Jan 24, 2019 · Von Willebrand factor (VWF) is a key player in the regulation of hemostasis by promoting recruitment of platelets to sites of vascular injury. An array of 6 C domains forms the dimeric C-terminal VWF stem.

May 27, 2021 · Interaction of factor VIII (FVIII) with von Willebrand factor (VWF) is mediated by the VWF D′D3 domains and thrombin-mediated release is essential for hemostasis after vascular injury. VWF-D′D3 mutations resulting in loss of FVIII binding are the underlying cause of von Willebrand disease (VWD) type 2N.

Sep 26, 2024 · Rondaptivon pegol (previously BT200) is a pegylated RNA aptamer that binds to the A1 domain of von Willebrand factor (VWF). Recent clinical trials demonstrated that BT200 significantly increased plasma VWF–factor VIII levels by attenuating VWF clearance.

Phenotypic von Willebrand disease (VWD) classification requires multiple tests including analysis of multimeric distributions von Willebrand factor (VWF) and evaluation of its structure. VWF multimer analysis is labor intensive, nonstandardized, and limited to specialized laboratories.

Von willebrand factor (VWF) is a large multimeric glycoprotein present in plasma. It is synthesized in Weibel-Palade bodies in endothelium, α-granules of platelets (megakaryocytes) and sub-endothelial connective tissue [7]. Each monomer of VWF contains 2050 amino acids with specific domains possessing specific functions [7].

Jun 10, 2010 · Twenty-two different mutations, most of them affecting cysteine residues, 17 of them being novel, are clustering mainly in the VWF D3 domain and correlate with the VWD2A/IIE phenotype. An intracellular retention of most mutants and/or a defect of multimerization seem to be the main pathogenic molecular mechanisms.

At sites of vascular injury, von Willebrand factor (VWF) mediates platelet adhesion through binding to platelet glycoprotein Ib (GPIb). Previous studies identified clusters of charged residues within VWF domain A1 that were involved in binding GPIb or botrocetin.

Previous studies have demonstrated that the A1A2A3 domains of VWF play a key role in regulating macrophage-mediated clearance in-vivo. In particular, the A1-domain has been shown to modulate interaction with macrophage LRP1 clearance receptor.

Jul 10, 2024 · Plate-binding assays were employed to characterize VWF binding to purified scavenger receptor class A member 1 (SR-A1), low-density lipoprotein receptor-related protein-1 (LRP1) cluster II or cluster IV receptors, and macrophage galactose-type lectin (MGL).

Dec 1, 2024 · Our results reveal domain-specific responses of vWF, particularly in the A2 and A3 domains, which demonstrate significant elongation under elevated shear—reflecting their pivotal roles in clotting processes.