Simultaneous Exposure of Sites in von Willebrand Factor for Glycoprotein Ib Binding and ADAMTS13 Cleavage
Author(s) -
Junmei Chen,
Minhua Ling,
Xiaoyun Fu,
José A. López,
Dominic W. Chung
Publication year - 2012
Publication title -
arteriosclerosis thrombosis and vascular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.007
H-Index - 270
eISSN - 1524-4636
pISSN - 1079-5642
DOI - 10.1161/atvbaha.112.254144
Subject(s) - adamts13 , von willebrand factor , ristocetin , chemistry , platelet membrane glycoprotein , glycoprotein ib , proteolysis , cleavage (geology) , von willebrand disease , glycoprotein , platelet , binding site , recombinant dna , biochemistry , biology , enzyme , immunology , gene , paleontology , fracture (geology)
Platelet-bound von Willebrand factor (VWF) was recently demonstrated to be a better substrate for ADAMTS13, suggesting that 1 conformational change exposes both the glycoprotein Ibα binding site in the A1 domain and the ADAMTS13 cleavage site in the A2 domain. Because ristocetin induces VWF to bind glycoprotein Ibα in the absence of shear stress, we evaluated whether it could also enhance ADAMTS13 proteolysis of VWF.
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