Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation.Zinc and calcium ions cooperatively modulate enzyme activity. The cleavage of the pro-domain is not required for protease activity. Dependence on calcium for proteolytic activity is mediated by the high affinity site.
Von Willebrand Factor (VWF) is a multimeric glycoprotein involved in hemostasis in blood, binds receptors on the surface of platelets and in connective tissue, thereby mediating the adhesion of platelets to sites of vascular injury. From studies it appears that VWF protein uncoils under these circumstances, decelerating passing platelets. VWF protein is deficient or defective in von Willebrand disease (VWD) and is involved in a large number of other diseases, including thrombosis, thrombotic thrombocytopenic purpura, Stroke, Heyde's syndrome, possibly hemolytic-uremic syndrome and so on.
There exists two types of tryptophanyl tRNA synthetases, the cytoplasmic form called WARS, the mitochondrial form called WARS2. WARS catalyzes the aminoacylation of tRNA (trp) with tryptophan and is induced by interferon. WARS regulates ERK, Akt, eNOS activation pathway, which are related with angiogenesis, cytoskelatal reorganization and shear stess-reponsive gene expression.
WW Domain-Binding Protein 1 (WBP1) is widely expressed in many tissues, but it is lowly expressed in the lung, placenta, kidney, and liver. WBP1 contains two WW-binding motifs: WW-binding 1 and WW-binding 2 that are involved in mediating protein-protein interactions through the binding of polyproline ligands. The WW-binding domain is composed of 38 to 40 semi-conserved amino acids shared by proteins with diverse functions including structural, regulatory, and signaling proteins. In addition, WBP1 also encodes a ligand of the WW domain of the Yes kinase-associated protein. This function has not been determined.
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