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Article

Protein Kinase C δ Activates Topoisomerase IIα To Induce Apoptotic Cell Death in Response to DNA Damage

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Pages 3414-3431 | Received 17 Jan 2006, Accepted 03 Feb 2006, Published online: 27 Mar 2023

REFERENCES

  • Akimitsu, N., K. Kamura, S. Tone, A. Sakaguchi, A. Kikuchi, H. Hamamoto, and K. Sekimizu. 2003. Induction of apoptosis by depletion of DNA topoisomerase IIα in mammalian cells. Biochem. Biophys. Res. Commun. 307:301–307.
  • Bharti, A., S. K. Kraeft, M. Gounder, P. Pandey, S. Jin, Z. M. Yuan, S. P. Lees-Miller, R. Weichselbaum, D. Weaver, L. B. Chen, D. Kufe, and S. Kharbanda. 1998. Inactivation of DNA-dependent protein kinase by protein kinase Cδ: implications for apoptosis. Mol. Cell. Biol. 18:6719–6728.
  • Blass, M., I. Kronfeld, G. Kazimirsky, P. M. Blumberg, and C. Brodie. 2002. Tyrosine phosphorylation of protein kinase Cδ is essential for its apoptotic effect in response to etoposide. Mol. Cell. Biol. 22:182–195.
  • Castedo, M., J. L. Perfettini, T. Roumier, K. Andreau, R. Medema, and G. Kroemer. 2004. Cell death by mitotic catastrophe: a molecular definition. Oncogene 23:2825–2837.
  • Chen, A. Y., and L. F. Liu. 1994. DNA topoisomerases: essential enzymes and lethal targets. Annu. Rev. Pharmacol. Toxicol. 34:191–218.
  • DeVries, T. A., M. C. Neville, and M. E. Reyland. 2002. Nuclear import of PKCδ is required for apoptosis: identification of a novel nuclear import sequence. EMBO J. 21:6050–6060.
  • Dignam, J. D., R. M. Lebovitz, and R. G. Roeder. 1983. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1475–1489.
  • Downes, C. S., D. J. Clarke, A. M. Mullinger, J. F. Gimenez-Abian, A. M. Creighton, and R. T. Johnson. 1994. A topoisomerase II-dependent G2 cycle checkpoint in mammalian cells. Nature 372:467–470.
  • Earnshaw, W. C., B. Halligan, C. A. Cooke, M. M. Heck, and L. F. Liu. 1985. Topoisomerase II is a structural component of mitotic chromosome scaffolds. J. Cell Biol. 100:1706–1715.
  • Emoto, Y., H. Kisaki, Y. Manome, S. Kharbanda, and D. Kufe. 1996. Activation of protein kinase Cδ in human myeloid leukemia cells treated with 1-β-d-arabinofuranosylcytosine. Blood 87:1990–1996.
  • Emoto, Y., Y. Manome, G. Meinhardt, H. Kisaki, S. Kharbanda, M. Robertson, T. Ghayur, W. W. Wong, R. Kamen, R. Weichselbaum, and D. Kufe. 1995. Proteolytic activation of protein kinase C δ by an ICE-like protease in apoptotic cells. EMBO J. 14:6148–6156.
  • Figeys, D., L. D. McBroom, and M. F. Moran. 2001. Mass spectrometry for the study of protein-protein interactions. Methods 24:230–239.
  • Fram, R. J., and D. W. Kufe. 1982. DNA strand breaks caused by inhibitors of DNA synthesis: 1-β-d-arabinofuranosylcytosine and aphidicolin. Cancer Res. 42:4050–4053.
  • Gasser, S. M., T. Laroche, J. Falquet, E. Boy de la Tour, and U. K. Laemmli. 1986. Metaphase chromosome structure. Involvement of topoisomerase II. J. Mol. Biol. 188:613–629.
  • Ghayur, T., M. Hugunin, R. V. Talanian, S. Ratnofsky, C. Quinlan, Y. Emoto, P. Pandey, R. Datta, Y. Huang, S. Kharbanda, H. Allen, R. Kamen, W. Wong, and D. Kufe. 1996. Proteolytic activation of protein kinase C δ by an ICE/CED 3-like protease induces characteristics of apoptosis. J. Exp. Med. 184:2399–2404.
