1. Introduction von Willebrand’s disease (vWd) was identified in 1926 among residents of the Aland Islands off the coasts of Finland by Erik von Willebrand, who described a severe bleeding disorder distinct from hemophilia, inherited as an autosomal trait [1]. In 1957, transfusion studies indicated that the defect could be corrected by a plasma factor distinct from factor VIII (FVIII), referred to as von Willebrand factor (vWf)[2]. Rapid progress has been made in the last two decades in the understanding of vWf biology and pathology. vWf synthesis and processing in endothelial cells (ECs) have been characterized [3]. The protein sequence has been obtained and the structure–function relationships have been largely elucidated [4]. The protein is involved in primary hemostasis, ie the formation of a platelet plug at sites of vascular injury, via multiple discrete functional domains. It also functions as an essential carrier protein for FVIII, ensuring the stability of this factor in the circulation. Many of the mutations which cause various forms of von Willebrand’s disease (vWd) have been identified and correlated to their effects on vWf structure and function [5, 6]. In addition, other diseases may be related to quantitative or functional defects in vWf. These include acquired vWd and recurrent thrombotic thrombocytopenic purpura [7–9]. vWf may be essential for arterial occlusion in ischemic heart disease [10]. Furthermore, vWf has also attracted interest as a plasma marker of endothelial activation in a number of chronic vascular disorders such as diabetesrelated angiopathies [11]. Acquired vWd and the role of vWf in chronic vascular disorders will not be discussed here. The present paper will focus on the current