ArticleJournal of thrombosis and haemostasis : JTH2024
R1205H (Vicenza) causes conformational changes in the von Willebrand factor D'D3 domains and enhances von Willebrand factor binding to clearance receptors LRP1 and SR-AI.
Article in Journal of thrombosis and haemostasis : JTH, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Natural variants of von Willebrand factor R1205 causing von Willebrand disease with accelerated von Willebrand factor clearance: In silico docking models and energetics of the interaction with both LRP1 and GpIb A1 domain.PLoS computational biology · 2025Article
- Interplay between circulating von Willebrand factor and neutrophils: implications for inflammation, neutrophil function, and von Willebrand factor clearance.Haematologica · 2025Article
- Frequency of type 2N von Willebrand disease among patients with mild or moderate factor VIII deficiency in an 18-month period in Iran.Blood transfusion = Trasfusione del sangueArticle
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Authors and funding
15 authors.
Funding
Abstract
backgroundvon Willebrand factor (VWF)-R1205H variant (Vicenza) results in markedly enhanced VWF clearance in humans that has been shown to be largely macrophage-mediated. However, the biological mechanisms underlying this enhanced clearance remain poorly understood.
objectivesThis study aimed to investigate the roles of (i) specific VWF domains and (ii) different macrophage receptors in regulating enhanced VWF-R1205H clearance.
methodsIn vivo clearance of full-length and truncated wild-type (WT)-VWF and VWF with R1205 substitutions was investigated in VWF
resultsIn full-length VWF missing the A1 domain, introduction of R1205H led to significantly enhanced clearance in VWF
conclusionDisruption of the positive charge at amino acid R1205 causes conformational changes in the VWF-D'D3 domains and triggers enhanced LRP1-mediated and SR-AI-mediated clearance.
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