ArticleResearch and practice in thrombosis and haemostasis2021
Fibronectin binding to von Willebrand factor occurs via the A1 domain.
Article in Research and practice in thrombosis and haemostasis, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- Von Willebrand disease: A century of progress.Research and practice in thrombosis and haemostasis · 2026Review
- A Damaging COL6A3 Variant Alters the MIR31HG-Regulated Response of Chondrocytes in Neocartilage Organoids to Hyperphysiologic Mechanical Loading.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Staphylococcus aureus iron-regulated surface determinant B (IsdB) protein interacts with von Willebrand factor and promotes adherence to endothelial cells.Scientific reports · 2021Article
- Commonly used anti-von Willebrand factor antibody for multimer analysis cross-reacts with fibronectin, which is difficult to distinguish from von Willebrand factor.Research and practice in thrombosis and haemostasis · 2021Article
- Erratum:.Research and practice in thrombosis and haemostasis · 2021Article
Corrections and comments
- Erratum issuedErratum:.2021
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundCollagen interactions with von Willebrand factor (VWF) perform an important role in initiation of hemostasis.
objectivesWe hypothesized that in addition to collagen, other extracellular matrix (ECM) proteins such as fibronectin can bind VWF.
methodsFibronectin-VWF interactions were measured by ELISA using both plasma-derived and recombinant VWF-containing variants in specific domains. Inhibition was measured by antibody competition using antibodies directed against both VWF and fibronectin. Binding affinities were measured by the Octet Biosensor for fibronectin and collagen IV.
resultsFibronectin was able to bind both plasma-derived and recombinant wild-type VWF. This interaction was inhibited by both anti-VWF antibodies and collagen types III and IV. Several VWF A1 domain variants in the region of the collagen IV binding site also demonstrated absent fibronectin binding, as did variants with defects in high-molecular-weight multimers. Binding affinity testing showed fibronectin has a strong affinity for VWF, in a range similar to that of collagen IV. Fibronectin binds VWF via a restricted region of the A1 domain. This interaction requires high-molecular-weight multimers and is similar to that seen with vascular collagens.
conclusionsTherefore, VWF would appear to be the common factor linking platelet adhesion to various ECM proteins and facilitating hemostasis under conditions of ECM exposure.
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Registered trials
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.