Study shows distinct biological functions of glycoprotein Ibα binding with von Willebrand factor and factor XI in platelets, indicating differing mechanisms are involved.
Platelets play crucial roles in regulating vascular functions [1–3] . Under high wall shear rate conditions, platelet adhesion is mediated exclusively by their membrane glycoprotein (GP) Ibα binding with the A1 domain of von Willebrand factor (VWF) [4] . The VWF binding site of GPIbα locates N-terminus leucine-rich repeat that is close to the binding site of coagulation factor XI (FXI) [5] . The biological function of GPIbα binding with FXI [6] differ substantially to the role of GPIba-VWF binding. However, the physical basis of the mechanisms of GPIba-VWF and GPIba-FXI bindings mediating their distinct biological functions remain unclear.
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Nakayama et al. (2026) studied this question.
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