Integrin engagement mediates tyrosine dephosphorylation on platelet-endothelial cell adhesion molecule 1. Academic Article uri icon

Overview

abstract

  • Platelet-endothelial cell adhesion molecule 1 (PECAM-1, CD31) is a 130-kDa member of the immunoglobulin gene superfamily expressed on endothelial cells, platelets, neutrophils, and monocytes and plays a role during endothelial cell migration. Phosphoamino acid analysis and Western blot analysis with anti-phosphotyrosine antibody show that endothelial PECAM-1 is tyrosine-phosphorylated. Phosphorylation is decreased with endothelial cell migration on fibronectin and collagen and with cell spreading on fibronectin but not on plastic. Cell adhesion on anti-integrin antibodies is also able to specifically induce PECAM-1 dephosphorylation while concurrently inducing pp125 focal adhesion kinase phosphorylation. Inhibition of dephosphorylation with sodium orthovanadate suggests that this effect is at least partially mediated by phosphatase activity. Tyr-663 and Tyr-686 are identified as potential phosphorylation sites and mutated to phenylalanine. When expressed, both mutants show reduced PECAM-1 phosphorylation but Phe-686 mutants also show significant reversal of PECAM-1-mediated inhibition of cell migration and do not localize PECAM-1 to cell borders. Our results suggest that beta 1-integrin engagement can signal to dephosphorylate PECAM-1 and that this signaling pathway may play a role during endothelial cell migration.

publication date

  • October 15, 1996

Research

keywords

  • Endothelium, Vascular
  • Platelet Endothelial Cell Adhesion Molecule-1

Identity

PubMed Central ID

  • PMC38140

Scopus Document Identifier

  • 0029858914

Digital Object Identifier (DOI)

  • 10.1073/pnas.93.21.11808

PubMed ID

  • 8876219

Additional Document Info

volume

  • 93

issue

  • 21