  • Goswami, P. C., J. L. Roti Roti, and C. R. Hunt. 1996. The cell cycle-coupled expression of topoisomerase IIα during S phase is regulated by mRNA stability and is disrupted by heat shock or ionizing radiation. Mol. Cell. Biol. 16:1500–1508.
  • Griffiths, G., B. Garrone, E. Deacon, P. Owen, J. Pongracz, G. Mead, A. Bradwell, D. Watters, and J. Lord. 1996. The polyether bistratene A activates protein kinase C-δ and induces growth arrest in HL60 cells. Biochem. Biophys. Res. Commun. 222:802–808.
  • Gschwendt, M., H. J. Muller, K. Kielbassa, R. Zang, W. Kittstein, G. Rincke, and F. Marks. 1994. Rottlerin, a novel protein kinase inhibitor. Biochem. Biophys. Res. Commun. 199:93–98.
  • Heck, M. M., W. N. Hittelman, and W. C. Earnshaw. 1988. Differential expression of DNA topoisomerases I and II during the eukaryotic cell cycle. Proc. Natl. Acad. Sci. USA 85:1086–1090.
  • Kellner, U., M. Sehested, P. B. Jensen, F. Gieseler, and P. Rudolph. 2002. Culprit and victim—DNA topoisomerase II. Lancet Oncol. 3:235–243.
  • Kharbanda, S., A. Bharti, D. Pei, J. Wang, P. Pandey, R. Ren, R. Weichselbaum, C. T. Walsh, and D. Kufe. 1996. The stress response to ionizing radiation involves c-Abl-dependent phosphorylation of SHPTP1. Proc. Natl. Acad. Sci. USA 93:6898–6901.
  • Kim, H. D., A. Tomida, Y. Ogiso, and T. Tsuruo. 1999. Glucose-regulated stresses cause degradation of DNA topoisomerase IIα by inducing nuclear proteasome during G1 cell cycle arrest in cancer cells. J. Cell. Physiol. 180:97–104.
  • Kimura, K., M. Saijo, M. Ui, and T. Enomoto. 1994. Growth state- and cell cycle-dependent fluctuation in the expression of two forms of DNA topoisomerase II and possible specific modification of the higher molecular weight form in the M phase. J. Biol. Chem. 269:1173–1176.
  • Kitamura, K., K. Mizuno, A. Etoh, Y. Akita, A. Miyamoto, K. Nakayama, and S. Ohno. 2003. The second phase activation of protein kinase C δ at late G1 is required for DNA synthesis in serum-induced cell cycle progression. Genes Cells 8:311–324.
  • Koriyama, H., Z. Kouchi, T. Umeda, T. C. Saido, T. Momoi, S. Ishiura, and K. Suzuki. 1999. Proteolytic activation of protein kinase C δ and ε by caspase-3 in U937 cells during chemotherapeutic agent-induced apoptosis. Cell Signal. 11:831–838.
  • Kufe, D. W., P. P. Major, E. M. Egan, and G. P. Beardsley. 1980. Correlation of cytotoxicity with incorporation of ara-C into DNA. J. Biol. Chem. 255:8997–9000.
  • Leitges, M., M. Mayr, U. Braun, U. Mayr, C. Li, G. Pfister, N. Ghaffari-Tabrizi, G. Baier, Y. Hu, and Q. Xu. 2001. Exacerbated vein graft arteriosclerosis in protein kinase Cδ-null mice. J. Clin. Investig. 108:1505–1512.
  • McPherson, J. P., and G. J. Goldenberg. 1998. Induction of apoptosis by deregulated expression of DNA topoisomerase IIα. Cancer Res. 58:4519–4524.
  • Miyamoto, A., K. Nakayama, H. Imaki, S. Hirose, Y. Jiang, M. Abe, T. Tsukiyama, H. Nagahama, S. Ohno, S. Hatakeyama, and K. I. Nakayama. 2002. Increased proliferation of B cells and auto-immunity in mice lacking protein kinase Cδ. Nature 416:865–869.
  • Mo, Y. Y., K. A. Ameiss, and W. T. Beck. 1998. Overexpression of human DNA topoisomerase II α by fusion to enhanced green fluorescent protein. BioTechniques 25:1052–1057.
  • Nakajima, T., K. Morita, N. Ohi, T. Arai, N. Nozaki, A. Kikuchi, F. Osaka, F. Yamao, and K. Oda. 1996. Degradation of topoisomerase IIα during adenovirus E1A-induced apoptosis is mediated by the activation of the ubiquitin proteolysis system. J. Biol. Chem. 271:24842–24849.
