메뉴 건너뛰기




Volumn 73, Issue 4, 2009, Pages 1196-1202

Peroxiredoxin IV Protects Cells From Radiation-Induced Apoptosis in Head-and-Neck Squamous Cell Carcinoma

Author keywords

Apoptosis; Head and neck cancer; Peroxiredoxin IV; Radiation seisitivity; Reactive oxygen species

Indexed keywords

IONIZING RADIATION; OXYGEN;

EID: 61349110067     PISSN: 03603016     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijrobp.2008.10.070     Document Type: Article
Times cited : (24)

References (45)
  • 2
    • 0037379216 scopus 로고    scopus 로고
    • Manganese superoxide dismutase-mediated gene expression in radiation-induced adaptive responses
    • Guo G., Yan-Sanders Y., Lyn-Cook B.D., et al. Manganese superoxide dismutase-mediated gene expression in radiation-induced adaptive responses. Mol Cell Biol 23 (2003) 2362-2378
    • (2003) Mol Cell Biol , vol.23 , pp. 2362-2378
    • Guo, G.1    Yan-Sanders, Y.2    Lyn-Cook, B.D.3
  • 3
    • 0028630905 scopus 로고
    • Antioxidant defense mechanisms: A new thiol-specific antioxidant enzyme
    • Rhee S.G., Kim K.H., Chae H.Z., et al. Antioxidant defense mechanisms: A new thiol-specific antioxidant enzyme. Ann N Y Acad Sci 738 (1994) 86-92
    • (1994) Ann N Y Acad Sci , vol.738 , pp. 86-92
    • Rhee, S.G.1    Kim, K.H.2    Chae, H.Z.3
  • 4
    • 0002891986 scopus 로고    scopus 로고
    • Antioxidant mechanisms in radiation injury and radioprotection
    • Chow C.K. (Ed), CRC Press, Boca Raton, FL
    • Weiss J.F., and Kumar K.S. Antioxidant mechanisms in radiation injury and radioprotection. In: Chow C.K. (Ed). Cellular antioxidant defense mechanisms (1998), CRC Press, Boca Raton, FL 163-189
    • (1998) Cellular antioxidant defense mechanisms , pp. 163-189
    • Weiss, J.F.1    Kumar, K.S.2
  • 5
    • 0027394553 scopus 로고
    • Overexpression of mitochondrial manganese superoxide dismutase promotes the survival of tumor cells exposed to interleukin-1, tumor necrosis factor, selected anticancer drugs, and ionizing radiation
    • Hirose K., Longo D.L., Oppenheim J.J., and Matsushima K. Overexpression of mitochondrial manganese superoxide dismutase promotes the survival of tumor cells exposed to interleukin-1, tumor necrosis factor, selected anticancer drugs, and ionizing radiation. FASEB J 7 (1993) 361-368
    • (1993) FASEB J , vol.7 , pp. 361-368
    • Hirose, K.1    Longo, D.L.2    Oppenheim, J.J.3    Matsushima, K.4
  • 6
    • 0032030989 scopus 로고    scopus 로고
    • Role of antioxidant enzymes on ionizing radiation resistance
    • Sun J., Chen Y., Li M., and Ge Z. Role of antioxidant enzymes on ionizing radiation resistance. Free Radic Biol Med 24 (1998) 586-593
    • (1998) Free Radic Biol Med , vol.24 , pp. 586-593
    • Sun, J.1    Chen, Y.2    Li, M.3    Ge, Z.4
  • 7
    • 0028457620 scopus 로고
    • Role of manganese superoxide dismutase in radioprotection using gene transfer studies
    • Suresh A., Tung F., Moreb J., and Zucali J.R. Role of manganese superoxide dismutase in radioprotection using gene transfer studies. Cancer Gene Ther 1 (1994) 85-90
    • (1994) Cancer Gene Ther , vol.1 , pp. 85-90
    • Suresh, A.1    Tung, F.2    Moreb, J.3    Zucali, J.R.4
  • 8
    • 0037376674 scopus 로고    scopus 로고
    • Oxidant signals and oxidative stress
    • Finkel T. Oxidant signals and oxidative stress. Curr Opin Cell Biol 15 (2003) 247-254
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 247-254
    • Finkel, T.1
  • 9
    • 0029556333 scopus 로고
    • Resistance to ionizing radiation and antioxidative defence in yeasts. Are antioxidant-deficient cells permanently stressed?
