Advertisement

Proteolytic Cleavage of Poly(ADP-Ribose) Polymerase in Human Leukemia Cells Treated with Etoposide and other Cytotoxic Agents

  • Scott H. Kaufmann
  • Serge Desnoyers
  • Brian Talbot
  • Guy G. Poirier
Conference paper

Abstract

Poly(ADP-ribose) polymerase (pADPRp, EC 2.4.2.30) is a nuclear enzyme that catalyzes the transfer of ADP-ribose units from NAD to various protein acceptors (reviewed in 1, 2). The activity of pADPRp in vitro is markedly stimulated by nicked DNA (3, 4), Likewise, pADPRp activity increases when nicks and single-stranded DNA regions are generated in vivo during the repair of DNA damage caused by alkylating agents (5).

Keywords

Proteolytic Cleavage Human Leukemia Cell Line Acute Myelogenous Leukemia Cell Cell Exclude Trypan Blue Johns Hopkins Oncology 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Althaus, F.R., and Richter, C. (1987) ADP-ribosylation of proteins. Part I. Enzymology and biochemical significance. in Molecular Biology, Biochemistry and Biophysics, Vol. 37, Springer-Verlag, Berlin.Google Scholar
  2. 2.
    DeMurcia, G., Huletsky, A., and Poirier, G. G. (1988) Biochem. Cell Biol. 66: 626–635.CrossRefGoogle Scholar
  3. 3.
    Benjamin, R. C., and Gill, D. M. (1980) J. Biol. Chem. 255: 10502–10508.PubMedGoogle Scholar
  4. 4.
    Ohgushi, H., Yoshihara, K, and Kamiya, T. (1980) J. Biol. Chem. 255: 6205–6211.PubMedGoogle Scholar
  5. 5.
    Singh, N., Poirier, G. G., and Cerutti, P. A. (1985) EMBO J. 4: 1491–1494.PubMedGoogle Scholar
  6. 6.
    Adamietz, P., and Rudolph, A. (1984) J. Biol. Chem. 259: 6841–6846.PubMedGoogle Scholar
  7. 7.
    Adamietz, P. (1987) Eur. J. Biochem. 169: 365–372.PubMedCrossRefGoogle Scholar
  8. 8.
    Boulikas, T. (1988) EMBO J. 7: 57–67.PubMedGoogle Scholar
  9. 9.
    Poirier, G.G., de Murcia, G., Jongstra-Bilen, J., Niedergang, C., and Mandel, P. (1982) Proc. Nat. Acad. Sci. U.S.A. 79: 3423–3427.CrossRefGoogle Scholar
  10. 10.
    Ferro, A.M., and Olivera, B.M. (1984) J. Biol. Chem. 259: 547–554, 1984.PubMedGoogle Scholar
  11. 11.
    Darby, M. K., Schmitt, B., Jongstra-Bilen, J., and Vosberg, H.-P. (1985) EMBO J. 4: 2129–2134.PubMedGoogle Scholar
  12. 12.
    Jacobson, E. L., Meadows, R., and Measel, J. (1985) Carcinogenesis 6: 711–714.PubMedCrossRefGoogle Scholar
  13. 13.
    Durkacz, B.W., Irwin, J., and Shall, S. (1981) Eur. J. Biochem. 121: 65–69, 1981.PubMedCrossRefGoogle Scholar
  14. 14.
    Wintersberger, U., and Wintersberger, E. (1985) FEBS. Let. 188: 189–191.CrossRefGoogle Scholar
  15. 15.
    Berger, N. (1985) Radiation Res. 101: 4–15.PubMedCrossRefGoogle Scholar
  16. 16.
    Carson, D.A., Seto, S., Wasson, D.B., and Carrera, C.J. (1986) Exp. Cell Res. 164: 273–281.PubMedCrossRefGoogle Scholar
  17. 17.
    Gaal, J.C., Smith, K.R., and Pearson, C.K. (1987) Trends in Biochemical Sciences 12: 129–130.CrossRefGoogle Scholar
