Where is von willebrand factor found

CysPhe, p. CysArg, and p. In addition, recombinant variants display reduced survival in a murine model. Mutations may induce enhanced binding to the regular clearance receptors, such as LRP1.

Studies in this direction are currently ongoing, and will provide more insight into how VWD-related mutations are associated with increased clearance of VWF. Many interesting and relevant reports and reviews have been published concerning the topics discussed in this review.

We apologize to those authors whose papers could not be referenced due to size restrictions. Correspondence: Peter J.

Sign In or Create an Account. Sign In. Skip Nav Destination Content Menu. Close Abstract. Article Navigation. Inherited Bleeding Disorders March 26, Lenting , Peter J. This Site. Google Scholar. Olivier D. Christophe , Olivier D. Blood 13 : — Article history Submitted:.

Connected Content. A related article has been published: Introduction to a series of reviews on inherited bleeding disorders. A companion article has been published: Diagnostic approach to von Willebrand disease.

View more. A companion article has been published: Rare bleeding disorders: diagnosis and treatment. A companion article has been published: Optimal treatment strategies for hemophilia: achievements and limitations of current prophylactic regimens.

View less. Cite Icon Cite. Figure 1. View large Download PPT. Figure 2. Figure 3. Figure 4. Figure 5. Contribution: O. Conflict-of-interest disclosure: The authors declare no competing financial interests. Search ADS. Low von Willebrand factor: sometimes a risk factor and sometimes a disease. Molecular cloning, expression and assembly of multimeric von Willebrand factor.

The von Willebrand factor predicted unpaired cysteines are essential for secretion. Biosynthesis of von Willebrand protein by human endothelial cells: processing steps and their intracellular localization. Shear-induced disulfide bond formation regulates adhesion activity of von Willebrand factor.

Localization of disulfide bonds in the cystine knot domain of human von Willebrand factor. Highly reinforced structure of a C-terminal dimerization domain in von Willebrand factor. In vitro multimerization of von Willebrand factor is triggered by low pH. Importance of the propolypeptide and free sulfhydryls. Intracellular storage and regulated secretion of von Willebrand factor in quantitative von Willebrand disease. Cysteine-mutations in von Willebrand factor associated with increased clearance.

Covalent regulation of ULVWF string formation and elongation on endothelial cells under flow conditions. Initial glycosylation and acidic pH in the Golgi apparatus are required for multimerization of von Willebrand factor. An experimental model to study the in vivo survival of von Willebrand factor.

Basic aspects and application to the RH mutation. Eur J Biochem. Structures of the asparagine-linked oligosaccharide chains of human von Willebrand factor. Occurrence of blood group A, B, and H O structures. Primary structure of the major O-glycosidically linked carbohydrate unit of human von Willebrand factor.

The plasma von Willebrand factor O-glycome comprises a surprising variety of structures including ABH antigens and disialosyl motifs. Immunolocalization of von Willebrand protein in Weibel-Palade bodies of human endothelial cells. A mouse model of severe von Willebrand disease: defects in hemostasis and thrombosis.

A two-tier Golgi-based control of organelle size underpins the functional plasticity of endothelial cells. A new look at Weibel-Palade body structure in endothelial cells using electron tomography.

The secretion of von Willebrand factor from endothelial cells; an increasingly complicated story. Quantitative phosphoproteomics unveils temporal dynamics of thrombin signaling in human endothelial cells. High-pressure freezing provides insights into Weibel-Palade body biogenesis. Discs large 1 Dlg1 scaffolding protein participates with clathrin and adaptator protein complex 1 AP-1 in forming Weibel-Palade bodies of endothelial cells.

Structural organization of Weibel-Palade bodies revealed by cryo-EM of vitrified endothelial cells. Assembly of Weibel-Palade body-like tubules from N-terminal domains of von Willebrand factor. A pH-regulated dimeric bouquet in the structure of von Willebrand factor. A revised model for the secretion of tPA and cytokines from cultured endothelial cells.

Identification of galectin-1 and galectin-3 as novel partners for von Willebrand factor. Characterization of the interaction between von Willebrand factor and osteoprotegerin. The Tie-2 ligand angiopoietin-2 is stored in and rapidly released upon stimulation from endothelial cell Weibel-Palade bodies.

Inducible secretion of large, biologically potent von Willebrand factor multimers. The high molecular weight form of endothelial cell von Willebrand factor is released by the regulated pathway. Real-time imaging of the dynamics and secretory behavior of Weibel-Palade bodies.

Selective release of molecules from Weibel-Palade bodies during a lingering kiss. Platelets adhere to and translocate on von Willebrand factor presented by endothelium in stimulated veins.

ADAMTS rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions. Multigranular exocytosis of Weibel-Palade bodies in vascular endothelial cells. Weibel-Palade bodies recruit Rab27 by a content-driven, maturation-dependent mechanism that is independent of cell type.

To facilitate binding to various cells and proteins, these subunits are cut into smaller pieces by an enzyme called ADAMTS Von Willebrand factor helps platelets stick together and adhere to the walls of blood vessels at the site of a wound. These groups of platelets form temporary clots, plugging holes in blood vessel walls to help stop bleeding. Von Willebrand factor also carries another blood clotting protein, coagulation factor VIII, to the area of clot formation.

More than mutations in the VWF gene have been found to cause von Willebrand disease. Mutations in the VWF gene that reduce the amount of von Willebrand factor cause type 1 von Willebrand disease. People with type 1 von Willebrand disease have von Willebrand factor in their bloodstream, but at reduced amounts. Mutations that disrupt the function of the von Willebrand factor cause the four subtypes of type 2 von Willebrand disease.

These mutations usually change one of the protein building blocks amino acids used to make von Willebrand factor, which can disrupt the factor's ability to bind to various cells and proteins needed to form a blood clot. Mutations that result in an abnormally short, nonfunctional von Willebrand factor generally cause the more severe type 3 von Willebrand disease. A reduction in the amount of von Willebrand factor or problems with its function slows the formation of blood clots, which causes the prolonged bleeding episodes seen in von Willebrand disease.

The type of treatment prescribed for VWD depends on the type and severity of the disease. For minor bleeds, treatment might not be needed. It works by making the body release more VWF into the blood. It also helps increase the level of factor VIII in the blood. These medicines are injected into a vein in the arm to replace the missing factor in the blood. A doctor can prescribe these pills for women who have heavy menstrual bleeding.

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