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Volumn 9, Issue 8, 2010, Pages 889-897

The epidermal growth factor receptor modulates DNA double-strand break repair by regulating non-homologous end-joining

Author keywords

A549 cells; Cetuximab; Epidermal growth factor receptor; Erlotinib; MAPK; Non homologous end joining

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; CETUXIMAB; EPIDERMAL GROWTH FACTOR RECEPTOR; ERLOTINIB; HISTONE H2AX; HISTONE H2AX GAMMA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; PROTEIN KINASE B; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 77955277480     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2010.05.005     Document Type: Article
Times cited : (108)

References (40)
  • 1
    • 63749086305 scopus 로고    scopus 로고
    • ErbB receptors and signaling pathways in cancer
    • Hynes N.E., MacDonald G. ErbB receptors and signaling pathways in cancer. Curr. Opin. Cell Biol. 2009, 21:177-184.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 177-184
    • Hynes, N.E.1    MacDonald, G.2
  • 2
    • 33746485766 scopus 로고    scopus 로고
    • Epidermal growth factor receptor targeting in cancer
    • Mendelsohn J., Baselga J. Epidermal growth factor receptor targeting in cancer. Semin. Oncol. 2006, 33:369-385.
    • (2006) Semin. Oncol. , vol.33 , pp. 369-385
    • Mendelsohn, J.1    Baselga, J.2
  • 4
    • 0032815618 scopus 로고    scopus 로고
    • Radiation-induced release of transforming growth factor alpha activates the epidermal growth factor receptor and mitogen-activated protein kinase pathway in carcinoma cells, leading to increased proliferation and protection from radiation-induced cell death
    • Dent P., Reardon D.B., Park J.S., et al. Radiation-induced release of transforming growth factor alpha activates the epidermal growth factor receptor and mitogen-activated protein kinase pathway in carcinoma cells, leading to increased proliferation and protection from radiation-induced cell death. Mol. Biol. Cell 1999, 10:2493-2506.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2493-2506
    • Dent, P.1    Reardon, D.B.2    Park, J.S.3
  • 5
    • 33747042839 scopus 로고    scopus 로고
    • Epidermal growth factor receptor and DNA double strand break repair: the cell's self-defence
    • Szumiel I. Epidermal growth factor receptor and DNA double strand break repair: the cell's self-defence. Cell Signal. 2006, 18:1537-1548.
    • (2006) Cell Signal. , vol.18 , pp. 1537-1548
    • Szumiel, I.1
  • 6
    • 28444453967 scopus 로고    scopus 로고
    • Inhibition of radiation-induced EGFR nuclear import by C225 (Cetuximab) suppresses DNA-PK activity
    • Dittmann K., Mayer C., Rodemann H.P. Inhibition of radiation-induced EGFR nuclear import by C225 (Cetuximab) suppresses DNA-PK activity. Radiother. Oncol. 2005, 76:157-161.
    • (2005) Radiother. Oncol. , vol.76 , pp. 157-161
    • Dittmann, K.1    Mayer, C.2    Rodemann, H.P.3
  • 7
    • 33746088022 scopus 로고    scopus 로고
    • Blockage of epidermal growth factor receptor-phosphatidylinositol 3-kinase-AKT signaling increases radiosensitivity of K-RAS mutated human tumor cells in vitro by affecting DNA repair
    • Toulany M., Kasten-Pisula U., Brammer I., et al. Blockage of epidermal growth factor receptor-phosphatidylinositol 3-kinase-AKT signaling increases radiosensitivity of K-RAS mutated human tumor cells in vitro by affecting DNA repair. Clin. Cancer Res. 2006, 12:4119-4126.
    • (2006) Clin. Cancer Res. , vol.12 , pp. 4119-4126
    • Toulany, M.1    Kasten-Pisula, U.2    Brammer, I.3
  • 8
    • 38049155945 scopus 로고    scopus 로고
    • Regulation of DNA double-strand break repair pathway choice
    • Shrivastav M., De Haro L.P., Nickoloff J.A. Regulation of DNA double-strand break repair pathway choice. Cell Res. 2008, 18:134-147.
