Regulation of Vascular Fibrinolysis by Type 1 Plasminogen Activator Inhibitor

  • Dietmar Seiffert
  • Benien E. Van Aken
  • David J. Loskutoff
Chapter
Part of the GWUMC Department of Biochemistry Annual Spring Symposia book series (GWUN)

Abstract

Vascular hemostasis results from the regulated interaction of the coagulation and fibrinolytic systems. Any imbalance in these systems leads to a tendency to develop a bleeding diathesis or to an increased risk of thrombosis. Thrombotic events have been implicated in the pathogenesis of cardiovascular disease, including myocardial infarction and stroke. The recent success of thrombolytic therapy in acute myocardial infarction has drawn considerable attention to the role of the fibrinolytic system in vascular disease.

Keywords

Plasminogen Activator Plasminogen Activator Inhibitor Fibrinolytic System Plasminogen Activation Atherosclerotic Vascular Disease 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

  1. 1.
    J.H. Henkin, P. Marcotte, and H. Yang, The Plasminogen-Plasmin System. Progress in Cardiovascular Diseases. 34:135 (1991).PubMedCrossRefGoogle Scholar
  2. 2.
    K.C. Robbins, The plasminogen-plasmin enzyme system, in: “Haemostasis and Thrombosis,” R.W. Colman et al., eds., J.B. Lippincott Company, Philadelphia, Toronto (1987).Google Scholar
  3. 3.
    L.A. Liotta, R.H. Goldfarb, R. Brundage, G.P. Siegal, V. Terranova, and S. Garbisa, Effect of plasminogen activator (urokinase), plasmin, and thrombin on glycoprotein and collagneous components of basement membranes. Cancer Res. 41:4629 (1982).Google Scholar
  4. 4.
    J.L. Gross, D. Moscatelli, E.A. Jaffer, and D.B. Rifkin, Plasminogen activator and collagenase production by cultured capillary endothelial cells. Cell Biol. 95:974 (1982).CrossRefGoogle Scholar
  5. 5.
    K. Dano, P.A. Andreasen, J. Grondahl-Hansen, P. Kristensen, L.S. Nielsen, and L. Skriver, Plasminogen activators, tissue degradation, and cancer. Adv Cancer Res. 44:139 (1985).PubMedCrossRefGoogle Scholar
  6. 6.
    O. Saksela and D.B. Rifkin, Cell-associated plasminogen activation: Regulation and physiological functions. Ann Rev Cell Biol. 4:93 (1988).PubMedCrossRefGoogle Scholar
  7. 7.
    F. Bachmann, Plasminogen Activators, in: “Haemostasis and Thrombosis,” R.W. Colman et al., eds., Lippincott Company, Philadelphia-Toronto (1987).Google Scholar
  8. 8.
    M. Hoylaerts, D.C. Rijken, H.R. Linjen, and D. Collen, Kinetics of the activation of plasminogen by human tissue plasminogen activator: Role of fibrin. JBiol Chem. 257:2912 (1982).Google Scholar
  9. 9.
    P. Carmeliet, L. Schoonjans, L. Kieckens, B. Ream, J. Degen, R. Bronson, R. de Vos, J.J. van den Oord, D. Collen, and R.C. Mulligan, Physiological consequences of loss of plasminogen activator gene function in mice. Nature. 368:419 (1994).PubMedCrossRefGoogle Scholar
  10. 10.
    R.D. Gerard and R.S. Meidell, Regulation of tissue plasminogen activator expression. Annu Rev Physiol. 51:245 (1989).PubMedCrossRefGoogle Scholar
  11. 11.
    D.J. Loskutoff, Regulation of PAI-1 gene expression. Fibrinolysis. 5:197 (1991).Google Scholar
  12. 12.
    D.J. Loskutoff, M. Sawdey, and J. Mimuro, Type 1 plasminogen activator inhibitor. Prog Hemost Thromb. 9:87 (1989).PubMedGoogle Scholar
  13. 13.
    P. Carmeliet, L. Kieckens, L. Schoonjans, B. Ream, A. van Nuffelen, G. Prendergast, M. Cole, R. Bronson, D. Collen, and R.C. Mulligan, Plasminogen activator inhibitor-1 gene-deficient mice I. Generation by homologous recombination and characterization. J Clin Invest. 92:2746 (1993).PubMedCrossRefGoogle Scholar
  14. 14.
    P. Carmeliet, J.M. Stassen, L. Schoonjans, B. Ream, J.J. van den Oord, M. de Mol, R.C. Mulligan, and D. Collen, Plasminogen activator inhibitor-1 gene deficient mice II. Effects on Hemostasis, Thrombosis, and Thrombolysis. J Clin Invest. 92:2756 (1993).PubMedCrossRefGoogle Scholar
  15. 15.
