Inhibition of Cysteine and Serine Proteinases by the Cowpox Virus Serpin CRMA

  • Tomoko Komiyama
  • Long T. Quan
  • Guy S. Salvesen
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 389)

Abstract

Interleukin lß converting enzyme (ICE) is the founding member of a family of cysteine proteinases active in the metabolism of intracellular proteins [1]. Other members of this family include Ich-1, CPP32, Ced-3, all of which have been implicated in apoptosis (programmed cell death) [2–4]. Though ICE itself may also be involved in apoptosis, its main role is probably to activate pro-interleukin-lß (proIL-lß) via specific cleavage following Asp residues [1,5].

Keywords

Urea Cysteine Serine Streptomyces Hunt 

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Reference

  1. 1.
    Thornberry, N. A. and Molineaux, S. M. (1995) Protein Science 4: 3–12.PubMedCrossRefGoogle Scholar
  2. 2.
    Wang, L., Miura, M., Bergeron, L., Zhu, H. & Yuan, J. (1994) Cell 78: 739–750.PubMedCrossRefGoogle Scholar
  3. 3.
    Fernandes-Alnemri, T., Litwack, G. & Alnemri, E. S. (1994) J. Biol. Chem. 269:30761–30764.PubMedGoogle Scholar
  4. 4.
    Yuan, J., Shaham, S., Ledoux, S., Ellis, H. M. & Horvitz, H. R. (1993) Cell 75: 653–660.PubMedCrossRefGoogle Scholar
  5. Kuida, K., Lippke, J. A., Ku, G., Harding, M. W., Livingston, D. J., Su, M. S.-S. & Flavell. R. A. (1995) Science 267:2000–2003.PubMedCrossRefGoogle Scholar
  6. 6.
    Ray, C. A., Black, R. A., Kronheim, S. R., Greenstreet, T. A., Salvesen, G. S. & Pickup, D. J. (1992) Cell 69: 597–604.PubMedCrossRefGoogle Scholar
  7. 7.
    Komiyama, T., Ray, C. A., Pickup, D. J., Howard, A. D., Thornberry, N. A., Peterson, E. P. & Salvesen, G. (1994) J. Biol. Chem. 269:19331–19337.PubMedGoogle Scholar
  8. 8.
    Pickup, D. J., Ink, B. S., Hu, W., Ray, C. A. & Joklik, W. K. (1986) Proc. Natl. Acad. Sci. USA 83:7698–7702.CrossRefGoogle Scholar
  9. 9.
    Huber, R. and Carrell, R. W. (1989) Biochemistry 28:8951–8971.PubMedCrossRefGoogle Scholar
  10. 10.
    Potempa, J., Korzus, E. and Travis, J. (1994) J. Biol. Chem. 269:15957–15960.PubMedGoogle Scholar
  11. 11.
    Carrell, R. W. and Boswell, D. R. (1986) in Proteinase Inhibitors (Barrett, A. J., and Salvesen, G., eds.) pp. 403–420 Elsevier Science Publishers, Amsterdam.Google Scholar
  12. 12.
    Travis, J. and Salvesen, G. S. (1983) Ann. Rev. Biochem. 52:655–709.PubMedCrossRefGoogle Scholar
  13. 13.
    Salvesen, G. and Enghild, J. J. (1993) in Acute Phase Proteins Molecular biology, biochemistry, and clinical applications (Mackiewicz, A., Kushner, I., and Baumann, H., eds.) pp. 117–147 CRC Press, Boca Raton.Google Scholar
  14. 14.
    Stein, P. E. and Carrell, R. W. (1995) Nature Structural Biology 2:96–113.PubMedCrossRefGoogle Scholar
  15. 15.
    Hunt, L. T. and Dayhoff, M. O. (1980) Biochem. Biophys. Res. Comm. 95:864–871.PubMedCrossRefGoogle Scholar
  16. 16.
    Flink, I. L., Bailey, T. J., Gustafson, T. A. & Markham, B. E. (1986) Proc. Natl. Acad. Sci. USA 83:7708–7712.CrossRefGoogle Scholar
  17. 17.
    Doolittle, R. F. (1983) Science 222:417–419.PubMedCrossRefGoogle Scholar
  18. 18.
    Remold-O’Donnell, E. (1993) FEBS Lett. 315:105–108.CrossRefGoogle Scholar
  19. 19.
    Pemberton, P. A., Stein, P. E., Pepys, M. B., Potter, J. M. & Carrell, R. W. (1988) Nature 336:257–258.PubMedCrossRefGoogle Scholar
