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. Author manuscript; available in PMC: 2010 Feb 4.
Published in final edited form as: Thromb Haemost. 2009 Dec 18;103(2):291–298. doi: 10.1160/TH09-07-0420
1. What is known on this topic
  • VWF plays a role in arterial platelet-plug formation as an anchor to the thrombogenic surface, as well as a bridging molecule between platelets

  • in arterial thrombi only 50 % of fibrinogen is converted to fibrin

  • for dissolution of a platelet-plug a mixture of VWF-fibrinogen/fibrin has to be cleaved

  • both VWF and fibrin(ogen) are cleaved by plasmin in isolated systems, but kinetic data are available only for fibrin(ogen)


2. What this paper adds
  • VWF at its physiological concentration, protects fibrinogen, but not fibrin from its degradation by plasmin, miniplasmin, and microplasmin

  • while acting as a non-competitive inhibitor of plasmin with a Ki of 5.4 μg/ml, VWF itself is not necessarily degraded

  • the primary interaction between VWF and plasmin is mediated by the catalytic domain of plasmin, but not by its active site and is modulated by the kringle 5 domain

  • the presence of VWF in platelet-rich thrombi may contribute to their thrombolytic resistance, and plasma VWF may help to preserve circulating fibrinogen in the course of thrombolysis