    • (2008) Cell Res. , vol.18 , pp. 134-147
    • Shrivastav, M.1    De Haro, L.P.2    Nickoloff, J.A.3
  • 10
    • 6344234817 scopus 로고    scopus 로고
    • Genetic steps of mammalian homologous repair with distinct mutagenic consequences
    • Stark J.M., Pierce A.J., Oh J., Pastink A., Jasin M. Genetic steps of mammalian homologous repair with distinct mutagenic consequences. Mol. Cell Biol. 2004, 24:9305-9316.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 9305-9316
    • Stark, J.M.1    Pierce, A.J.2    Oh, J.3    Pastink, A.4    Jasin, M.5
  • 11
    • 47249095041 scopus 로고    scopus 로고
    • Hierarchy of nonhomologous end-joining, single-strand annealing and gene conversion at site-directed DNA double-strand breaks
    • Mansour W.Y., Schumacher S., Rosskopf R., et al. Hierarchy of nonhomologous end-joining, single-strand annealing and gene conversion at site-directed DNA double-strand breaks. Nucleic Acids Res. 2008, 36:4088-4098.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4088-4098
    • Mansour, W.Y.1    Schumacher, S.2    Rosskopf, R.3
  • 12
    • 11244280890 scopus 로고    scopus 로고
    • Involvement of poly(ADP-ribose) polymerase-1 and XRCC1/DNA ligase III in an alternative route for DNA double-strand breaks rejoining
    • Audebert M., Salles B., Calsou P. Involvement of poly(ADP-ribose) polymerase-1 and XRCC1/DNA ligase III in an alternative route for DNA double-strand breaks rejoining. J. Biol. Chem. 2004, 279:55117-55126.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55117-55126
    • Audebert, M.1    Salles, B.2    Calsou, P.3
  • 13
    • 43349088569 scopus 로고    scopus 로고
    • Distinct roles of XRCC4 and Ku80 in non-homologous end-joining of endonuclease- and ionizing radiation-induced DNA double-strand breaks
    • Schulte-Uentrop L., El-Awady R.A., Schliecker L., Willers H., Dahm-Daphi J. Distinct roles of XRCC4 and Ku80 in non-homologous end-joining of endonuclease- and ionizing radiation-induced DNA double-strand breaks. Nucleic Acids Res. 2008, 36:2561-2569.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2561-2569
    • Schulte-Uentrop, L.1    El-Awady, R.A.2    Schliecker, L.3    Willers, H.4    Dahm-Daphi, J.5
  • 14
    • 56449098784 scopus 로고    scopus 로고
    • Erlotinib attenuates homologous recombinational repair of chromosomal breaks in human breast cancer cells
    • Li L., Wang H., Yang E.S., Arteaga C.L., Xia F. Erlotinib attenuates homologous recombinational repair of chromosomal breaks in human breast cancer cells. Cancer Res. 2008, 68:9141-9146.
    • (2008) Cancer Res. , vol.68 , pp. 9141-9146
    • Li, L.1    Wang, H.2    Yang, E.S.3    Arteaga, C.L.4    Xia, F.5
  • 15
    • 66149094649 scopus 로고    scopus 로고
    • Pro-survival AKT and ERK signaling from EGFR and mutant EGFRvIII enhances DNA double-strand break repair in human glioma cells
    • Golding S.E., Morgan R.N., Adams B.R., Hawkins A.J., Povirk L.F., Valerie K. Pro-survival AKT and ERK signaling from EGFR and mutant EGFRvIII enhances DNA double-strand break repair in human glioma cells. Cancer Biol. Ther. 2009, 8:730-738.
    • (2009) Cancer Biol. Ther. , vol.8 , pp. 730-738
    • Golding, S.E.1    Morgan, R.N.2    Adams, B.R.3    Hawkins, A.J.4    Povirk, L.F.5    Valerie, K.6
  • 16
    • 33847066413 scopus 로고    scopus 로고
    • Extracellular signal-related kinase positively regulates ataxia telangiectasia mutated, homologous recombination repair, and the DNA damage response
    • Golding S.E., Rosenberg E., Neill S., Dent P., Povirk L.F., Valerie K. Extracellular signal-related kinase positively regulates ataxia telangiectasia mutated, homologous recombination repair, and the DNA damage response. Cancer Res. 2007, 67:1046-1053.
    • (2007) Cancer Res. , vol.67 , pp. 1046-1053
    • Golding, S.E.1    Rosenberg, E.2    Neill, S.3    Dent, P.4    Povirk, L.F.5    Valerie, K.6
  • 17
    • 49349094037 scopus 로고    scopus 로고
    • Involvement of Rad51 in cytotoxicity induced by epidermal growth factor receptor inhibitor (gefitinib, IressaR) and chemotherapeutic agents in human lung cancer cells
    • Ko J.C, Ciou S.C., Cheng C.M., et al. Involvement of Rad51 in cytotoxicity induced by epidermal growth factor receptor inhibitor (gefitinib, IressaR) and chemotherapeutic agents in human lung cancer cells. Carcinogenesis 2008, 29:1448-1458.
