Identification of a glycoprotein ligand for E-selectin on mouse myeloid cells

J Cell Biol. 1993 Apr;121(2):449-59. doi: 10.1083/jcb.121.2.449.


E-selectin is an inducible endothelial cell adhesion molecule for neutrophils which functions as a Ca(2+)-dependent lectin. Using a recombinant, antibody-like form of mouse E-selectin, we have searched for glycoprotein ligands on mouse neutrophils and the neutrophil progenitor cell line 32D cl 3. We have identified a 150-kD glycoprotein as the only protein which could be affinity-isolated with soluble E-selectin from [35S]methionine/[35S]cysteine-labeled 32D cl 3 cells. Binding of this protein was strictly Ca(2+)-dependent, was blocked by a cell adhesion-blocking mAb against mouse E-selectin, and required the presence of sialic acid on the 150-kD ligand. This glycoprotein was also affinity-isolated from mature neutrophils, in addition to a minor component at 250 kD, but could not be isolated from several other non-myeloid cell lines. The 150-kD glycoprotein was the only protein from 32D cl 3 cells, which was detectable by silver-staining after a one-step affinity-isolation.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Antibodies / immunology
  • Binding Sites
  • Calcium / pharmacology
  • Cell Adhesion Molecules / immunology
  • Cell Adhesion Molecules / metabolism*
  • Cell Line / chemistry
  • E-Selectin
  • Glycoproteins / chemistry*
  • Glycoproteins / isolation & purification
  • Ligands*
  • Mice
  • Molecular Weight
  • N-Acetylneuraminic Acid
  • Neutrophils / metabolism*
  • Recombinant Fusion Proteins
  • Sialic Acids / analysis
  • Sialic Acids / metabolism
  • Tumor Cells, Cultured


  • Antibodies
  • Cell Adhesion Molecules
  • E-Selectin
  • Glycoproteins
  • Ligands
  • Recombinant Fusion Proteins
  • Sialic Acids
  • N-Acetylneuraminic Acid
  • Calcium