The CD41/CD61 (GPIIb/IIIa) complex contributes to human neutrophil adhesiveness

Background Neutrophils can release pro-inflammatory cytokines and neutrophil extracellular traps (NETs), leading to vascular thrombosis. Neutrophil-platelet interaction, a major component of thrombosis, is more pronounced in inflammatory pathologies, such as heart failure (HF). Recently, the platelet receptor CD41/CD61 (GPIIb/IIIa), known for its role in platelet adhesion and aggregation via its binding to fibrinogen, was found on the membrane of neutrophils from lung cancer patients. Our objectives were to determine CD41/CD61 expression on neutrophils and its role in healthy volun-teers (HV) and acute decompensated heart failure patients (ADHF). Results Localization and expression of CD41/CD61 complex on isolated neutrophils were determined by flow cytometry and confocal microscopy. We assessed the CD41/CD61 role on neutrophil adhesion onto human extracellular matrix (hECM), NETosis and biomarkers release. CD41/CD61 complex was intracellularly expressed in 80–90% of neutrophils, but only between 8–13% on their extra-cellular membrane. The CD41/CD61 complex plays a role in neutrophil adhesion onto hECM, since its blockade by an anti-CD41 monoclonal antibody or its antagonist, eptifibatide, reduced IL-8 and PMA induced neutrophil adhesion from 52–100% in both HV and ADHF patients. Conclusions In summary, neutrophil specific CD41/CD61 expression contributes to neutrophil adhesiveness without affecting significantly cytokine release and NETosis in both HV and ADHF patients.