Neutrophil P-selectin-glycoprotein-ligand-I binding to platelet P-selectin enhances metalloproteinase 2 secretion and platelet-neutrophil aggregation

Haissam Abou-Saleh, Jean François Théorêt, Daniel Yacoub, Yahye Merhi

Research output: Contribution to journalArticle

24 Citations (Scopus)


Platelets and neutrophils constitute a high source of metalloproteinases (MMPs), and their interactions via P-selectin and P-selectin-glycoprotein-ligand-1 (PSGL-1) are involved in thrombosis, vascular remodelling, and restenosis. We investigated the impact of these interactions on platelet MMP-2 secretion and function in platelet and neutrophil aggregation. The secretion of MMP-2 from human platelets was significantly increased three-fold after thrombin activation, and enhanced two-fold in the presence of neutrophils. Neutrophil supernatant had no effect on platelet MMP-2 secretion. While no MMP-2 was detected in the supernatant of neutrophils, a high amount of MMP-9 was released by neutrophils, and remained unchanged upon thrombin activation or in the presence of platelets. Platelet P-selectin, which increased significantly after activation, triggered platelet binding to neutrophils that was completely inhibited by P-selectin or PSGL-1 antagonists, and was reduced by 50% with a GPIIb/IIIa antagonist. P-selectin or PSGL-1 antagonism abolished the enhanced secretion of platelet MMP-2 in the presence of neutrophils and reduced platelet-neutrophil aggregation. Platelet activation and binding to neutrophils enhance the secretion of platelet MMP-2 via an adhesive interaction between P-selectin and PSGL-1, which contribute to increase platelet-neutrophil aggregation.

Original languageEnglish
Pages (from-to)1230-1235
Number of pages6
JournalThrombosis and Haemostasis
Issue number6
Publication statusPublished - Dec 2005
Externally publishedYes



  • Cell adhesion molecules
  • Leukocytes
  • Metalloproteinases
  • Platelets

ASJC Scopus subject areas

  • Hematology

Cite this