    • Jaruga E., Lapshina E.A., Biliński T., et al. Resistance to ionizing radiation and antioxidative defence in yeasts. Are antioxidant-deficient cells permanently stressed?. Biochem. Mol Biol Int 37 (1995) 467-473
    • (1995) Biochem. Mol Biol Int , vol.37 , pp. 467-473
    • Jaruga, E.1    Lapshina, E.A.2    Biliński, T.3
  • 11
    • 0346340021 scopus 로고    scopus 로고
    • Thioredoxin system in premature and newborn biology
    • Das K.C. Thioredoxin system in premature and newborn biology. Antioxid Redox Signal 6 (2004) 177-184
    • (2004) Antioxid Redox Signal , vol.6 , pp. 177-184
    • Das, K.C.1
  • 12
    • 0036287739 scopus 로고    scopus 로고
    • Advances in our understanding of peroxiredoxin, a multifunctional mammalian redox protein
    • Fujii J., and Ikeda Y. Advances in our understanding of peroxiredoxin, a multifunctional mammalian redox protein. Redox Rep 7 (2002) 123-130
    • (2002) Redox Rep , vol.7 , pp. 123-130
    • Fujii, J.1    Ikeda, Y.2
  • 14
    • 27744456655 scopus 로고    scopus 로고
    • Involvement of peroxiredoxin I in protecting cells from radiation-induced death
    • Zhang B., Su Y., Ai G., et al. Involvement of peroxiredoxin I in protecting cells from radiation-induced death. J Radiat Res 46 (2005) 305-312
    • (2005) J Radiat Res , vol.46 , pp. 305-312
    • Zhang, B.1    Su, Y.2    Ai, G.3
  • 15
    • 28644438156 scopus 로고    scopus 로고
    • The role of peroxiredoxin II in radiation-resistant MCF-7 breast cancer cells
    • Wang T., Tamae D., LeBon T., et al. The role of peroxiredoxin II in radiation-resistant MCF-7 breast cancer cells. Cancer Res 65 (2005) 10338-10346
    • (2005) Cancer Res , vol.65 , pp. 10338-10346
    • Wang, T.1    Tamae, D.2    LeBon, T.3
  • 16
    • 13544263241 scopus 로고    scopus 로고
    • Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: A new insight into the peroxiredoxin oligomerism
    • Echalier A., Trivelli X., Corbier C., et al. Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: A new insight into the peroxiredoxin oligomerism. Biochemistry 44 (2005) 1755-1767
    • (2005) Biochemistry , vol.44 , pp. 1755-1767
    • Echalier, A.1    Trivelli, X.2    Corbier, C.3
  • 17
    • 0035844694 scopus 로고    scopus 로고
    • Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography
    • Harris J.R., Schroder E., Isupov M.N., et al. Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography. Biochim Biophys Acta 1547 (2001) 221-234
    • (2001) Biochim Biophys Acta , vol.1547 , pp. 221-234
    • Harris, J.R.1    Schroder, E.2    Isupov, M.N.3
  • 18
    • 0037064080 scopus 로고    scopus 로고
    • Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid
    • Yang K.S., Kang S.W., Woo H.A., et al. Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J Biol Chem 277 (2002) 38029-38036
    • (2002) J Biol Chem , vol.277 , pp. 38029-38036
    • Yang, K.S.1    Kang, S.W.2    Woo, H.A.3
  • 19
    • 0032843695 scopus 로고    scopus 로고
    • Oxidative stress-inducible proteins in macrophages
    • Ishii T., Itoh K., Sato H., and Bannai S. Oxidative stress-inducible proteins in macrophages. Free Radic Res 31 (1999) 351-355
    • (1999) Free Radic Res , vol.31 , pp. 351-355
    • Ishii, T.1    Itoh, K.2    Sato, H.3    Bannai, S.4
  • 20
    • 0042568938 scopus 로고    scopus 로고
    • Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression
