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Platelet von Willebrand Factor
Mayo Clinic Proceedings, 1991von Willebrand factor (vWF) circulates in the blood in two distinct compartments. One, plasma vWF, is synthesized and released from endothelial cells; the second, synthesized by megakaryocytes, circulates in platelets primarily stored in the alpha granules.
H R, Gralnick +6 more
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Platelet von Willebrand factor: Comparison with plasma von Willebrand factor
Thrombosis Research, 1985Platelet von Willebrand factor (vWf) was compared to its plasma counterpart. The platelet vWf was different from plasma vWf in that the multimeric organization was different, larger multimers were present, and the ratio of vWf activity to antigen was higher.
H R, Gralnick +5 more
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Von Willebrand factor and thrombosis
Annals of Hematology, 2006There is increasing evidence that von Willebrand factor (VWF), an adhesive multimeric protein that has an important function in primary hemostasis and as a carrier of factor VIII, has a pivotal role in thrombogenesis. In fact, while the presence in plasma of unusually large VWF multimers due to a congenital or acquired deficiency of a VWF-cleaving ...
Franchini M, LIPPI, Giuseppe
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Von Willebrand factor processing
Hämostaseologie, 2017SummaryVon Willebrand factor (VWF) is a multimeric glycoprotein essential for primary haemostasis that is produced only in endothelial cells and megakaryocytes. Key to VWF’s function in recruitment of platelets to the site of vascular injury is its multimeric structure.
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von Willebrand Factor, von Willebrand Factor-Cleaving Protease, and Shear Stress
Cardiovascular & Hematological Agents in Medicinal Chemistry, 2007von Willebrand factor (VWF) is a multimeric plasma glycoprotein (GP) involved in platelet adhesion at the site of vascular damage, which acts as a bridge between the injured subendothelium and the platelet receptors. The multimeric structure of VWF allows it to support multiple interactions with platelets and endothelial components under high shear ...
P, Perutelli, A C, Molinari
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Von Willebrand factor multimer patterns in von Willebrand's disease
British Journal of Haematology, 1983Summary. The von Willebrand factor antigen (factor VIII‐related antigen, VIIIR:Ag) multimer pattern has been analysed by SDS‐agarose electrophoresis of plasmas from 116 patients (47 families) with von Willebrand's disease. In addition to previously recognized patterns, a subclassification was established between plasmas that had a type Ia pattern ...
L W, Hoyer +5 more
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Antibodies to von Willebrand factor in von Willebrand disease
1995The occurrence of an alloantibody directed against von Willebrand factor in a multitransfused patient with severe (type III) von Willebrand disease was first reported in 2 consecutive studies by Sarji et al. (1974) and Stratton et al. (1975). After this, 14 additional cases of alloantibodies were described and reviewed by Mannucci and Mari (1984).
P M, Mannucci, A B, Federici
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von Willebrand's factor and von Willebrand's disease.
Current opinion in hematology, 1997von Willebrand's factor is required for platelet adhesion to subendothelium, and for normal factor VIII survival in the circulation. These functions require the assembly of von Willebrand's factor into multimers that exhibit properly regulated binding to platelet glycoprotein lb. Recent studies suggest that the propeptide of von Willebrand's factor may
T, Matsushita, Z, Dong, J E, Sadler
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[Von Willebrand factor and Von Willebrand disease].
Nederlands tijdschrift voor geneeskunde, 2014Von Willebrand factor (VWF) is a multimeric adhesive protein that binds platelets to exposed subendothelium and carries factor VIII in the circulation. VWD is classified into three major subtypes, distinguished by a quantitative deficiency of VWF (type 1: partial deficiency; type 3: complete deficiency) or qualitative defects of VWF (type 2A, 2B, 2M ...
Paul W M, Verhezen +2 more
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von Willebrand factor and von Willebrand disease.
Blood, 1987Progress has occurred in the past several years in the understanding of the structure and function of von Willebrand factor (vWF). This multimeric glycoprotein exhibits a dual role, that of mediating platelet adhesion and aggregation onto thrombogenic surfaces, and that of functioning as carrier in plasma for the factor VIII procoagulant protein.
Z M, Ruggeri, T S, Zimmerman
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