The co-influence of VWD type 2B/2M mutations in the A1 domain and platelet GPIb alpha on the rate of cleavage to VWF by ADAMTS13

摘要

Introduction: In plasma, the size of the von Willebrand factor (VWF) multimer is down-regulated by ADAMTS13 (a disintegrin and metalloprotease with thrombospondin type 1 repeats, member 13). The binding of platelets or glycoprotein (GP) Ib alpha recombinant fragment to VWF domain A1 may increase the cleavage by ADAMTS13 to VWF. Both type 2B and type 2M von Willebrand disease (VWD) result in bleeding disorders with the diathesis of increased and decreased binding affinity between GPIb alpha and VWF, respectively. However, the influence of 2B/2M VWD mutations in the A1 domain and GPIb alpha on cleavage by ADAMTS13 to VWF needs further study.