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ADAMTS ‐13 and von Willebrand factor: a dynamic duo
Author(s) -
South K.,
Lane D. A.
Publication year - 2018
Publication title -
journal of thrombosis and haemostasis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.947
H-Index - 178
eISSN - 1538-7836
pISSN - 1538-7933
DOI - 10.1111/jth.13898
Subject(s) - von willebrand factor , adamts , hemostasis , platelet , antithrombotic , chemistry , conformational change , von willebrand disease , medicine , metalloproteinase , biochemistry , matrix metalloproteinase , thrombospondin
Summary von Willebrand factor ( VWF ) is a key player in hemostasis, acting as a carrier for factor VIII and capturing platelets at sites of vascular damage. To capture platelets, it must undergo conformational changes, both within its A1 domain and at the macromolecular level through A2 domain unfolding. Its size and this function are regulated by the metalloproteinase ADAMTS ‐13. Recently, it has been shown that ADAMTS ‐13 undergoes a conformational change upon interaction with VWF , and that this enhances its activity towards its substrate. This review summarizes recent work on these conformational transitions, describing how they are controlled. It points to their importance in hemostasis, bleeding disorders, and the developing field of therapeutic application of ADAMTS ‐13 as an antithrombotic agent in obstructive microvascular thrombosis and in cardiovascular disease.