Defining the Molecular Basis Underlying the Physiological Interaction Between Von Willebrand Factor and Galectins in Normal Plasma.
Orla Rawley1, Jamie O’Sullivan1, Alain Chion1, Niamh O’Regan1, Vince Jenkins1,2, Teresa Brophy1 and James S. O’Donnell1,2.
1Haemostasis Research Group, Institute of Molecular Medicine, St. James’s Hospital, Trinity College Dublin, Ireland.2National Centre for Coagulation Disorders, St James’s Hospital, Dublin.
Von Willebrand Factor (VWF) is extensively glycosylated with both N- and O-linked carbohydrates. Importantly, these complex glycan structures influence VWF functional properties, including susceptibility to ADAMTS13 proteolysis, and plasma clearance. Although, the molecular mechanisms through which the glycans modulate VWF biology remain poorly understood, recent data suggest that plasma VWF circulates in complex with specific members of the galectin family. Moreover, these galectin interactions modulate VWF-mediated thrombus formation. In this context, we sought to define the molecular basis underlying the interactions between VWF and galectins-1 and -3 respectively.