    • (2008) Carcinogenesis , vol.29 , pp. 1448-1458
    • Ko, J.C.1    Ciou, S.C.2    Cheng, C.M.3
  • 18
    • 33847061736 scopus 로고    scopus 로고
    • Erlotinib directly inhibits HER2 kinase activation and downstream signaling events in intact cells lacking epidermal growth factor receptor expression
    • Schaefer G., Shao L., Totpal K., Akita R.W. Erlotinib directly inhibits HER2 kinase activation and downstream signaling events in intact cells lacking epidermal growth factor receptor expression. Cancer Res. 2007, 67:1228-1238.
    • (2007) Cancer Res. , vol.67 , pp. 1228-1238
    • Schaefer, G.1    Shao, L.2    Totpal, K.3    Akita, R.W.4
  • 19
    • 59649128223 scopus 로고    scopus 로고
    • Impact of homologous recombination on individual cellular radiosensitivity
    • Koch K., Wrona A., Dikomey E., Borgmann K. Impact of homologous recombination on individual cellular radiosensitivity. Radiother. Oncol. 2009, 90:265-272.
    • (2009) Radiother. Oncol. , vol.90 , pp. 265-272
    • Koch, K.1    Wrona, A.2    Dikomey, E.3    Borgmann, K.4
  • 20
    • 0042632901 scopus 로고    scopus 로고
    • Pathways of DNA double-strand break repair during the mammalian cell cycle
    • Rothkamm K., Kruger I., Thompson L.H., Lobrich M. Pathways of DNA double-strand break repair during the mammalian cell cycle. Mol. Cell Biol. 2003, 23:5706-5715.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 5706-5715
    • Rothkamm, K.1    Kruger, I.2    Thompson, L.H.3    Lobrich, M.4
  • 21
    • 24744449739 scopus 로고    scopus 로고
    • Radiation-induced epidermal growth factor receptor nuclear import is linked to activation of DNA-dependent protein kinase
    • Dittmann K., Mayer C., Fehrenbacher B., et al. Radiation-induced epidermal growth factor receptor nuclear import is linked to activation of DNA-dependent protein kinase. J. Biol. Chem. 2005, 280:31182-31189.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31182-31189
    • Dittmann, K.1    Mayer, C.2    Fehrenbacher, B.3
  • 22
    • 0031891006 scopus 로고    scopus 로고
    • Physical interaction between epidermal growth factor receptor and DNA-dependent protein kinase in mammalian cells
    • Bandyopadhyay D., Mandal M., Adam L., Mendelsohn J., Kumar R. Physical interaction between epidermal growth factor receptor and DNA-dependent protein kinase in mammalian cells. J. Biol. Chem. 1998, 273:1568-1573.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1568-1573
    • Bandyopadhyay, D.1    Mandal, M.2    Adam, L.3    Mendelsohn, J.4    Kumar, R.5
  • 23
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein
    • Kubota Y., Nash R.A., Klungland A., Schar P., Barnes D.E., Lindahl T. Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein. EMBO J. 1996, 15:6662-6670.
    • (1996) EMBO J. , vol.15 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3    Schar, P.4    Barnes, D.E.5    Lindahl, T.6
  • 24
    • 33644858558 scopus 로고    scopus 로고
    • Condensin I interacts with the PARP-1-XRCC1 complex and functions in DNA single-strand break repair
    • Heale J.T., Ball A.R., Schmiesing J.A., et al. Condensin I interacts with the PARP-1-XRCC1 complex and functions in DNA single-strand break repair. Mol. Cell 2006, 21:837-848.
    • (2006) Mol. Cell , vol.21 , pp. 837-848
    • Heale, J.T.1    Ball, A.R.2    Schmiesing, J.A.3
  • 25
    • 0035846899 scopus 로고    scopus 로고
    • XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair
    • Whitehouse C.J., Taylor R.M., Thistlethwaite A., et al. XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair. Cell 2001, 104:107-117.
