Analysis Biomolecular Interactions of Gal-1 and Gal-3 With Von Willebrand Factor (VWF) by BLI (CAT#: STEM-MB-0144-CJ)

Introduction

Von Willebrand factor (VWF) is an adhesive protein that is critical to the recruitment of platelets in response to vessel injury. The majority of the circulating VWF molecules are produced in the endothelial cells, where VWF is synthesized as a single prepropolypeptide chain. Following signal peptide removal, the polypeptides are assembled into C-terminal linked pro-VWF dimers. An important portion of the newly synthesized VWF multimers is directed to endothelial storage organelles, Weibel-Palade (WP) bodies. VWF is obligatory for the formation of WP bodies, which are indeed absent in endothelial cells isolated from VWF-deficient mice or dogs. These storage organelles also contain other proteins besides VWF, including P-selectin, osteoprotegerin, CD63, and interleukin-8. Some of these proteins directly interact with VWF, which may facilitate their uptake into the WP bodies.