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VON WILLEBRAND FACTOR (vWF) PRO-POLYPEPTIDE IS REQUIRED FOR vWF MULTIMER FORMATION [PDF]

Thrombosis and Haemostasis, 1987
The von Willebrand factor (vWF) is a multimeric plasma glycoprotein synthesized in vascular endothelial cells as a pre-pro-polypeptide with a highly repetitive domain structure, symbolized by the formula:(H)-D1-D2-D'-D3-A1-A2-A3-D4-B1-B2-B3-C1-C2-(0H).A heterologous expression system, consisting of a monkey kidney cell line (C0S-1), transfected with ...
Hans Pannekoek, C L Verweij, M. Hart
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The role of VWF in the immunogenicity of FVIII

Thrombosis Research, 2008
Up to 33% of patients with severe haemophilia A develop inhibitory antibodies to factor VIM (FVIII) that can significantly impair treatment with FVIII. The plasma protein von Willebrand factor (VWF) binds to FVIII and is known to be important for the functioning of FVIII.
Sébastien Lacroix-Desmazes, Suryasarathi Dasgupta, Yohann Repessé, Srinivas V. Kaveri   +3 more
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Alanine Scanning Mutagenesis of the VWF-A1 Flanking Regions of VWF and the Impact on Ristocetin-induced VWF Interaction with Platelets

Blood, 2013
Abstract Von Willebrand disease is a bleeding disorder with reduced or abnormal function of VWF. While VWF has at least three functions (binding to FVIII, platelet GPIb, and collagen), the function of VWF has been quantified primarily using techniques in which ristocetin promotes the binding of VWF to platelet GPIb. It is recognized that
Matt Hille, J. Paul Scott, Sandra L. Haberichter, Robert R. Montgomery, Veronica H. Flood, Patti A Morateck   +5 more
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ADAMTS13 content and VWF multimer and triplet structure in commercially available VWF/FVIII concentrates

Biologicals, 2015
ADAMTS13 is a metalloproteinase that cleaves von Willebrand factor (VWF) into smaller multimers in vivo. This cleavage creates both the typical multimeric size distribution and the characteristic triplet band distribution of VWF. Here we analysed ADAMTS13 content, VWF multimeric size distribution and VWF triplet structure in five commercial VWF/factor ...
Birte Fuchs, Werner Hofmann, Mario Kröning, Claudine Fisseau, Christoph Kannicht   +4 more
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Sugar targets VWF for the chop

Blood, 2010
In this issue of Blood , McGrath et al provide new insights into the influence of glycosylation on VWF proteolysis by ADAMTS13.[1][1] Von Willebrand factor (VWF) is synthesized in vascular endothelial cells and megakaryocytes and undergoes extensive processing prior to secretion.
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VWF secretion: what's in a name?

Blood, 2008
In this issue of Blood , Giblin and colleagues report that the continuous spontaneous release of VWF from endothelial cells is largely due to secretion of a stored form of the mature protein and not to its continuous transit out of the cell by classic constitutive secretion. von Willebrand Factor (
Jill M. Johnsen, Jose A. Lopez
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Binding of FVIII to Recombinant VWF

Blood, 2010
Abstract Abstract 1408 Von Willebrand factor (VWF) forms a non-covalent complex with FVIII in the circulation, which not only stabilizes the heterodimeric structure of FVIII but also protects this coagulation protein from early proteolytic degradation and cellular uptake.
Hartmut J. Ehrlich, Peter Turecek, Hanspeter Rottensteiner, Gerald Schrenk, Katalin Varadi, Friedrich Scheiflinger   +5 more
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Genetic Determinants of Plasma Von Willebrand Factor (VWF) and VWF Propeptide Levels

Blood, 2012
Abstract Abstract 3313 Plasma VWF levels vary by approximately five-fold in healthy populations and are influenced by both environmental and inherited factors. Low levels of VWF are associated with bleeding and elevated levels with increased risk for thrombosis.
Jun Li, Ayse Bilge Ozel, David R. Siemieniak, David Ginsburg, Karl C. Desch   +4 more
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Chromatography of vWF on dextran sulphate sepharose

Thrombosis Research, 1987
A relatively simple and reproducible chromatographic separation using Dextran Sulphate (DS) Agarose is described for the purification of vWf:Ag from cryoprecipitate or plasma source material. The elution profiles suggest high affinity of vWf for the matrix permitting resolution from Fibrinogen, IgG and the unbound Albumin.
Paul Harrison, G. F. Savidge, R.H. Saundry   +2 more
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VWF, ADAMTS13, and acute coronary syndromes [PDF]

Blood, 2016
In this issue of Blood, Pedrazzini et al1 have taken an important step toward revitalizing our view of coronary artery thrombosis and providing a new target for the pharmacologic treatment of acute coronary syndromes (ACS).
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