    • (2001) Cell , vol.104 , pp. 107-117
    • Whitehouse, C.J.1    Taylor, R.M.2    Thistlethwaite, A.3
  • 26
    • 0034769605 scopus 로고    scopus 로고
    • MAPK dependence of DNA damage repair: ionizing radiation and the induction of expression of the DNA repair genes XRCC1 and ERCC1 in DU145 human prostate carcinoma cells in a MEK1/2 dependent fashion
    • Yacoub A., Park J.S., Qiao L., Dent P., Hagan M.P. MAPK dependence of DNA damage repair: ionizing radiation and the induction of expression of the DNA repair genes XRCC1 and ERCC1 in DU145 human prostate carcinoma cells in a MEK1/2 dependent fashion. Int. J. Radiat. Biol. 2001, 77:1067-1078.
    • (2001) Int. J. Radiat. Biol. , vol.77 , pp. 1067-1078
    • Yacoub, A.1    Park, J.S.2    Qiao, L.3    Dent, P.4    Hagan, M.P.5
  • 27
    • 14944342130 scopus 로고    scopus 로고
    • Nonhomologous end-joining of site-specific but not of radiation-induced DNA double-strand breaks is reduced in the presence of wild-type p53
    • Dahm-Daphi J., Hubbe P., Horvath F., et al. Nonhomologous end-joining of site-specific but not of radiation-induced DNA double-strand breaks is reduced in the presence of wild-type p53. Oncogene 2005, 24:1663-1672.
    • (2005) Oncogene , vol.24 , pp. 1663-1672
    • Dahm-Daphi, J.1    Hubbe, P.2    Horvath, F.3
  • 28
    • 34447574977 scopus 로고    scopus 로고
    • Positional stability of single double-strand breaks in mammalian cells
    • Soutoglou E., Dorn J.F., Sengupta K., et al. Positional stability of single double-strand breaks in mammalian cells. Nat. Cell Biol. 2007, 9:675-682.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 675-682
    • Soutoglou, E.1    Dorn, J.F.2    Sengupta, K.3
  • 29
    • 0032861343 scopus 로고    scopus 로고
    • Megabase chromatin domains involved in DNA double-strand breaks in vivo
    • Rogakou E.P., Boon C., Redon C., Bonner W.M. Megabase chromatin domains involved in DNA double-strand breaks in vivo. J. Cell Biol. 1999, 146:905-916.
    • (1999) J. Cell Biol. , vol.146 , pp. 905-916
    • Rogakou, E.P.1    Boon, C.2    Redon, C.3    Bonner, W.M.4
  • 30
    • 27844576828 scopus 로고    scopus 로고
    • Huge differences in cellular radiosensitivity due to only very small variations in double-strand break repair capacity
    • Kasten-Pisula U., Tastan H., Dikomey E. Huge differences in cellular radiosensitivity due to only very small variations in double-strand break repair capacity. Int. J. Radiat. Biol. 2005, 81:409-419.
    • (2005) Int. J. Radiat. Biol. , vol.81 , pp. 409-419
    • Kasten-Pisula, U.1    Tastan, H.2    Dikomey, E.3
  • 31
    • 39749129748 scopus 로고    scopus 로고
    • Gefitinib radiosensitizes non-small cell lung cancer cells by suppressing cellular DNA repair capacity
    • Tanaka T., Munshi A., Brooks C., Liu J., Hobbs M.L., Meyn R.E. Gefitinib radiosensitizes non-small cell lung cancer cells by suppressing cellular DNA repair capacity. Clin. Cancer Res. 2008, 14:1266-1273.
    • (2008) Clin. Cancer Res. , vol.14 , pp. 1266-1273
    • Tanaka, T.1    Munshi, A.2    Brooks, C.3    Liu, J.4    Hobbs, M.L.5    Meyn, R.E.6
  • 32
    • 14744298238 scopus 로고    scopus 로고
    • Radiosensitization of Ras-mutated human tumor cells in vitro by the specific EGF receptor antagonist BIBX1382BS
    • Toulany M., Dittmann K., Baumann M., Rodemann H.P. Radiosensitization of Ras-mutated human tumor cells in vitro by the specific EGF receptor antagonist BIBX1382BS. Radiother. Oncol. 2005, 74:117-129.
    • (2005) Radiother. Oncol. , vol.74 , pp. 117-129
    • Toulany, M.1    Dittmann, K.2    Baumann, M.3    Rodemann, H.P.4
  • 33
    • 28444475478 scopus 로고    scopus 로고
    • Radioresistance of K-Ras mutated human tumor cells is mediated through EGFR-dependent activation of PI3K-AKT pathway
    • Toulany M., Dittmann K., Kruger M., Baumann M., Rodemann H.P. Radioresistance of K-Ras mutated human tumor cells is mediated through EGFR-dependent activation of PI3K-AKT pathway. Radiother. Oncol. 2005, 76:143-150.
