Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

ADAMTS13

  • Christian R. Robinson
  • Ina Laura Pieper
  • Venkateswarlu Kanamarlapudi
Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_101991

Synonyms

Historical Background

The ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) are a family of proteases that include 19 members. ADAMTS are closely related to the ADAM (a disintegrin and metalloproteinase) subfamily of metalloendopeptidases, sharing similar metalloproteinase domains. ADAMTS are secreted proteases that are involved in matrix proteoglycan cleavage, processing of collagen, and regulating processes such as angiogenesis and hemostasis (Porter et al. 2005).

ADAMTS13 is a protein of 1,427 amino acids with a deduced molecular weight of 190 kDa (Levy et al. 2001). ADAMTS13 was originally identified as a von Willebrand factor (vWF)-cleaving protease (vWF-cp), later discovered to be a novel member of the ADAMTS family. Following genome-wide linkage analysis, the ADAMTS13 gene was located on the human chromosome 9q34 (Levy...

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References

  1. Anderson PJ, Kokame K, Sadler JE. Zinc and calcium ions cooperatively modulate ADAMTS13 activity. J Biol Chem. 2006;281:850–7.PubMedCrossRefGoogle Scholar
  2. Bartoli CR, Kang J, Restle DJ, Zhang DM, Shabahang C, Acker MA, et al. Inhibition of ADAMTS-13 by doxycycline reduces von Willebrand factor degradation during supraphysiological shear stress: therapeutic implications for left ventricular assist device-associated bleeding. JACC Heart Fail. 2015;3:860–9.PubMedCrossRefGoogle Scholar
  3. Cal S, Obaya AJ, Llamazares M, Garabaya C, Quesada V, López-Otín C. Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains. Gene. 2002;283:49–62.PubMedCrossRefGoogle Scholar
  4. de Vries PS, van Herpt TT, Ligthart S, Hofman A, Ikram MA, van Hoek M, et al. ADAMTS13 activity as a novel risk factor for incident type 2 diabetes mellitus: a population-based cohort study. Diabetologia. 2017;60:280–286.PubMedCrossRefGoogle Scholar
  5. Fujikawa K, Suzuki H, McMullen B, Chung D. Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family. Blood. 2001;98:1662–6.PubMedCrossRefGoogle Scholar
  6. Furlan M, Robles R, Lämmle B. Partial purification and characterization of a protease from human plasma cleaving von Willebrand factor to fragments produced by in vivo proteolysis. Blood. 1996;87:4223–34.PubMedPubMedCentralGoogle Scholar
  7. Furlan M, Robles R, Morselli B, Sandoz P, Lämmle B. Recovery and half-life of von Willebrand factor-cleaving protease after plasma therapy in patients with thrombotic thrombocytopenic purpura. Thromb Haemost. 1999;81:8–13.PubMedCrossRefGoogle Scholar
  8. Gerritsen HE, Robles R, Lämmle B, Furlan M. Partial amino acid sequence of purified von Willebrand factor-cleaving protease. Blood. 2001;98:1654–61.PubMedCrossRefGoogle Scholar
  9. Kokame K, Matsumoto M, Soejima K, Yagi H, Ishizashi H, Funato M, et al. Mutations and common polymorphisms in ADAMTS13 gene responsible for von Willebrand factor-cleaving protease activity. Proc Natl Acad Sci U S A. 2002;99:11902–7.PubMedPubMedCentralCrossRefGoogle Scholar
  10. Levy GG, Nichols WC, Lian EC, Foroud T, McClintick JN, McGee BM, et al. Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura. Nature. 2001;413:488–94.PubMedCrossRefGoogle Scholar
  11. Moake JL, Rudy CK, Troll JH, Weinstein MJ, Colannino NM, Azocar J, et al. Unusually large plasma factor VIII:von Willebrand factor multimers in chronic relapsing thrombotic thrombocytopenic purpura. N Engl J Med. 1982;307:1432–5.PubMedCrossRefGoogle Scholar
  12. Moake JL, Byrnes JJ, Troll JH, Rudy CK, Hong SL, Weinstein MJ, et al. Effects of fresh-frozen plasma and its cryosupernatant fraction on von Willebrand factor multimeric forms in chronic relapsing thrombotic thrombocytopenic purpura. Blood. 1985;65:1232–6.PubMedPubMedCentralGoogle Scholar
  13. Muia J, Zhu J, Gupta G, Haberichter SL, Friedman KD, Feys HB, et al. Allosteric activation of ADAMTS13 by von Willebrand factor. Proc Natl Acad Sci U S A. 2014;111:18584–9.PubMedPubMedCentralCrossRefGoogle Scholar
  14. Porter S, Clark IM, Kevorkia L, Edwards DR. The ADAMTS metalloproteinases. Biochem J. 2005;386:15–27.PubMedPubMedCentralCrossRefGoogle Scholar
  15. Tsai HM. Physiologic cleavage of von Willebrand factor by a plasma protease is dependent on its conformation and requires calcium ion. Blood. 1996;87:4235–44.PubMedPubMedCentralGoogle Scholar
  16. Tsai HM, Sussman II, Ginsburg D, Lankhof H, Sixma JJ, Nagel RL. Proteolytic cleavage of recombinant type 2A von Willebrand factor mutants R834W and R834Q: inhibition by doxycycline and by monoclonal antibody VP-1. Blood. 1997;89:1954–62.PubMedPubMedCentralGoogle Scholar
  17. Turner NA, Nolasco L, Ruggeri ZM, Moake JL. Endothelial cell ADAMTS-13 and VWF: production, release, and VWF string cleavage. Blood. 2009;114:5102–11.PubMedPubMedCentralCrossRefGoogle Scholar
  18. Uemura M, Tatsumi K, Matsumoto M, Fujimoto M, Matsuyama T, Ishikawa M, et al. Localization of ADAMTS13 to the stellate cells of human liver. Blood. 2005;106:922–4.PubMedCrossRefGoogle Scholar
  19. Xiang Y, de Groot R, Crawley JT, Lane DA. Mechanism of von Willebrand factor scissile bond cleavage by a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13 (ADAMTS13). Proc Natl Acad Sci U S A. 2011;108:11602–7.PubMedPubMedCentralCrossRefGoogle Scholar
  20. Zheng X, Chung D, Takayama TK, Majerus EM, Sadler JE, Fujikawa K. Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura. J Biol Chem. 2001;276:41059–63.PubMedCrossRefGoogle Scholar
  21. Zheng X, Nishio K, Majerus EM, Sadler JE. Cleavage of von Willebrand factor requires the spacer domain of the metalloprotease ADAMTS13. J Biol Chem. 2003;278:30136–41.PubMedCrossRefGoogle Scholar

Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  • Christian R. Robinson
    • 1
    • 2
  • Ina Laura Pieper
    • 1
    • 2
  • Venkateswarlu Kanamarlapudi
    • 1
  1. 1.Institute of Life Science 1, School of MedicineSwansea UniversitySwanseaUK
  2. 2.Calon Cardio-Technology LtdInstitute of Life Science 2, Medical School, Swansea UniversitySwanseaUK