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.
Surgical Research Laboratory, Department of Surgery, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands. j.a.lisman@chir.umcg.nl
Ton
T
Lisman
Philip G
PG
de Groot
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