Dichotomy in the laminin-binding properties of soluble and membrane-bound human galactoside-binding protein

Biochem Biophys Res Commun. 1992 Aug 14;186(3):1674-80. doi: 10.1016/s0006-291x(05)81601-8.


Recent studies indicate that galactoside-binding proteins may bind the poly-N-acetyllactosamine sequences of laminin. We questioned whether human galactoside-binding protein (hL-31) binds to laminin and whether cells that express hL-31 on their surface use it as a laminin receptor to promote cellular attachment. The data show that both lectin and cells bind to immobilized laminin. The binding of soluble lectin to laminin is inhibited by lactose, while cell adhesion to it is not. The results indicate that laminin may be a ligand for soluble galactoside-binding proteins.

Publication types

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

MeSH terms

  • Binding Sites
  • Cell Adhesion
  • Cell Line
  • Cell Membrane / metabolism
  • Cytosol / metabolism
  • Fluorescent Antibody Technique
  • Galactosides / metabolism
  • Galectins
  • Hemagglutinins / analysis
  • Hemagglutinins / metabolism*
  • Humans
  • Immunoblotting
  • Kinetics
  • Laminin / analysis
  • Laminin / metabolism*


  • Galactosides
  • Galectins
  • Hemagglutinins
  • Laminin