ArticleThe Journal of biological chemistry2014
Thrombin-dependent Incorporation of von Willebrand Factor into a Fibrin Network.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 45 citations in OpenAlex.
- Fibrin Monomer in Thrombosis and Haemostasis: A Clinical Biomarker and Beyond.International journal of molecular sciences · 2025Review
- Computer based visualization of clot structures in extracorporeal membrane oxygenation and histological clot investigations for understanding thrombosis in membrane lungs.Frontiers in medicine · 2024Article
- Current insights into the role of citrullination in thrombosis.Current opinion in chemical biology · 2023Review
- The mechanistic and structural role of von Willebrand factor in endotoxemia-enhanced deep vein thrombosis in mice.Journal of thrombosis and haemostasis : JTH · 2023Article
- Investigating thrombin-loaded fibrin in whole blood clot microfluidic assay via fluorogenic peptide.Biophysical journal · 2023Article
- Endothelial-derived von Willebrand factor accelerates fibrin clotting within engineered microvessels.Journal of thrombosis and haemostasis : JTH · 2022Article
- Aberrant Fibrin Clot Structure Visualized Ex Vivo in Critically Ill Patients With Severe Acute Respiratory Syndrome Coronavirus 2 Infection.Critical care medicine · 2022Observational
- Staphylococcus aureus iron-regulated surface determinant B (IsdB) protein interacts with von Willebrand factor and promotes adherence to endothelial cells.Scientific reports · 2021Article
- Platelet binding to polymerizing fibrin is avidity driven and requires activated αIIbβ3 but not fibrin cross-linking.Blood advances · 2021Article
- Dominant role of αIIbβ3 in platelet interactions with cross-linked fibrin fragment D-dimer.Blood advances · 2020Article
- Von Willebrand factor as a thrombotic and inflammatory mediator in critical illness.Transfusion · 2020Article
- Modulating the rate of fibrin formation and clot structure attenuates microvascular thrombosis in systemic inflammation.Blood advances · 2020Article
- Implant stability in patients treated with platelet-rich fibrin and bovine bone substitute for alveolar ridge preservation is associated with peripheral blood cells and coagulation factors.Clinical and experimental dental research · 2020Observational
- Clinical evaluation of Emblica Officinalis Gatertn (Amla) in healthy human subjects: Health benefits and safety results from a randomized, double-blind, crossover placebo-controlled study.Contemporary clinical trials communications · 2020Article
- Structural analysis of ischemic stroke thrombi: histological indications for therapy resistance.Haematologica · 2020Article
- Insights Into Immunothrombosis: The Interplay Among Neutrophil Extracellular Trap, von Willebrand Factor, and ADAMTS13.Frontiers in immunology · 2020Review
- Atherothrombosis and Thromboembolism: Position Paper from the Second Maastricht Consensus Conference on Thrombosis.Thrombosis and haemostasis · 2018Article
- Article
- Fibrin Formation, Structure and Properties.Sub-cellular biochemistry · 2017Review
- Thrombin Generation and Atherothrombosis: What Does the Evidence Indicate?Journal of the American Heart Association · 2016Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Attachment of platelets from the circulation onto a growing thrombus is a process involving multiple platelet receptors, endothelial matrix components, and coagulation factors. It has been indicated previously that during a transglutaminase reaction activated factor XIII (FXIIIa) covalently cross-links von Willebrand factor (VWF) to polymerizing fibrin. Bound VWF further recruits and activates platelets via interactions with the platelet receptor complex glycoprotein Ib (GPIb). In the present study we found proof for binding of VWF to a fibrin monomer layer during the process of fibrinogen-to-fibrin conversion in the presence of thrombin, arvin, or a snake venom from Crotalus atrox. Using a domain deletion mutant we demonstrated the involvement of the C domains of VWF in this binding. Substantial binding of VWF to fibrin monomers persisted in the presence of the FXIIIa inhibitor K9-DON, illustrating that cross-linking via factor XIII is not essential for this phenomenon and suggesting the identification of a second mechanism through which VWF multimers incorporate into a fibrin network. Under high shear conditions, platelets were shown to adhere to fibrin only if VWF had been incorporated. In conclusion, our experiments show that the C domains of VWF and the E domain of fibrin monomers are involved in the incorporation of VWF during the polymerization of fibrin and that this incorporation fosters binding and activation of platelets. Fibrin thus is not an inert end product but partakes in further thrombus growth. Our findings help to elucidate the mechanism of thrombus growth and platelet adhesion under conditions of arterial shear rate.
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