High Shear Stress Attenuates Agonist-Induced, Glycoprotein IIb/IIIa-Mediated Platelet Aggregation When von Willebrand Factor Binding to Glycoprotein Ib/IX Is Blocked

1997 ◽  
Vol 233 (3) ◽  
pp. 796-800 ◽  
Author(s):  
Kaori Iijima ◽  
Mitsuru Murata ◽  
Kosei Nakamura ◽  
Tetsuya Kitaguchi ◽  
Makoto Handa ◽  
...  
Keyword(s):  
Shear Stress ◽  
Platelet Aggregation ◽  
Von Willebrand Factor ◽  
High Shear ◽  
High Shear Stress ◽  
Glycoprotein Ib ◽  
Factor Binding ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Total inhibition of high shear stress induced platelet aggregation by homodimeric von Willebrand factor A1-loop fragments

1999 ◽  
Vol 105 (4) ◽  
pp. 1092-1100 ◽  
Author(s):  
Shuji Miura ◽  
Yoshihiko Sakurai ◽  
Hideo Takatsuka ◽  
Akira Yoshioka ◽  
Masanori Matsumoto ◽  
...  
Keyword(s):  
Shear Stress ◽  
Platelet Aggregation ◽  
Von Willebrand Factor ◽  
High Shear ◽  
High Shear Stress ◽  
Total Inhibition ◽  
Von Willebrand ◽  
Willebrand Factor

von Willebrand Factor Ristocetin Cofactor Activity Correlates with Platelet Function in a High Shear Stress System

2000 ◽  
Vol 84 (10) ◽  
pp. 727-728 ◽  
Author(s):  
Agnès Veyradier ◽  
Edith Fressinaud ◽  
Catherine Boyer-Neumann ◽  
Marc Trossaert ◽  
Dominique Meyer
Keyword(s):  
Shear Stress ◽  
Von Willebrand Factor ◽  
Stress System ◽  
High Shear ◽  
High Shear Stress ◽  
Cofactor Activity ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Ristocetin Cofactor ◽  
Ristocetin Cofactor Activity

scholarly journals Platelet adhesion involves a novel interaction between vimentin and von Willebrand factor under high shear stress

Blood ◽  
2014 ◽  
Vol 123 (17) ◽  
pp. 2715-2721 ◽  
Author(s):  
Qi Da ◽  
Molly Behymer ◽  
Juliana I. Correa ◽  
K. Vinod Vijayan ◽  
Miguel A. Cruz
Keyword(s):  
Shear Stress ◽  
Von Willebrand Factor ◽  
Platelet Adhesion ◽  
High Shear ◽  
High Shear Stress ◽  
Platelet Surface ◽  
Key Points ◽  
Von Willebrand ◽  
Willebrand Factor

Key Points Vimentin expressed on the platelet surface serves as adhesive receptor for VWF.

Direct demonstration of radiolabeled von willebrand factor binding to platelet glycoprotein Ib and IIb-IIIa in the presence of shear stress

1995 ◽  
Vol 23 (6) ◽  
pp. 787-793 ◽  
Author(s):  
Jeffrey K. McCrary ◽  
Leticia H. Nolasco ◽  
J. David Hellums ◽  
Michael H. Kroll ◽  
Nancy A. Turner ◽  
...  
Keyword(s):  
Shear Stress ◽  
Von Willebrand Factor ◽  
Platelet Glycoprotein ◽  
Glycoprotein Ib ◽  
Factor Binding ◽  
Direct Demonstration ◽  
Von Willebrand ◽  
Willebrand Factor

High Shear Stress and Immobilization of Von Willebrand Factor Promotes the VWF-Cleaving Protease Activity as Assessed by the Cone and Plate(let) Analyzer.

Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 849-849
Author(s):  
David Varon ◽  
Boris Shenkman ◽  
Ulrich Budde ◽  
Dorothea Angerhaus ◽  
Reinhard Schneppenheim ◽  
...  
Keyword(s):  
Shear Stress ◽  
Von Willebrand Factor ◽  
Platelet Adhesion ◽  
Thrombus Formation ◽  
Static Condition ◽  
High Shear ◽  
High Shear Stress ◽  
Polystyrene Surface ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract The metalloprotease ADAMTS-13 cleaves von Willebrand factor (VWF) that is released from endothelial cells as a large multimeric protein. However, the specific physiological conditions required for the function of this von Willebrand factor-cleaving protease (VWF-CP) are not yet established. In this study we determined the optimal conditions for the VWF-CP activity using the Cone and Plate(let) Analyzer (CPA). Proteolysis of a soluble recombinant VWF by a recombinant VWF-CP in the absence or the presence of BaCl2 (for induction of VWF-CP) was performed under static and flow (2050 s−1) conditions. The resulted fragments of the soluble VWF were immobilized on a polystyrene surface and non-adhering sites were blocked with 1% BSA. In parallel, polystyrene surface immobilized VWF was similarly treated by VWF-CP. The immobilized cleaved VWF fragments by the above protocols served as a substrate for citrated whole blood platelet adhesion under flow (2050 s−1). Reduction of platelet adhesion (surface coverage, SC) in BaCl2 treated compared to untrerated sample reflects the degree of VWF-CP activity. Platelet adhesion (SC, %) to VWF proteolytic products generated under the indicated conditions: Static w/o BaCl2 Static + BaCl2 Flow w/o BaCl2 Flow + BaCl2 Soluble VWF 15.0 ± 3.4 11.1 ± 2.7 13.6 ± 2.2 8.0 ± 2.1 Immobil. VWF 19.1 ± 3.0 12.0 ± 4.1 6.5 ± 1.1 1.0 ± 0.6 Maximal VWF-CP activity as reflected by maximal reduction (85%) of platelet adhesion was observed when immobilized VWF was treated by VWF-CP under flow. Minimal effect of VWF-CP activity was observed when soluble VWF was treated under static condition (26% reduction). Intermediate effect was observed with soluble VWF under flow (41%) and with immobilized VWF under static condition (37%). It should be noted that in the case of immobilized VWF application of flow alone (without BaCl2) was sufficient to induce a remarkable decrease of platelet adhesion (66%). In conclusion, both immobilization of VWF and high shear stress are important conditions for VWF-CP function, suggesting that stretching of immobilized VWF under flow exposes the VWF-cleavage site and thereby may serve as a control mechanism of platelet adhesion at the site of thrombus formation.

Sign in / Sign up

Export Citation Format

Share Document