The interaction of recombinant factor VIIa with platelet glycoprotein Ib.
Recombinant factor VIIa (rFVIIa) exerts potent prohemostatic activities via both tissue factor-dependent and -independent mechanisms. Tissue factor-independent enhancement of hemostasis involves a direct interaction of rFVIIa with the activated platelet membrane resulting in factor X activation. We have recently shown that rFVIIa binds to the platelet glycoprotein Ib/IX/V complex in addition to the negatively charged membrane surface. This interaction appears to slightly enhance tissue factor-independent thrombin generation. These findings add to our understanding of the mechanism of action of rFVIIa and may lead to improved therapeutic use of the drug.
Lisman
Ton
T
Surgical Research Laboratory, Department of Surgery, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands. j.a.lisman@chir.umcg.nl
de Groot
Philip G
PG
D001777:Blood Coagulation; D001792:Blood Platelets / Q000378:metabolism*; D015942:Factor VIIa / Q000737:chemistry*; D006801:Humans; D008954:Models, Biological; D010743:Phospholipids / Q000737:chemistry; D019038:Platelet Glycoprotein GPIb-IX Complex / Q000737:chemistry*; D011485:Protein Binding; D011486:Protein C / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry; D013917:Thrombin / Q000737:chemistry; D013925:Thromboplastin / Q000737:chemistry
D010743:Phospholipids; D019038:Platelet Glycoprotein GPIb-IX Complex; D011486:Protein C; D011994:Recombinant Proteins; D013925:Thromboplastin; C103587:recombinant FVIIa; D015942:Factor VIIa; D013917:Thrombin