Abstract
Recently, the platelet-binding function of the blood protein von Willebrand factor (VWF) has been shown to be activated by oxidizing conditions such as created by inflammation. This observation has been linked to the oxidation of methionine residues in three tandem A domains of VWF. Here, we used a dynamic flow assay to investigate which auto-inhibitory mechanisms of VWF are shut down leading to the observed activation. The results show that oxidizing agents do not directly activate the A1 domain, which is the domain in VWF that contains the binding site to platelet surface receptors, but are likely to remove the inhibitory function of neighboring domains of A1.
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