  20. 20.
    Stein, P. E., Tewkesbury, D. A. & Carrell, R. W. (1989) Biochem. J. 262:103–107.PubMedGoogle Scholar
  21. 21.
    Potempa, J., Fedak, D., Dubin, A., Mast, A. & Travis, J. (1991) J. Biol. Chem. 266:21482–21487.PubMedGoogle Scholar
  22. 22.
    Mast, A. E., Enghild, J. J. & Salvesen, G. (1992) Biochemistry 31:2720–2728.PubMedCrossRefGoogle Scholar
  23. 23.
    Mast, A. E., Enghild, J. J., Pizzo, S. V. & Salvesen, G. (1991) Biochemistry 30:1723–1730PubMedCrossRefGoogle Scholar
  24. 24.
    Carrell, R. W. and Owen, M. C. (1986) Nature 322:730–732.CrossRefGoogle Scholar
  25. 25.
    Schulze, A. J., Huber, R., Degryse, E., Speck, D. & Bischoff, R. (1991) Eur. J. Biochem. 202:1147–1155.PubMedCrossRefGoogle Scholar
  26. 26.
    Davis, A. E. I., Aulak, K., Parad, R. B., Stecklein, H. R., Eldering, E., Hack, C. E., Kramer, J., Strunk, R. C., Bissler, J. & Rosen, F. S. (1992) Nature Genetics 1:354–358.PubMedCrossRefGoogle Scholar
  27. 27.
    Hood, D. B., Huntington, J. A. & Gettins, P. G. W. (1994) Biochemistry 33:8538–8547.PubMedCrossRefGoogle Scholar
  28. 28.
    Remold-O’Donnell, E., Chin, J. & Alberts, M. (1992) Proc. Natl. Acad. Sci. USA 89:5635–5639.CrossRefGoogle Scholar
  29. 29.
    Dubin, A., Travis, J., Enghild, J. J. & Potempa, J. (1992) J. Biol. Chem. 267:6576–6583.PubMedGoogle Scholar
  30. 30.
    Suminami, Y., Kishi, F., Sekiguchi, K. & Kato, H. (1991) Biochim. Biophys. Commun. 181:51–58.CrossRefGoogle Scholar
  31. 31.
    Morgenstern, K. A., Henzel, W. J., Baker, J. B., Wong, S. & Pastuszyn, A. (1993) J. Biol. Chem. 268:21560–21568.PubMedGoogle Scholar
  32. 32.
    Patston, P. A., Gettins, P., Beechem, J. & Schapira, M. (1991) Biochemistry 30:8876–8882.PubMedCrossRefGoogle Scholar
  33. 33.
    Patston, P. A. (1995) Inflammation 19:75–81.PubMedCrossRefGoogle Scholar
  34. 34.
    Schechter, N. M., Jordan, L. M., James, A. M., Cooperman, B., Wang, Z. M. & Rubin, H. (1993) J. Biol. Chem. 268:23626–23633.PubMedGoogle Scholar
  35. 35.
    Enghild, J. J., Valnickova, Z., Thorgersen, I. B., Pizzo, S. V. & Salvesen, G. (1993) Biochem. J. 291:933–938.PubMedGoogle Scholar
  36. 36.
    Quan, L. T., Caputo, A., Bleakley, R. C., Pickup, J. P. & Salvesen, G. S. (1995) J. Biol. Chem. 270: 10377–10379.PubMedCrossRefGoogle Scholar
  37. 37.
    Salvesen, G. (1994) in Proteolysis and Protein Turnover (Bond, J. S. and Barrett, A. J., eds.) pp. 57–63 Portland Press, London and Chapel Hill.Google Scholar
  38. 38.
    Wilson, K. R., Black, J.-A. F., Thompson, J. A., Kim, E. E., Griffith, J. P., Navia, M. A., Murcko, M. A., Chambers, S. P., Aldape, R. A., Raybuck, S. A. & Livingston, D. J. (1994) Nature 370:270–273.PubMedCrossRefGoogle Scholar
  39. 39.
    Walker, N. P. C., Talanian, R. V., Brady, K. D., Dang, L. C., Bump, N. J., Ferenz, C. R., Franklin, S., Ghayur, T., Hackett, M. C., Hammiii, L. D., Herzog, L., Huguin, M., Houy, W., Mankovich, J. A., McGuiness, L., Oriewicz, E., Paskind, M., Pratt, C. A., Reis, R, Summan, A., Terranova, M., Weich, J. P., Xiong, L., Moller, A., Tracey, D. E., Kamen, R. & Wong, W. W. (1994) Cell 78: 343–3522.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • Tomoko Komiyama
    • 1
  • Long T. Quan
    • 1
  • Guy S. Salvesen
    • 1
  1. 1.Department of PathologyDuke University Medical CenterDurhamUSA

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