    • Neumann C.A., Krause D.S., Carman C.V., et al. Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression. Nature 424 (2003) 561-565
    • (2003) Nature , vol.424 , pp. 561-565
    • Neumann, C.A.1    Krause, D.S.2    Carman, C.V.3
  • 21
    • 0032575488 scopus 로고    scopus 로고
    • Thioredoxin peroxidase (natural killer enhancing factor) regulation of activator protein-1 function in endothelial cells
    • Shau H., Huang A.C., Faris M., et al. Thioredoxin peroxidase (natural killer enhancing factor) regulation of activator protein-1 function in endothelial cells. Biochem Biophys Res Commun 249 (1998) 683-686
    • (1998) Biochem Biophys Res Commun , vol.249 , pp. 683-686
    • Shau, H.1    Huang, A.C.2    Faris, M.3
  • 22
    • 0025289049 scopus 로고
    • Free radicals, antioxidant enzymes and carcinogenesis
    • Sun Y. Free radicals, antioxidant enzymes and carcinogenesis. Free Radic Biol Med 8 (1990) 583-599
    • (1990) Free Radic Biol Med , vol.8 , pp. 583-599
    • Sun, Y.1
  • 23
    • 0028903502 scopus 로고
    • Thiol-mediated redox regulation of apoptosis. Possible roles of cellular thiols other than glutathione in T cell apoptosis
    • Sato N., Iwata S., Nakamura K., et al. Thiol-mediated redox regulation of apoptosis. Possible roles of cellular thiols other than glutathione in T cell apoptosis. J Immunol 154 (1995) 3194-3203
    • (1995) J Immunol , vol.154 , pp. 3194-3203
    • Sato, N.1    Iwata, S.2    Nakamura, K.3
  • 24
    • 1842295744 scopus 로고    scopus 로고
    • Regulatory role for a novel human thioredoxinperoxidase in NF-κB activation
    • Jin D.Y., Chae H.Z., Rhee S.G., and Jeang K.T. Regulatory role for a novel human thioredoxinperoxidase in NF-κB activation. J Biol Chem 272 (1997) 30952-30961
    • (1997) J Biol Chem , vol.272 , pp. 30952-30961
    • Jin, D.Y.1    Chae, H.Z.2    Rhee, S.G.3    Jeang, K.T.4
  • 25
    • 0033734877 scopus 로고    scopus 로고
    • Characterization of human and mouse peroxiredoxin IV:evidence for inhibition by Prx-IV of epidermal growth factor- and p53-induced reactive oxygen species
    • Wong C.M., Chun A.C., Kok K.H., et al. Characterization of human and mouse peroxiredoxin IV:evidence for inhibition by Prx-IV of epidermal growth factor- and p53-induced reactive oxygen species. Antioxid Redox Signal 2 (2000) 507-518
    • (2000) Antioxid Redox Signal , vol.2 , pp. 507-518
    • Wong, C.M.1    Chun, A.C.2    Kok, K.H.3
  • 26
    • 61349157404 scopus 로고    scopus 로고
    • Proteomic analysis of two head and neck cancer cell lines presenting different radiation sensitivity
    • Lee Y.S., Chang H.W., Jeong J.E., et al. Proteomic analysis of two head and neck cancer cell lines presenting different radiation sensitivity. Acta Otolaryngol 4 (2007) 1-7
    • (2007) Acta Otolaryngol , vol.4 , pp. 1-7
    • Lee, Y.S.1    Chang, H.W.2    Jeong, J.E.3
  • 27
    • 0011002606 scopus 로고    scopus 로고
    • Establishment and characterization of nine new head and neck cancer cell lines
    • Kim S.Y., Chu K.C., Lee H.R., et al. Establishment and characterization of nine new head and neck cancer cell lines. Acta Otolaryngol 117 (1997) 775-784
    • (1997) Acta Otolaryngol , vol.117 , pp. 775-784
    • Kim, S.Y.1    Chu, K.C.2    Lee, H.R.3
  • 28
    • 16244371725 scopus 로고    scopus 로고
    • Chemoradiation after surgery for high-risk head and neck cancer patients: How strong is the evidence?
