ADAMTS-13 and von Willebrand factor: a dynamic duo

K South, D A Lane

Research output: Contribution to journalReview articlepeer-review


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.

Original languageEnglish
Pages (from-to)6-18
Number of pages13
JournalJournal of thrombosis and haemostasis : JTH
Issue number1
Publication statusPublished - 1 Jan 2018


  • ADAMTS13 Protein/chemistry
  • Animals
  • Blood Platelets/enzymology
  • Cerebrovascular Disorders/blood
  • Fibrinolytic Agents/therapeutic use
  • Hemostasis
  • Humans
  • Models, Molecular
  • Myocardial Infarction/blood
  • Protein Conformation
  • Protein Folding
  • Structure-Activity Relationship
  • von Willebrand Factor/chemistry


Dive into the research topics of 'ADAMTS-13 and von Willebrand factor: a dynamic duo'. Together they form a unique fingerprint.

Cite this