Regulation of cellular adhesion to extracellular matrix proteins by galectin-3

Biochem Biophys Res Commun. 1998 May 29;246(3):788-91. doi: 10.1006/bbrc.1998.8708.


The control of cellular adhesion to extracellular matrix proteins is poorly understood. In the present analyses, we set out to test the hypothesis that high galectin-3 concentration on the cell surface downregulates cellular adhesion to the extracellular matrix proteins. Various tumor cell lines were briefly incubated without or with galectin-3 and then allowed to adhere to wells coated with laminin-1, collagen IV and fibronectin. Our data demonstrated that the cells which were incubated with galectin-3 prior to plating had significantly reduced adhesion to extracellular matrix proteins. This inhibition involved the carbohydrate recognition domain of the lectin because adhesion was achieved in the presence of galectin-3 and lactose but not galectin-3 and sucrose. Furthermore we demonstrated that galectin-3 associates with alpha 1 beta 1 integrin in a lactose dependent manner.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antigens, Differentiation / pharmacology*
  • Cell Adhesion / drug effects*
  • Collagen / metabolism
  • Dose-Response Relationship, Drug
  • Extracellular Matrix Proteins / metabolism*
  • Female
  • Fibronectins / metabolism
  • Galectin 3
  • Humans
  • Integrin alpha1beta1
  • Integrins / metabolism
  • Laminin / metabolism
  • Male
  • Mice
  • Protein Binding
  • Tumor Cells, Cultured


  • Antigens, Differentiation
  • Extracellular Matrix Proteins
  • Fibronectins
  • Galectin 3
  • Integrin alpha1beta1
  • Integrins
  • Laminin
  • Collagen