    • (2005) Radiother. Oncol. , vol.76 , pp. 143-150
    • Toulany, M.1    Dittmann, K.2    Kruger, M.3    Baumann, M.4    Rodemann, H.P.5
  • 34
    • 20144377465 scopus 로고    scopus 로고
    • HER2 overexpression increases sensitivity to gefitinib, an epidermal growth factor receptor tyrosine kinase inhibitor, through inhibition of HER2/HER3 heterodimer formation in lung cancer cells
    • Hirata A., Hosoi F., Miyagawa M., et al. HER2 overexpression increases sensitivity to gefitinib, an epidermal growth factor receptor tyrosine kinase inhibitor, through inhibition of HER2/HER3 heterodimer formation in lung cancer cells. Cancer Res. 2005, 65:4253-4260.
    • (2005) Cancer Res. , vol.65 , pp. 4253-4260
    • Hirata, A.1    Hosoi, F.2    Miyagawa, M.3
  • 35
    • 2642570481 scopus 로고    scopus 로고
    • Sensitivity to gefitinib (Iressa, ZD1839) in non-small cell lung cancer cell lines correlates with dependence on the epidermal growth factor (EGF) receptor/extracellular signal-regulated kinase 1/2 and EGF receptor/Akt pathway for proliferation
    • Ono M, Hirata A., Kometani T., et al. Sensitivity to gefitinib (Iressa, ZD1839) in non-small cell lung cancer cell lines correlates with dependence on the epidermal growth factor (EGF) receptor/extracellular signal-regulated kinase 1/2 and EGF receptor/Akt pathway for proliferation. Mol. Cancer Ther. 2004, 3:465-472.
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 465-472
    • Ono, M.1    Hirata, A.2    Kometani, T.3
  • 36
    • 0029814271 scopus 로고    scopus 로고
    • A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor
    • Tzahar E., Waterman H., Chen X., et al. A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor. Mol. Cell Biol. 1996, 16:5276-5287.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 5276-5287
    • Tzahar, E.1    Waterman, H.2    Chen, X.3
  • 37
    • 0028302018 scopus 로고
    • ErbB3 is involved in activation of phosphatidylinositol 3-kinase by epidermal growth factor
    • Soltoff S.P., Carraway K.L., Prigent S.A., Gullick W.G., Cantley L.C. ErbB3 is involved in activation of phosphatidylinositol 3-kinase by epidermal growth factor. Mol. Cell Biol. 1994, 14:3550-3558.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 3550-3558
    • Soltoff, S.P.1    Carraway, K.L.2    Prigent, S.A.3    Gullick, W.G.4    Cantley, L.C.5
  • 38
    • 34547114987 scopus 로고    scopus 로고
    • Inhibition of phosphatidylinositol-3-OH kinase/Akt signaling impairs DNA repair in glioblastoma cells following ionizing radiation
    • Kao G.D., Jiang Z., Fernandes A.M., Gupta A.K., Maity A. Inhibition of phosphatidylinositol-3-OH kinase/Akt signaling impairs DNA repair in glioblastoma cells following ionizing radiation. J. Biol. Chem. 2007, 282:21206-21212.
    • (2007) J. Biol. Chem. , vol.282 , pp. 21206-21212
    • Kao, G.D.1    Jiang, Z.2    Fernandes, A.M.3    Gupta, A.K.4    Maity, A.5
  • 39
    • 51049105757 scopus 로고    scopus 로고
    • Targeting of AKT1 enhances radiation toxicity of human tumor cells by inhibiting DNA-PKcs-dependent DNA double-strand break repair
    • Toulany M., Kehlbach R., Florczak U., et al. Targeting of AKT1 enhances radiation toxicity of human tumor cells by inhibiting DNA-PKcs-dependent DNA double-strand break repair. Mol. Cancer Ther. 2008, 7:1772-1781.
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 1772-1781
    • Toulany, M.1    Kehlbach, R.2    Florczak, U.3
  • 40
    • 66249149058 scopus 로고    scopus 로고
    • EGFRvIII and DNA double-strand break repair: a molecular mechanism for radioresistance in glioblastoma
    • Mukherjee B., McEllin B., Camacho C.V., et al. EGFRvIII and DNA double-strand break repair: a molecular mechanism for radioresistance in glioblastoma. Cancer Res. 2009, 69:4252-4259.
    • (2009) Cancer Res. , vol.69 , pp. 4252-4259
    • Mukherjee, B.1    McEllin, B.2    Camacho, C.V.3


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