© 1996 American Heart Association, Inc.
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Platelet Adhesion to Multimeric and Dimeric von Willebrand Factor and to Collagen Type III Preincubated With von Willebrand Factor
From the Department of Hematology, University Hospital, Utrecht, Netherlands, and the Division of Hematology-Oncology (R.J.W., R.I.H.), Department of Medicine, Brigham and Women's Hospital, Boston, Mass.
Correspondence to Dr J.J. Sixma, Department of Haematology, University Hospital Utrecht, PO Box 85500, 3508 GA Utrecht, Netherlands. E-mail jsixma@lab.azu.nl.
Abstract As part of a systematic study of platelet interaction with adhesive proteins under flow conditions, we studied platelet adhesion to multimeric and dimeric von Willebrand factor (vWF) coated to glass. vWF-dependent adhesion to collagen type III was studied for comparison. Adhesion to glass-coated vWF and vWF-mediated adhesion to collagen type III were in many respects similar. Both showed no decrease at increasing shear rates and a decline to 50% of maximum with a low-molecular-weight multimeric fraction. Adhesion to glass-coated vWF was partially inhibited by heparin and completely inhibited by prostaglandin I2 and anti–glycoprotein (GP) Ib and anti–GPIIb-IIIa antibodies. vWF-dependent adhesion to collagen was not inhibited by heparin, was partially inhibited by anti–GPIIb-IIIa, and was completely inhibited by prostaglandin I2 and anti-GPIb. Recombinant dimeric vWF was made by deletion of the propeptide and expression in Chinese hamster ovary cells. Adhesion was 50% of that with plasma vWF, and larger concentrations of dimeric vWF were required. Adhesion to dimeric vWF was optimal at 1500 s-1, with a gradual decrease at higher shear rates. We conclude that adhesion to collagen type III is strongly but not completely determined by the adhesive properties of vWF.
Key Words: von Willebrand factor • collagen type III • platelet • adhesion
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