    • Bernier J., and Cooper J.S. Chemoradiation after surgery for high-risk head and neck cancer patients: How strong is the evidence?. Oncologist 10 (2005) 215-224
    • (2005) Oncologist , vol.10 , pp. 215-224
    • Bernier, J.1    Cooper, J.S.2
  • 29
    • 0034651902 scopus 로고    scopus 로고
    • Mature results of a phase III randomized trial comparing concurrent chemoradiotherpy with radiation therapy alone in patients with stage III and IV squamous cell carcinoma of the head and neck
    • Adelstein D.J., Lavertu P., Saxton J.P., et al. Mature results of a phase III randomized trial comparing concurrent chemoradiotherpy with radiation therapy alone in patients with stage III and IV squamous cell carcinoma of the head and neck. Cancer 88 (2000) 876-883
    • (2000) Cancer , vol.88 , pp. 876-883
    • Adelstein, D.J.1    Lavertu, P.2    Saxton, J.P.3
  • 30
    • 0034681783 scopus 로고    scopus 로고
    • Chemotherapy added to locoregional treatment for head and neck squamous-cell carcinoma: Three meta-analyses of updated individual data. MACH-NC Collaborative group. Meta-analysis of Chemotherapy on Head and Neck Cancer
    • Pignon J.P., Bourhis J., Domenege C., and Designé L. Chemotherapy added to locoregional treatment for head and neck squamous-cell carcinoma: Three meta-analyses of updated individual data. MACH-NC Collaborative group. Meta-analysis of Chemotherapy on Head and Neck Cancer. Lancet 355 (2000) 949-955
    • (2000) Lancet , vol.355 , pp. 949-955
    • Pignon, J.P.1    Bourhis, J.2    Domenege, C.3    Designé, L.4
  • 31
    • 0141673128 scopus 로고    scopus 로고
    • Biological chemistry of reactive oxygen and nitrogen and radiation-induced signal transduction mechanisms
    • Mikkelsen R.B., and Wardman P. Biological chemistry of reactive oxygen and nitrogen and radiation-induced signal transduction mechanisms. Oncogene 22 (2003) 5734-5754
    • (2003) Oncogene , vol.22 , pp. 5734-5754
    • Mikkelsen, R.B.1    Wardman, P.2
  • 32
    • 0036923274 scopus 로고    scopus 로고
    • Role of reactive oxygen species in cells overexpressing manganese superoxide dismutase: Mechanism for induction of radioresistance
    • Takada Y., Hachiya M., Park S.H., et al. Role of reactive oxygen species in cells overexpressing manganese superoxide dismutase: Mechanism for induction of radioresistance. Mol Cancer Res 1 (2002) 137-146
    • (2002) Mol Cancer Res , vol.1 , pp. 137-146
    • Takada, Y.1    Hachiya, M.2    Park, S.H.3
  • 33
    • 0034490213 scopus 로고    scopus 로고
    • Antisense of human peroxiredoxin II enhances radiation-induced cell death
    • Park S.H., Chung Y.M., Lee Y.S., et al. Antisense of human peroxiredoxin II enhances radiation-induced cell death. Clin Cancer Res 6 (2000) 4915-4920
    • (2000) Clin Cancer Res , vol.6 , pp. 4915-4920
    • Park, S.H.1    Chung, Y.M.2    Lee, Y.S.3
  • 34
    • 0037114781 scopus 로고    scopus 로고
    • Induction of radioprotective peroxiredoxin-I by ionizing irradiation
    • Chen W.C., McBride W.H., Iwamoto K.S., et al. Induction of radioprotective peroxiredoxin-I by ionizing irradiation. J Neurosci Res 70 (2002) 794-798
    • (2002) J Neurosci Res , vol.70 , pp. 794-798
    • Chen, W.C.1    McBride, W.H.2    Iwamoto, K.S.3
  • 35
    • 30544431972 scopus 로고    scopus 로고
    • Inhibition of lung tumor growth and augmentation of radiosensitivity by decreasing peroxiredoxin I expression
    • Chen M.F., Keng P.C., Shau H., et al. Inhibition of lung tumor growth and augmentation of radiosensitivity by decreasing peroxiredoxin I expression. Int J Radiat Oncol Biol Phys 64 (2006) 581-591
    • (2006) Int J Radiat Oncol Biol Phys , vol.64 , pp. 581-591
    • Chen, M.F.1    Keng, P.C.2    Shau, H.3
  • 36
    • 33751161235 scopus 로고    scopus 로고
    • p53 status is a major determinant of effects of decreasing peroxiredoxin I expression on tumor growth and response of lung cancer cells to treatment
