Background: The plasma metalloprotease ADAMTS13 regulates the thrombotic activity of the von Willebrand factor (VWF). ADAMTS13 is highly glycosylated and its carbohydrate chains are capped with sialic acid (SA). Thus, ADAMTS13 may interact with carbohydrate- and/or SA-binding plasma membrane receptors that are involved in the clearance of various plasma proteins.
View Article and Find Full Text PDFMembrane fission, the division of a membrane-bound structure into two discrete compartments, is essential for diverse cellular events, such as endocytosis and vesicle/granule biogenesis; however, the process remains unclear. The hemostatic protein von Willebrand factor is produced in vascular endothelial cells and packaged into specialized secretory granules, Weibel-Palade bodies (WPBs) at the -Golgi network (TGN). Here, we reported that V0a1, a V-ATPase component, is required for the membrane fission of WPBs.
View Article and Find Full Text PDFVon Willebrand factor (VWF) is a 500- to 15 000-kDa multimeric protein circulating in the blood. When VWF has a higher molecular weight, its hemostatic activity is greater. The size distribution of VWF multimers is usually analyzed by SDS-agarose gel electrophoresis followed by immunoblotting.
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