  • Nishizuka, Y. 1988. The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature 334:661–665.
  • Salmena, L., V. Lam, J. P. McPherson, and G. J. Goldenberg. 2001. Role of proteasomal degradation in the cell cycle-dependent regulation of DNA topoisomerase IIα expression. Biochem. Pharmacol. 61:795–802.
  • Santiago-Walker, A. E., A. J. Fikaris, G. G. Kao, E. J. Brown, M. G. Kazanietz, and J. L. Meinkoth. 2005. Protein kinase C δ stimulates apoptosis by initiating G1 phase cell cycle progression and S phase arrest. J. Biol. Chem. 280:32107–32114.
  • Sugimoto, K., K. Yamada, M. Egashira, Y. Yazaki, H. Hirai, A. Kikuchi, and K. Oshimi. 1998. Temporal and spatial distribution of DNA topoisomerase II alters during proliferation, differentiation, and apoptosis in HL-60 cells. Blood 91:1407–1417.
  • Tanabe, K., Y. Ikegami, R. Ishida, and T. Andoh. 1991. Inhibition of topoisomerase II by antitumor agents bis(2,6-dioxopiperazine) derivatives. Cancer Res. 51:4903–4908.
  • Thielmann, H. W., and O. Popanda. 1998. Doxorubicin and gamma rays increase the level of DNA topoisomerase IIα in nuclei of normal and xeroderma pigmentosum fibroblasts. J. Cancer Res. Clin. Oncol. 124:355–366.
  • Wang, J. C. 2002. Cellular roles of DNA topoisomerases: a molecular perspective. Nat. Rev. Mol. Cell. Biol. 3:430–440.
  • Wang, J. C. 1996. DNA topoisomerases. Annu. Rev. Biochem. 65:635–692.
  • Woessner, R. D., M. R. Mattern, C. K. Mirabelli, R. K. Johnson, and F. H. Drake. 1991. Proliferation- and cell cycle-dependent differences in expression of the 170 kilodalton and 180 kilodalton forms of topoisomerase II in NIH-3T3 cells. Cell Growth Differ. 2:209–214.
  • Yoshida, K. and H. Liu, and Y. Miki. 2006. Protein kinase C δ regulates Ser46 phosphorylation of p53 tumor suppressor in the apoptotic response to DNA damage. J. Biol. Chem. 281:5734–5740.
  • Yoshida, K., S. Kharbanda, and D. Kufe. 1999. Functional interaction between SHPTP1 and the Lyn tyrosine kinase in the apoptotic response to DNA damage. J. Biol. Chem. 274:34663–34668.
  • Yoshida, K., K. Komatsu, H. G. Wang, and D. Kufe. 2002. c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein in response to DNA damage. Mol. Cell. Biol. 22:3292–3300.
  • Yoshida, K., and D. Kufe. 2001. Negative regulation of the SHPTP1 protein tyrosine phosphatase by protein kinase C δ in response to DNA damage. Mol. Pharmacol. 60:1431–1438.
  • Yoshida, K., Y. Miki, and D. Kufe. 2002. Activation of SAPK/JNK signaling by protein kinase Cδ in response to DNA damage. J. Biol. Chem. 277:48372–48378.
  • Yoshida, K., H. G. Wang, Y. Miki, and D. Kufe. 2003. Protein kinase Cδ is responsible for constitutive and DNA damage-induced phosphorylation of Rad9. EMBO J. 22:1431–1441.
  • Yoshida, K., R. Weichselbaum, S. Kharbanda, and D. Kufe. 2000. Role for Lyn tyrosine kinase as a regulator of stress-activated protein kinase activity in response to DNA damage. Mol. Cell. Biol. 20:5370–5380.
  • Yuan, Z. M., T. Utsugisawa, T. Ishiko, S. Nakada, Y. Huang, S. Kharbanda, R. Weichselbaum, and D. Kufe. 1998. Activation of protein kinase C δ by the c-Abl tyrosine kinase in response to ionizing radiation. Oncogene 16:1643–1648.

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