie-Ange Krzewinski-Recchi
  • Gilles Courtand
  • Xuefen Le Bourhis
  • Philippe Delannoy
Report

DOI: 10.1007/s10549-004-3137-3

Cite this article as:
Julien, S., Lagadec, C., Krzewinski-Recchi, MA. et al. Breast Cancer Res Treat (2005) 90: 77. doi:10.1007/s10549-004-3137-3
  • 256 Downloads

Summary

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 α2,6-sialyltransferase: ST6GalNAc I, which catalyzes the transfer of a sialic acid residue in α2,6-linkage to the GalNAcα1-O-Ser/Thr structure. The resulting disaccharide (Neu5Acα2-6GalNAcα1-O-Ser/Thr) cannot be further elongated and sialyl-Tn expression results therefore in a shortening of the O-glycan chains. However, usual breast cancer cell lines express neither ST6GalNAc I nor sialyl-Tn antigen. We have previously shown that stable transfection of MDA-MB-231 cells with the hST6GalNAc I cDNA induces the sialyl-Tn antigen expression at the cell surface and leads to a decreased cell growth and an increased cell migration. We describe herein the generation of new T47-D clones expressing sialyl-Tn antigen after hST6GalNAc I cDNA stable transfection. sialyl-Tn antigen is carried by several high molecular weight membrane bound O-glycoproteins, including MUC1. We show that sialyl-Tn expression induces a decrease of cell growth and adhesion, and an increase of cell migration in sialyl-Tn positive clones compared to mock transfected cells. These observations show that the alteration of the O-glycans pattern is sufficient to modify the biological features of cancer cells. These T47-D sialyl-Tn expressing clones might allow further in vivo investigation to determine precisely the impact of such O-glycosylation modifications on breast cancer development.

Keywords

adhesion breast cancer migration O-glycosylation sialyl-Tn ST6GalNAc I 

Abbreviations

Core1β3GalT

UDP-Gal

GalNAc β1,3

galactosyltransferase (EC 2.4.1.122)

ECM

extracellular matrix

mAb

monoclonal antibody

NBT

nitroblue tetrazolium

ST6GalNAc I

CMP-Neu5Ac

R-GalNAcα1

O-Ser/Thr α2,6-sialyltransferase (EC 2.4.99.3)

STn

sialyl-Tn antigen

Tn antigen

Thomsen-nouveau antigen

Copyright information

© Springer 2005

Authors and Affiliations

  • Sylvain Julien
    • 1
  • Chann Lagadec
    • 2
  • Marie-Ange Krzewinski-Recchi
    • 1
  • Gilles Courtand
    • 3
  • Xuefen Le Bourhis
    • 2
  • Philippe Delannoy
    • 1
    • 4
  1. 1.Unité de Glycobiologie Structurale et FonctionnelleUMR CNRS no. 8576, GDR CNRS no. 2590France
  2. 2.Laboratoire de Biologie du DéveloppementINSERM ESPRIFrance
  3. 3.Centre Commun de Mesures Imagerie CellulaireUniversité des Sciences et Technologies de LilleVilleneuve d’AscqFrance
  4. 4.Unité de Glycobiologie Structurale et Fonctionnelle, Laboratoire de Chimie BiologiqueUniversité des Sciences et Technologies de LilleVilleneuve d’AscqFrance

Personalised recommendations