ArticleBiophysical journal2002
Selectin-like kinetics and biomechanics promote rapid platelet adhesion in flow: the GPIb(alpha)-vWF tether bond.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
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Who cites it
82 citing papers in PubMed, 180 citations in OpenAlex.
- The N-terminal flanking region of the A1 domain regulates the force-dependent binding of von Willebrand factor to platelet glycoprotein Ibα.The Journal of biological chemistry · 2013Trial
- Biomechanical anticoagulation by spherical platelets in extracorporeal systems.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Reversible formation of von-Willebrand-factor-platelet aggregates in microvascular blood flow.PNAS nexus · 2025Article
- Theory and Examples of Catch Bonds.The journal of physical chemistry. B · 2024Article
- A computational investigation of occlusive arterial thrombosis.Biomechanics and modeling in mechanobiology · 2024Article
- Molecular mechanisms of catch bonds and their implications for platelet hemostasis.Biophysical reviews · 2023Review
- Why platelet mechanotransduction matters for hemostasis and thrombosis.Journal of thrombosis and haemostasis : JTH · 2023Review
- A Computational Investigation of Occlusive Arterial Thrombosis.Research square · 2023Article
- Biomechanical activation of blood platelets via adhesion to von Willebrand factor studied with mesoscopic simulations.Biomechanics and modeling in mechanobiology · 2023Article
- A Multiscale Model for Shear-Mediated Platelet Adhesion Dynamics: Correlating In Silico with In Vitro Results.Annals of biomedical engineering · 2023Article
- Signaling mechanisms of the platelet glycoprotein Ib-IX complex.Platelets · 2022Review
- The N-terminal autoinhibitory module of the A1 domain in von Willebrand factor stabilizes the mechanosensor catch bond.RSC chemical biology · 2022Article
- In Vitro Measurements of Shear-Mediated Platelet Adhesion Kinematics as Analyzed through Machine Learning.Annals of biomedical engineering · 2021Article
- Article
- A Comparative Evaluation of an Automated Functional Assay for Von Willebrand Factor Activity in Type 1 Von Willebrand Disease.International journal of general medicine · 2021Article
- Clot Permeability, Agonist Transport, and Platelet Binding Kinetics in Arterial Thrombosis.Biophysical journal · 2020Article
- Dynamic catch-bonding generates the large stall forces of cytoplasmic dynein.Physical biology · 2020Article
- Biomechanical thrombosis: the dark side of force and dawn of mechano-medicine.Stroke and vascular neurology · 2020Review
- Force-Dependent Binding Constants.Biochemistry · 2019Review
- Stress phase angle regulates differentiation of human adipose-derived stem cells toward endothelial phenotype.Progress in biomaterials · 2018Article
22 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The ability of platelets to tether to and translocate on injured vascular endothelium relies on the interaction between the platelet glycoprotein receptor Ib alpha (GPIb(alpha)) and the A1 domain of von Willebrand factor (vWF-A1). To date, limited information exists on the kinetics that govern platelet interactions with vWF in hemodynamic flow. We now report that the GPIb(alpha)-vWF-A1 tether bond displays similar kinetic attributes as the selectins including: 1) the requirement for a critical level of hydrodynamic flow to initiate adhesion, 2) short-lived tethering events at sites of vascular injury in vivo, and 3) a fast intrinsic dissociation rate constant, k(0)(off) (3.45 +/- 0.37 s(-1)). Values for k(off), as determined by pause time analysis of transient capture/release events, were also found to vary exponentially (4.2 +/- 0.8 s(-1) to 7.3 +/- 0.4 s(-1)) as a function of the force applied to the bond (from 36 to 217 pN). The biological importance of rapid bond dissociation in platelet adhesion is demonstrated by kinetic characterization of the A1 domain mutation, I546V that is associated with type 2B von Willebrand disease (vWD), a bleeding disorder that is due to the spontaneous binding of plasma vWF to circulating platelets. This mutation resulted in a loss of the shear threshold phenomenon, a approximately sixfold reduction in k(off), but no significant alteration in the ability of the tether bond to resist shear-induced forces. Thus, flow dependent adhesion and rapid and force-dependent kinetic properties are the predominant features of the GPIb(alpha)-vWF-A1 tether bond that in part may explain the preferential binding of platelets to vWF at sites of vascular injury, the lack of spontaneous platelet aggregation in circulating blood, and a mechanism to limit thrombus formation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.