Thrombosis Research
Volume 125, Supplement 1 , Pages S13-S15, April 2010

The interaction of recombinant factor VIIa with platelet glycoprotein Ib

  • Ton Lisman

      Affiliations

    • Surgical Research Laboratory, Department of Surgery, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands
    • Corresponding Author InformationCorresponding author. Surgical Research Laboratory, BA 44, University Medical Center Groningen, Hanzeplein 1, 9713GZ Groningen, The Netherlands. Tel.: +31 50 3619028; fax: +31 50 363 2796.
    • ,
  • Philip G. de Groot

      Affiliations

    • Department of Clinical Chemistry and Haematology, University Medical Center Utrecht, Utrecht, The Netherlands

published online 22 February 2010.

Abstract 

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.

Abbreviations: rFVIIa, recombinant factor VIIa, gla, gamma carboxyglutamic acid, GPIbα, glycoprotein Ibα, VWF, von Willebrand factor

Keywords: Platelet, Coagulation, Recombinant factor VIIa, Glycoprotein Ib, Thrombin

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PII: S0049-3848(10)00077-0

doi:10.1016/j.thromres.2010.01.024

Thrombosis Research
Volume 125, Supplement 1 , Pages S13-S15, April 2010

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