    W.P. Fay, A.D. Shapiro, J.L. Shih, R.R. Schleef, and D. Ginsburg, Complete deficiency of plasminogen-activator inhibitor type 1 due to a frame-shift mutation. N Engl J Med. 327:1729 (1992).PubMedCrossRefGoogle Scholar
  16. 16.
    R.R. Schleef, D.L. Higgins, E. Pillemer, and L.J. Levitt, Bleeding diathesis due to decreased functional activity of type 1 plasminogen activator inhibitor. J Clin Invest. 83:1747 (1989).PubMedCrossRefGoogle Scholar
  17. 17.
    P.J. Declerk, M. de Mol, M.-C. Alessi, S. Baudner, E.-P. Paques, K.T. Preissner, G. Mueller-Berghaus, and D. Collen, Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma: Identification as a multimeric form of S protein (vitronectin). J Biol Chem 263:15454 (1988).Google Scholar
  18. 18.
    B. Wiman, T. Lindahi, and A. Almqvist, Evidence for a discrete binding protein of plasminogen activator inhibitor in plasma. Thromb Haemost. 59:392 (1988).PubMedGoogle Scholar
  19. 19.
    D. Seiffert and D.J. Loskutoff, Kinetic analysis of the interaction between type 1 plasminogen activator inhibitor and vitronectin and evidence that the bovine inhibitor binds to a thrombin-derived amino-terminal fragment of bovine vitronectin. Biochem Biophys Acta. 1078:23 (1991).PubMedCrossRefGoogle Scholar
  20. 20.
    D. Seiffert, N.N. Wagner, and D.J. Loskutoff, Serum-derived vitronectin influences the pericellular distribution of type 1 plasminogen activator inhibitor. J Cell Biol. 111:1283 (1990).PubMedCrossRefGoogle Scholar
  21. 21.
    K.T. Preissner, J. Grulich-Henn, H.J. Ehrlich, P. Declerck, C. Justus, D. Collen, H. Pannekoek, and G. Mueller-Berghaus, Structural requirements for the extracellular interaction of plasminogen activator inhibitor 1 with endothelial cell matrix-associated vitronectin. J Biol Chem. 265:18490 (1990).PubMedGoogle Scholar
  22. 22.
    B. Wiman and A. Hamsten, Impaired fibrinolyis and risk of thromboembolism. Progress in Cardiovascular Diseases. 34:179 (1991).PubMedCrossRefGoogle Scholar
  23. 23.
    M. Sawdey and D.J. Loskutoff, Regulation of murine type 1 plasminogen activator inhibitor gene expression in vivo. J Clin Invest. 88:1346 (1991).PubMedCrossRefGoogle Scholar
  24. 24.
    M. Keeton, Y. Eguchi, M. Sawdey, C. Ahn, and D.J. Loskutoff, Cellular localization of type 1 plasminogen activator inhibitor messenger RNA and protein in murine renal tissue. Am JPathol. 142:59 (1993).Google Scholar
  25. 25.
    J. Schneiderman, M. Sawdey, M. Keeton, G.M. Bordin, E.F. Bernstein, R.B. Dilley, and D.J. Loskutoff, Increased type 1 plasminogen activator inhibitor gene expression in atherosclerotic human arteries. Proc Nall Acad Sci USA. 89:6998 (1992).CrossRefGoogle Scholar
  26. 26.
    F. Lupu, G.E. Bergonzelli, D.A. Heim, E. Cousin, C.Y. Genton, F. Bachmann, and E.K.O. Kruithof, Localization and production of plasminogen activator inhibitor-1 in human healthy and atherosclerotic arteries. Arteriosclerosis and Thrombosis. 13:1090 (1993).PubMedCrossRefGoogle Scholar
  27. 27.
    F. Niculescu, H.G. Rus, D. Porutiu, V. Ghiurca, and R. Vlaicu, Immunoelectron-microscopic localization of S-protein/vitronectin in human atherosclerotic wall. Atherosclerosis. 78:197 (1989).PubMedCrossRefGoogle Scholar
  28. 28.
    C. Guettier, N. Hinglais, P. Bruneval, M. Kazatchkine, J. Bariety, and J.-P. Camilleri, Immunohistochemical localization of S protein/vitronectin in human atherosclerotic versus arteriosclerotic arteries. Virchows Archiv A Pathol Anat. 414:309 (1989).CrossRefGoogle Scholar
  29. 29.
    R. Sato, Y. Komme, T. Imanaka, T. Takano. Monoclonal antibody EMR1 a/212D recognizing site of deposition of extracellular lipid in atherosclerosis. Isolation and Characterization of a cDNA clone for the antigen. J Biol Chem. 265:21232 (1990).PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Dietmar Seiffert
    • 1
  • Benien E. Van Aken
    • 1
  • David J. Loskutoff
    • 1
  1. 1.Department of Vascular BiologyThe Scripps Research InstituteLa JollaUSA

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