  18. 18.
    Das, S.K., and Berger, N.A. (1986) Biochem. Biophys. Res. Commun. 137: 1153–1158.Google Scholar
  19. 19.
    Ikejima, M., Nogushi, S., Yamashita, R., Ogura, T., Sugimura, T., Gill, D.M., and Miwa, M. (1990) J. Biol. Chem. 265: 21907–21913.PubMedGoogle Scholar
  20. 20.
    Berger, N.A., Berger, S.J., Sudar, D.C., and Distelhort, C.W. (1987) J. Clin. Invest. 79: 1558–1563.PubMedCrossRefGoogle Scholar
  21. 21.
    Kaufmann, S.H. (1989) Cancer Res. 49: 5870–5878.PubMedGoogle Scholar
  22. 22.
    Wyllie, A.H., Kerr, J.F.R., and Currie, A.R. (1980) Int. Rev. Cytology 68: 251–306.CrossRefGoogle Scholar
  23. 23.
    Wyllie, A.H. (1980). Nature 284: 555–556.PubMedCrossRefGoogle Scholar
  24. 24.
    Lamarre, D., Talbot, B., de Murcia, G., Laplante, C., Leduc, Y., Mazen, A., and Poirier, G.G. (1988) Biochim. Biophys. Acta 950: 147–160.PubMedCrossRefGoogle Scholar
  25. 25.
    Simonin, F., Menissier-de Murcia, J., Poch, O., Muller, S., Gradwohl, G., Molinete, M., Penning, C, Keith, G., and de Murcia, G. (1990) J. Biol. Chem. 265: 19249–19256, 1990.PubMedGoogle Scholar
  26. 26.
    Kameshita, I., Masuda, Z., Taniguschi, T., and Shizuta, Y. (1984) J. Biol. Chem. 259: 4770–4776, 1984.PubMedGoogle Scholar
  27. 27.
    Smith, G.K., Duch, D.S., Dev, I.K, Banks, S.D., and Kaufmann, S.H. (1991) Submitted.Google Scholar
  28. 28.
    Lockshin, R.A., and Zakeri, Z.F. (1990) J. Gerontology 45: B135–140.CrossRefGoogle Scholar
  29. 29.
    Wylie, A.H., Morris, R.G., Smith, A.L., and Dunlop, D. (1984) J. Pathol. 142: 67–77.CrossRefGoogle Scholar
  30. 30.
    Vedekis, W.V., and Bradshaw, H.D., Jr. (1983) Mol. Cell, Endocrinol. 30: 215–227.CrossRefGoogle Scholar
  31. 31.
    Wielckens, K., Delfs, T., Muth, A., Freese, V., and Kleeberg, H.J. (1987) J. Steroid Biochem. 27: 413–419, 1987.PubMedCrossRefGoogle Scholar
  32. 32.
    Waring, P. (1990) J. Biol. Chem. 265: 14476–14480.PubMedGoogle Scholar
  33. 33.
    Kameshita, I., Mitsuuchi, Y., Matsuda, M., and Shizuta, Y. (1989) in ADP-ribose Transfer Reactions. Mechanisms and Biological Significance. M. K. Jacobson and E. L. Jacobson, eds. Springer-Verlag, New York, pp. 71–75.CrossRefGoogle Scholar
  34. 34.
    Shimizu, T., Kubota, M., Tanizawa, A., Sano, H., Kasai, Y., Hashimoto, H., Akiyama, Y., and Mikawa, H. (1990) Biochem. Biophys. Res. Commun. 169: 1172–1177.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1992

Authors and Affiliations

  • Scott H. Kaufmann
    • 1
  • Serge Desnoyers
    • 2
  • Brian Talbot
    • 3
  • Guy G. Poirier
    • 2
  1. 1.The Johns Hopkins Oncology CenterBaltimoreUSA
  2. 2.Laboratory of Poly(ADP-ribose) Metabolism, Molecular Endocrinology Dept.Laval University Medical CenterSte-FoyCanada
  3. 3.Department of BiologyUniversity of SherbrookeSherbrookeCanada

Personalised recommendations