    • Chen M.F., Chen W.C., Wu C.T., et al. p53 status is a major determinant of effects of decreasing peroxiredoxin I expression on tumor growth and response of lung cancer cells to treatment. Int J Radiat Oncol Biol Phys 66 (2006) 1461-1472
    • (2006) Int J Radiat Oncol Biol Phys , vol.66 , pp. 1461-1472
    • Chen, M.F.1    Chen, W.C.2    Wu, C.T.3
  • 37
    • 3142741615 scopus 로고    scopus 로고
    • PRDX4, a member of the peroxiredoxin family, is fused to AML1 (RUNX1) in an acute myeloid leukemia patient with a t(X;21)(p22;q22)
    • Zhang Y., Emmanuel N., Kamboj G., et al. PRDX4, a member of the peroxiredoxin family, is fused to AML1 (RUNX1) in an acute myeloid leukemia patient with a t(X;21)(p22;q22). Genes Chromosomes Cancer 40 (2004) 365-370
    • (2004) Genes Chromosomes Cancer , vol.40 , pp. 365-370
    • Zhang, Y.1    Emmanuel, N.2    Kamboj, G.3
  • 38
    • 0038122766 scopus 로고    scopus 로고
    • Molecular characterization of acute leukemias by use of microarray technology
    • Kohlmann A., Schoch C., Schnittger S., et al. Molecular characterization of acute leukemias by use of microarray technology. Genes Chromosomes Cancer 37 (2003) 396-405
    • (2003) Genes Chromosomes Cancer , vol.37 , pp. 396-405
    • Kohlmann, A.1    Schoch, C.2    Schnittger, S.3
  • 39
    • 3843146451 scopus 로고    scopus 로고
    • Peroxiredoxins, a novel protein family in lung cancer
    • Lehtonen S.T., Svensk A.M., Soini Y., et al. Peroxiredoxins, a novel protein family in lung cancer. Int J Cancer 111 (2004) 514-521
    • (2004) Int J Cancer , vol.111 , pp. 514-521
    • Lehtonen, S.T.1    Svensk, A.M.2    Soini, Y.3
  • 40
    • 0032557424 scopus 로고    scopus 로고
    • The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Evidence for the participation of reactive oxygen species in this mechanism
    • Kowaltowski A.J., Netto L.E., and Vercesi A.E. The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Evidence for the participation of reactive oxygen species in this mechanism. J Biol Chem 273 (1998) 12766-12769
    • (1998) J Biol Chem , vol.273 , pp. 12766-12769
    • Kowaltowski, A.J.1    Netto, L.E.2    Vercesi, A.E.3
  • 41
    • 0034640460 scopus 로고    scopus 로고
    • Catalases and thioredoxin peroxidase protect Saccharomyces cerevisiae against Ca(2+)-induced mitochondrial membrane permeabilization and cell death
    • Kowaltowski A.J., Vercesi A.E., Rhee S.G., and Netto L.E. Catalases and thioredoxin peroxidase protect Saccharomyces cerevisiae against Ca(2+)-induced mitochondrial membrane permeabilization and cell death. FEBS Lett 473 (2000) 177-182
    • (2000) FEBS Lett , vol.473 , pp. 177-182
    • Kowaltowski, A.J.1    Vercesi, A.E.2    Rhee, S.G.3    Netto, L.E.4
  • 43
    • 0037076433 scopus 로고    scopus 로고
    • The c-Myc target gene PRDX3 is required for mitochondrial homeostasis and neoplastic transformation
    • Wonsey D.R., Zeller K.I., and Dang C.V. The c-Myc target gene PRDX3 is required for mitochondrial homeostasis and neoplastic transformation. Proc Natl Acad Sci U S A 99 (2002) 6649-6654
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 6649-6654
    • Wonsey, D.R.1    Zeller, K.I.2    Dang, C.V.3
  • 44
    • 0037044804 scopus 로고    scopus 로고
    • Pag, a putative tumor suppressor, interacts with the Myc Box II domain of c-Myc and selectively alters its biological function and target gene expression
    • Mu Z.M., Yin X.Y., and Prochownik E.V. Pag, a putative tumor suppressor, interacts with the Myc Box II domain of c-Myc and selectively alters its biological function and target gene expression. J Biol Chem 277 (2002) 43175-43184
    • (2002) J Biol Chem , vol.277 , pp. 43175-43184
    • Mu, Z.M.1    Yin, X.Y.2    Prochownik, E.V.3
  • 45
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Wood Z.A., Poole L.B., and Karplus P.A. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300 (2003) 650-653
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.