Structure and function of the selectin ligand PSGL-1

Braz J Med Biol Res. 1999 May;32(5):519-28. doi: 10.1590/s0100-879x1999000500004.

Abstract

P-selectin glycoprotein ligand-1 (PSGL-1) is a dimeric mucin-like 120-kDa glycoprotein on leukocyte surfaces that binds to P- and L-selectin and promotes cell adhesion in the inflammatory response. The extreme amino terminal extracellular domain of PSGL-1 is critical for these interactions, based on site-directed mutagenesis, blocking monoclonal antibodies, and biochemical analyses. The current hypothesis is that for high affinity interactions with P-selectin, PSGL-1 must contain O-glycans with a core-2 branched motif containing the sialyl Lewis x antigen (NeuAc alpha 2-->3Gal beta 1-->4[Fuc alpha 1-->3]GlcNAc beta 1-->R). In addition, high affinity interactions require the co-expression of tyrosine sulfate on tyrosine residues near the critical O-glycan structure. This review addresses the biochemical evidence for this hypothesis and the evidence that PSGL-1 is an important in vivo ligand for cell adhesion.

Publication types

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

MeSH terms

  • Arteriosclerosis / metabolism
  • Cell Adhesion
  • E-Selectin
  • Humans
  • Lectins
  • Ligands*
  • Membrane Glycoproteins / physiology*
  • Neutrophils
  • Structure-Activity Relationship
  • Tyrosine

Substances

  • E-Selectin
  • Lectins
  • Ligands
  • Membrane Glycoproteins
  • P-selectin ligand protein
  • Tyrosine