Skip to main content

Antithrombin III and Other Natural Inhibitors of Coagulation

  • Chapter
Advances in Hemostasis and Thrombosis

Part of the book series: Ettore Majorana International Science Series ((LIFESCI,volume 20))

  • 47 Accesses

Abstract

The presence of naturally occurring inhibitory proteins appears to be one of the major systems for controlling the activation sequence in coagulation and for limiting thrombin formation. Plasma proteins which have been characterized as inhibitors of coagulation enzymes and cofactors are listed in Table 1.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. D.M. Tellefsen, D.W. Majerus, and M.K. Blank, Heparin cofactor II. Purification and properties of a heparin-dependent inhibitor of thrombin in human plasma, J. Biol. Chem., 257: 2162–2169 (1982).

    Google Scholar 

  2. W.W. Fish and I. Bjork, Release of a two-chain form of anti-thrombin from the antithrombin-thrombin complex, Eur. J. Biochem., 101: 31–38 (1979).

    Article  Google Scholar 

  3. S. Radoff and I. Danishefsky, High-affinity heparin: chain length, affinity for antithrombin and anticoagulant activity, Arch. Biochem. & Biophy., 215: 163–170 (1982).

    Article  Google Scholar 

  4. D.P. Thomas, J.W. Barrowcliffe, R.E. Merton, J. Stocks, J. Dawes, and D.S. Pepper, In vivo release of antiXa clotting activity by a heparin analogue, Thromb. Res., 17: 831–840 (1980).

    Article  Google Scholar 

  5. G. Sas, D.S. Pepper, and J.D. Cash, Plasma and serum anti-thrombin III differentiation by crossed immunoelectrophoresis, Thromb. Res., 6: 87–91 (1975).

    Article  Google Scholar 

  6. D.R. Ambruso, B.D. Leonard, R.D. Bies, L. Jacobson, W.E. Hathaway, and E.B. Reeve, Antithrombin III deficiency: decreased synthesis of a biochemically normal molecule, Blood, 60: 78–83 (1982).

    Google Scholar 

  7. G. Sas, I. Peto, D. Banhegyi, G. Blasko, and G. Domjan, Heterogeneity of the “classical” antithrombin III deficiency, Thromb. & Haemost., 43: 133–136 (1980).

    Google Scholar 

  8. T. Barbui and F. Rodeghiero, Hereditary dysfunctional antithrombin III, Thromb. & Haemost., 45: 97 (1981).

    Google Scholar 

  9. P.J. Sorensen, G. Sas, I. Peto, G. Blasko, T. Kremmer, and A. Samu, Distinction of two pathologic antithrombin III molecules: antithrombin III “Aalbor” and antithrombin III “Budapest,” Thromb. Res., 26: 211–219 (1982).

    Article  Google Scholar 

  10. C. Boyer, A. Tripodi, M. Wolf, P.M. Mannucci, and M.J. Larrieu, Antitrombina III Milano: una nuova variante qualitativa. Atti del VII Congresso Nazionale della Società Italiana per lo studio dell’Emostasi e delle Trombosi, Roma 18–20 Ottobre, p. 58 (1982).

    Google Scholar 

  11. T. Barbui, G. Finazzi, F. Rodeghiero, and E. Dini, Immunoelectrophoretic evidence of a thrombin-induced abnormality in a new variant of hereditary dysfunctional antithrombin III (AT III ‘Vicenza’), Br. J. Haematol., (in press).

    Google Scholar 

  12. T.H. Tran, H. Bounameaux, C. Bondeli, H. Honkanen, G.A. Marbert, and F. Duckert, Purification and partial characterization of a hereditary abnormal antithrombin III fraction of a patient with recurrent thrombophlebitis, Thromb. & Haemost., 44: 87–91 (1980).

    Google Scholar 

  13. E.B. Reeve, Steady state relations between factors X, Xa, II, IIa antithrombin III and alpha-2-macroglobulin in thrombosis, Thromb. Res., 18: 19–31 (1980).

    Article  ADS  Google Scholar 

  14. P.M. Mannucci, C. Boyer, M. Wolf, A. Tripodi, and M.J. Larrieu, Treatment of congenital antithrombin III deficiency with concentrates, Br. J. Haematol., 50: 531–535 (1982).

    Article  Google Scholar 

  15. H.G. Schipper, C.S.P. Jenkins, L.H. Kahle, and J.W. Ten Cate, Antithrombin III transfusion in disseminated intravascular coagulation, Lancet, ii: 854–856 (1978).

    Article  Google Scholar 

  16. R.A. Marlar and J.H. Griffin, Deficiency of protein C inhibitor in combined factor V/VIII disease, J. Clin. Invest., 66: 1186–1189 (1980).

    Article  Google Scholar 

  17. J.H. Griffin, B. Evatt, T.S. Zimmermann, A.J. Kleiss, and C. Wideman, Deficiency of protein C in congenital thrombotic disease, J. Clin. Invest., 68: 1370–1373 (1981).

    Article  Google Scholar 

  18. R.M. Bertina, A.W. Broekmans, I.K. Van Der Linden, and K. Mertens, Protein C deficiency in a Dutch family with thrombotic disease, Thromb. & Haemost., 48: 1–5 (1982).

    Google Scholar 

  19. P.M. Mannucci and S. Viganô, Deficiencies of protein C, and inhibitor of blood coagulation, Lancet, ii: 463–467 (1982).

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1985 Plenum Press, New York

About this chapter

Cite this chapter

Barbui, T., Finazzi, G. (1985). Antithrombin III and Other Natural Inhibitors of Coagulation. In: Cajozzo, A., Perricone, R., Di Marco, P., Palazzolo, P. (eds) Advances in Hemostasis and Thrombosis. Ettore Majorana International Science Series, vol 20. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9424-6_12

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-9424-6_12

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4615-9426-0

  • Online ISBN: 978-1-4615-9424-6

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics