1AO3, 1ATZ, 1AUQ, 1FE8, 1FNS, 1IJB, 1IJK, 1M10, 1OAK, 1U0N, 2ADF, 3GXB, 3HXO, 3HXQ, 3PPV, 3PPW, 3PPX, 3PPY, 3ZQK, 4DMU, 1UEX, 2MHP, 2MHQ, 4C29, 4C2A, 4C2B, 4NT5, 5BV8745022371ENSG00000110799ENSMUSG00000001930P04275Q8CIZ8NM_000552NM_011708NP_000543NP_035838Von Willebrand factor (VWF) (German: [fɔn ˈvɪləbʁant]) is a blood glycoprotein that promotes primary hemostasis, specifically, platelet adhesion.

After glycosylation in the Golgi apparatus, VWF is packaged into storage granules, Weibel-Palade bodies (WPBs) in endothelial cells, and α-granules in platelets.

Therefore, VWF deficiency or dysfunction (von Willebrand disease) leads to a bleeding tendency, which is most apparent in tissues having high blood flow shear in narrow vessels.

[7] The biological breakdown (catabolism) of VWF is largely mediated by the enzyme ADAMTS13 (acronym of "a disintegrin-like and metalloprotease with thrombospondin type 1 motif no.

This leads to decreased breakdown of the ultra-large multimers of VWF and microangiopathic hemolytic anemia with deposition of fibrin and platelets in small vessels, and capillary necrosis.

High plasma VWF levels were found to be an independent predictor of major bleeding in anticoagulated atrial fibrillation patients.

[15] VWF is named after Erik Adolf von Willebrand, a Finnish physician who in 1926 first described a hereditary bleeding disorder in families from Åland.

[5] Harvey J. Weiss[17] and coworkers developed a quantitative assay for VWF function that remains a mainstay of laboratory evaluation for VWD to this day.

[19] Recently, It has been reported that the cooperation and interactions within the von Willebrand Factors enhances the adsorption probability in the primary haemostasis.