Analysis Biomolecular Interactions of VWF-Galectin by BLI (CAT#: STEM-MB-0106-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. 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. 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. Indeed, VWF multimers assemble into twisted bundles and networks that form long strings along the endothelial surface. These VWF strings are able to catch platelets, and these platelet-decorated strings can be visualized via microscopy in vitro and in vivo. During its synthesis, VWF is also subject to extensive glycosylation. The mature VWF subunit contains 12 sites for N-linked glycosylation and 10 sites for O-linked glycosylation. The carbohydrate structures on VWF play an important role in the various steps of the VWF life-cycle.