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Prepublished online as a Blood First Edition Paper on May 8, 2003; DOI 10.1182/blood-2003-03-0717.
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Blood, 1 September 2003, Vol. 102, No. 5, pp. 1701-1707
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
The contribution of glycoprotein VI to stable platelet adhesion and thrombus formation illustrated by targeted gene deletion
Kazunobu Kato,
Taisuke Kanaji,
Susan Russell,
Thomas J. Kunicki,
Kenichi Furihata,
Sachiko Kanaji,
Patrizia Marchese,
Armin Reininger,
Zaverio M. Ruggeri, and
Jerry Ware
From the Roon Research Center for Arteriosclerosis and Thrombosis,
Division of Experimental Hemostasis and Thrombosis, Department of Molecular
and Experimental Medicine, The Scripps Research Institute, La Jolla, CA;
Department of Experimental Medicine Torrey Pines Institute for Molecular
Studies, San Diego, CA; and Department of Transfusion Medicine and
Hemostaseology, University of Munich, Munich, Germany.
Platelet interaction with exposed adhesive ligands at sites of vascular
injury is required to initiate a normal hemostatic response and may become a
pathogenic factor in arterial diseases leading to thrombosis. We report a
targeted disruption in a key receptor for collagen-induced platelet
activation, glycoprotein (GP) VI. The breeding of mice with heterozygous GP VI
alleles produced the expected frequency of wild-type, heterozygous, and
homozygous genotypes, indicating that these animals had no reproductive
problems and normal viability. GP VInull platelets failed to
aggregate in response to type I fibrillar collagen or convulxin, a snake venom
protein and known platelet agonist of GP VI. Nevertheless, tail bleeding time
measurements revealed no severe bleeding tendency as a consequence of GP VI
deficiency. Ex vivo platelet thrombus formation on type I collagen fibrils was
abolished using blood from either GP VInull or
FcR- null animals. Reflection interference contrast
microscopy revealed that the lack of thrombus formation by GP
VInull platelets could be linked to a defective platelet activation
following normal initial tethering to the surface, visualized as lack of
spreading and less stable adhesion. These results illustrate the role of GP VI
in postadhesion events leading to the development of platelet thrombi on
collagen fibrils.
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