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Blood, 15 August 2001, Vol. 98, No. 4, pp. 1038-1046
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Platelet glycoprotein V binds to collagen and participates in
platelet adhesion and aggregation
Sylvie Moog,
Pierre Mangin,
Nadège Lenain,
Catherine Strassel,
Catherine Ravanat,
Simone Schuhler,
Monique Freund,
Martine Santer,
Mark Kahn,
Bernhard Nieswandt,
Christian Gachet,
Jean-Pierre Cazenave, and
François Lanza
From INSERM U.311, Etablissement Français du
Sang-Alsace, Strasbourg, France; University of Pennsylvania,
Philadelphia, PA; and Witten/Herdecke University, Klinikum Wuppertal,
Germany.
Glycoprotein V (GPV) is a subunit of the platelet GPIb-V-IX
receptor for von Willebrand factor and thrombin. GPV is cleaved from
the platelet surface during activation by thrombin, but its role in
hemostasis is still unknown. It is reported that GPV knockout mice had
a decreased tendency to form arterial occluding thrombi in an
intravital thrombosis model and abnormal platelet interaction with the
subendothelium. In vitro, GPV-deficient platelets exhibited defective
adhesion to a collagen type I-coated surface under flow or static
conditions. Aggregation studies demonstrated a decreased response of
the GPV-deficient platelets to collagen, reflected by an increased lag
phase and reduced amplitude of aggregation. Responses to adenosine
diphosphate, arachidonic acid, and the thromboxane analog U46619 were
normal but were enhanced to low thrombin concentrations. The defect of
GPV null platelets made them more sensitive to inhibition by the
anti-GPVI monoclonal antibody (mAb) JAQ1, and this was also the case in
aspirin- or apyrase-treated platelets. Moreover, an mAb (V.3) against
the extracellular domain of human GPV selectively inhibited
collagen-induced aggregation in human or rat platelets. V.3
injected in rats as a bolus decreased the ex vivo collagen aggregation
response without affecting the platelet count. Finally, surface plasmon
resonance studies demonstrated binding of recombinant soluble GPV on a
collagen-coupled matrix. In conclusion, GPV binds to collagen and
appears to be required for normal platelet responses to this agonist.
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