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Blood, 1 October 2000, Vol. 96, No. 7, pp. 2469-2478
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
The GPIb thrombin-binding site is essential for
thrombin-induced platelet procoagulant activity
Dagmar Dörmann,
Kenneth J. Clemetson, and
Beate
E. Kehrel
From the Klinik und Poliklinik für
Anästhesiologie und operative Intensivmedizin, Experimental and
Clinical Haemostasis, University of Münster, Germany; Theodor
Kocher Institute, University of Berne, Switzerland.
The role of the platelet glycoprotein (GP) Ib-V-IX receptor in
thrombin activation of platelets has remained controversial although
good evidence suggests that blocking this receptor affects platelet
responses to this agonist. The mechanism of expression of procoagulant
activity in response to platelet agonists is also still obscure. Here,
the binding site for thrombin on GPIb is shown to have a key role in
the exposure of negatively charged phospholipids on the platelet
surface and thrombin generation, in response to thrombin, which also
requires protease-activated receptor-1, GPIIb-IIIa, and
platelet-platelet contact. Von Willebrand factor binding to GPIb is not
essential to initiate development of platelet procoagulant activity.
Inhibition of fibrinogen binding to GPIIb-IIIa also failed to block
platelet procoagulant activity. Both heparin and low molecular weight
heparin block thrombin-induced platelet procoagulant activity,
which may account for part of their clinical efficacy. This study
demonstrates a new, critical role for platelet GPIb in hemostasis,
showing that platelet activation and coagulation are tightly
interwoven, which may have implications for alternative therapies for
thrombotic diseases.
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