Histochemistry and Cell Biology

, Volume 126, Issue 4, pp 437–444

Binding of galectin-1 (gal-1) to the Thomsen–Friedenreich (TF) antigen on trophoblast cells and inhibition of proliferation of trophoblast tumor cells in vitro by gal-1 or an anti-TF antibody

  • Udo Jeschke
  • Uwe Karsten
  • Irmi Wiest
  • Sandra Schulze
  • Christina Kuhn
  • Klaus Friese
  • Hermann Walzel
Original Paper

DOI: 10.1007/s00418-006-0178-1

Cite this article as:
Jeschke, U., Karsten, U., Wiest, I. et al. Histochem Cell Biol (2006) 126: 437. doi:10.1007/s00418-006-0178-1

Abstract

Galectin-1 (gal-1), a member of the mammalian β-galactoside-binding proteins, recognizes preferentially Galβ1-4GlcNAc sequences of several cell surface oligosaccharides. We demonstrate histochemically that the lectin recognizes appropriate glycotopes on the syncytiotrophoblast and extravillous trophoblast layer from second trimester human placenta and on BeWo chorion carcinoma cells. Gal-1 binding to BeWo cells was diminished by the Thomsen–Friedreich (TF)-disaccharide (Galβ1-3GalNAc-) conjugated to polyacrylamide (TF–PAA). Gal-1 also inhibited BeWo cell proliferation in a concentration-dependent manner. Similar antiproliferative effects were also observed with an anti-TF monoclonal antibody (mAb, A78-G/A7). Therefore, we conclude that ligation of Galβ1-4GlcNAc and Galβ1-3GalNAc epitopes on BeWo cells may have regulatory effects on cell proliferation.

Keywords

Galectin-1Thomsen–FriedenreichImmunocytochemistryPlacentaBeWo cells

Copyright information

© Springer-Verlag 2006

Authors and Affiliations

  • Udo Jeschke
    • 1
  • Uwe Karsten
    • 2
  • Irmi Wiest
    • 1
  • Sandra Schulze
    • 1
  • Christina Kuhn
    • 1
  • Klaus Friese
    • 1
  • Hermann Walzel
    • 3
  1. 1.First Department of Obstetrics and GynaecologyLudwig Maximilians University of MunichMunichGermany
  2. 2.Max Delbrück Centre for Molecular MedicineBerlinGermany
  3. 3.Institute of Medical Biochemistry and Molecular BiologyUniversity of RostockRostockGermany