von Willebrand factor; vWF; ristocetin cofactor; factor VIII related antigen; contains: von Willebrand antigen 2 (VWF, F8VWF)
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Function
- important in the maintenance of hemostasis
- promotes adhesion of platelets to the sites of vascular injury
- mediates platelet adhesion to collagen via binding sites for collagen & for glycoprotein Ib & glycoprotein IIb/IIIa on surface of activated platelets
- acts as a chaperone for coagulation factor VIII
- binds factor VIII preventing association of factor VIII with phospholipid membranes
- vWF is cleaved by vWF-cleaving protease degrading its platelet adhesion-promoting properties
- plasmin also cleaves large vWF multimers; however platelet adhesive-promoting properties of vWF are largely retained
Structure
- forms large (> 1000 kD) multimers
- the von Willebrand antigen 2 is required for multimerization of vWF & for its targeting to storage granules
- multimers consist of 250 kD subunits linked by disulfide bonds
- all Cys are involved in intrachain or interchain disulfide bonds
- N- & O-glycosylated
- contains 1 CTCK (C-terminal cystine knot-like) domain
- contains 4 TIL (trypsin inhibitory-like) domains
- contains 3 VWFA domains
- contains 3 VWFC domains
- contains 4 VWFD domains
Compartment
- secreted, extracellular space, extracellular matrix
- localized to storage granules
Expression
Pathology
- defects in VWF are the cause of von Willebrand disease
- disruption of HMW vWF multimers may occur with aortic valvular stenosis stenosis & other other forms of turbulent blood flow resulting in secondary von Willebrand disease (Heyde's syndrome)
More general terms
More specific terms
Additional terms
Component of
- antihemophilic factor/von willebrand factor
- recombinant factor VIII/von Willebrand factor
- factor VIII/von Willebrand factor; vWF-rich factor VIII
References
- ↑ Cotran et al Robbins Pathologic Basis of Disease, W.B. Saunders Co, Philadelphia, PA 1989 pg 696
- ↑ Kane WH, Davie EW. Blood coagulation factors V and VIII: structural and functional similarities and their relationship to hemorrhagic and thrombotic disorders. Blood. 1988 Mar;71(3):539-55. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/3125864
- ↑ Andrews BS. Is the WKS motif the tissue-factor binding site for coagulation factor VII? Trends Biochem Sci. 1991 Jan;16(1):31-6. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/2053135
- ↑ Furlan M, Robles R, Lamie B. Partial purification and characterization of a protease from human plasma cleaving von Willebrand factor to fragments produced by in vivo proteolysis. Blood. 1996 May 15;87(10):4223-34. PMID: https://www.ncbi.nlm.nih.gov/pubmed/8639781
- ↑ Entrez Gene http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=7450
- ↑ UniProt http://www.uniprot.org/uniprot/P04275.html
- ↑ vWF; von Willebrand factor (vWF) mutation db http://www.vwf.group.shef.ac.uk/
- ↑ GeneReviews http://www.ncbi.nlm.nih.gov/sites/genetests/lab/gene/VWF
- ↑ Wikipedia; Note: Von Willebrand factor entry http://en.wikipedia.org/wiki/Von_Willebrand_factor