Seminars in Hematology
Volume 41, Issue 1 , Pages 15-23 , January 2004

Cleavage of von Willebrand factor by ADAMTS-13 on endothelial cells

  • José A López

      Affiliations

    • Corresponding Author InformationAddress correspondence to José A. López, MD, Thrombosis Research Section, Department of Medicine, BCM286, N1319, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA
    • Division of Thrombosis Research, Department of Medicine, Baylor College of Medicine, Houston, TX, USA
    • ,
  • Jing-fei Dong

      Affiliations

    • Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USA

References 

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  2. Dent JA, Galbusera M, Ruggeri ZM. Heterogeneity of plasma von Willebrand factor multimers resulting from proteolysis of the constituent subunit. J Clin Invest. 1991;88:774–782
  3. Furlan M. Von Willebrand factor (Molecular size and functional activity). Ann Hematol. 1996;72:341–348
  4. Sadler JE. Biochemistry and genetics of von Willebrand factor. Annu Rev Biochem. 1998;67:395–424
  5. Moake JL, Turner NA, Stathopoulos NA, Nolasco LH, Hellums JD. Involvement of large plasma von Willebrand factor (vWF) multimers and unusually large vWF forms derived from endothelial cells in shear stress-induced platelet aggregation. J Clin Invest. 1986;78:1456–1461
  6. Frangos JA, Moake JL, Nolasco L, Phillips MD, McIntire LV. Cryosupernatant regulates accumulation of unusually large vWF multimers from endothelial cells. Am J Physiol. 1989;256:H1635–H1644
  7. Arya M, Anvari B, Romo GM, Cruz MA, Dong JF, McIntire LV, et al.  Ultralarge multimers of von Willebrand factor form spontaneous high-strength bonds with the platelet glycoprotein Ib-IX complex (Studies using optical tweezers). Blood. 2002;99:3971–3977
  8. Borthakur G, Cruz MA, Dong JF, McIntire L, Li F, López JA, et al.  Sulfatides inhibit platelet adhesion to von Willebrand factor in flowing blood. J Thromb Haemost. 2003;1:1288–1295
  9. Dong JF, Moake JL, Nolasco L, Bernardo A, Arceneaux W, Shrimpton CN, et al.  ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions. Blood. 2002;100:4033–4039
  10. Savage B, Sixma JJ, Ruggeri ZM. Functional self-association of von Willebrand factor during platelet adhesion under flow. Proc Natl Acad Sci USA. 2002;99:425–430
  11. Padilla A, Moake J, Bernardo A, Ball C, Wang Y, Arya M, et al: P-selectin binds and anchors newly released ultra-large von Willebrand factor multimers to the endothelial cell surface. (submitted)
  12. Vu T-KH, Hung DT, Wheaton VI, Coughlin SR. Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell. 1991;64:1057–1068
  13. Coughlin SR. How the protease thrombin talks to cells. Proc Natl Acad Sci USA. 1999;96:11023–11027
  14. Dong JF, Moake JL, Bernardo A, Fujikawa K, Ball C, Nolasco L, et al.  ADAMTS-13 metalloprotease interacts with the endothelial cell-derived ultra-large von Willebrand factor. J Biol Chem. 2003;278:29633–29639
  15. 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;413:488–494
  16. Schneppenheim R, Budde U, Oyen F, Angerhaus D, Aumann V, Drewke E, et al.  von Willebrand factor cleaving protease and ADAMTS13 mutations in childhood TTP. Blood. 2003;101:1845–1850
  17. Zimmerman TS, Dent JA, Ruggeri ZM, Nannini LH. Subunit composition of plasma von Willebrand factor (Cleavage is present in normal individuals, increased in IIA and IIB von Willebrand disease, but minimal in variants with aberrant structure of individual oligomers (types IIC, IID, and IIE)). J Clin Invest. 1986;77:947–951
  18. Emsley J, Cruz M, Handin R, Liddington R. Crystal structure of the von Willebrand Factor A1 domain and implications for the binding of platelet glycoprotein Ib. J Biol Chem. 1998;273:10396–10401
  19. Bienkowska J, Cruz M, Atiemo A, Handin R, Liddington R. The von willebrand factor A3 domain does not contain a metal ion-dependent adhesion site motif. J Biol Chem. 1997;272:25162–25167
  20. Huizinga EG, Martijn vdP, Kroon J, Sixma JJ, Gros P. Crystal structure of the A3 domain of human von Willebrand factor (Implications for collagen binding). Structure. 1997;5:1147–1156
  21. Tsai HM, Sussman II, Nagel RL. Shear stress enhances the proteolysis of von Willebrand factor in normal plasma. Blood. 1994;83:2171–2179

☆ Supported by a Specialized Centers in Hemostatic and Thrombotic Diseases grant from the National Institutes of Health, no. P50 HL65967.

PII: S0037-1963(03)00269-5

doi: 10.1053/j.seminhematol.2003.10.004

Seminars in Hematology
Volume 41, Issue 1 , Pages 15-23 , January 2004

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