The unfolding tale of PECAM-1

FEBS Lett. 2003 Apr 10;540(1-3):7-14. doi: 10.1016/s0014-5793(03)00224-2.


Platelet endothelial cell adhesion molecule-1 (PECAM-1/CD31) is a member of the immunoglobulin (Ig) superfamily that has distinctive features of an immunoreceptor based upon its genomic structure and the presence of intrinsic immunoreceptor tyrosine inhibitory motifs (ITIMs) in its ligand binding polypeptide. This has lead to its subclassification into the Ig-ITIM superfamily. Its amino-terminal Ig-like domain of PECAM-1 is necessary for its homophilic binding, which plays an important role in cell-cell interactions. Its intracellular ITIMs serve as scaffolds for recruitment of signalling molecules including protein-tyrosine phosphatases to mediate its inhibitory co-receptor activity. Increasing evidence has implicated PECAM-1 in a plethora of biological phenomena, including modulation of integrin-mediated cell adhesion, transendothelial migration, angiogenesis, apoptosis, cell migration, negative regulation of immune cell signalling, autoimmunity, macrophage phagocytosis, IgE-mediated anaphylaxis and thrombosis. In this review, we discuss some of the new developments attributed to this molecule and its unique roles in biology.

Publication types

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

MeSH terms

  • Enzymes / metabolism
  • Humans
  • Ligands
  • Platelet Endothelial Cell Adhesion Molecule-1 / chemistry
  • Platelet Endothelial Cell Adhesion Molecule-1 / genetics
  • Platelet Endothelial Cell Adhesion Molecule-1 / metabolism
  • Platelet Endothelial Cell Adhesion Molecule-1 / physiology*
  • Protein Conformation
  • Protein Denaturation
  • Signal Transduction


  • Enzymes
  • Ligands
  • Platelet Endothelial Cell Adhesion Molecule-1