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Volumn 99, Issue 2, 2008, Pages 376-384

Histone deacetylase inhibitors enhance the chemosensitivity of tumor cells with cross-resistance to a wide range of DNA-damaging drugs

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCYSTEINE; ANTINEOPLASTIC AGENT; BLEOMYCIN; CISPLATIN; CYTARABINE; DOUBLE STRANDED DNA; DOXORUBICIN; ETOPOSIDE; FLUOROURACIL; HISTONE; HISTONE DEACETYLASE INHIBITOR; MITOMYCIN C; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; PACLITAXEL; REACTIVE OXYGEN METABOLITE; ROMIDEPSIN; SERINE; TOPOTECAN; VINCRISTINE;

EID: 38949146354     PISSN: 13479032     EISSN: 13497006     Source Type: Journal    
DOI: 10.1111/j.1349-7006.2007.00669.x     Document Type: Article
Times cited : (78)

References (40)
  • 1
    • 33947315736 scopus 로고    scopus 로고
    • Cancer epigenomics: DNA methylomes and histone-modification maps
    • Estellaer M. Cancer epigenomics: DNA methylomes and histone-modification maps. Nat Rev Genet 2007; 8: 286-98.
    • (2007) Nat Rev Genet , vol.8 , pp. 286-298
    • Estellaer, M.1
  • 2
    • 33847065486 scopus 로고    scopus 로고
    • The epigenomics of cancer
    • Jones PA, Baylin SB. The epigenomics of cancer. Cell 2007; 128: 683-92.
    • (2007) Cell , vol.128 , pp. 683-692
    • Jones, P.A.1    Baylin, S.B.2
  • 3
    • 0037154963 scopus 로고    scopus 로고
    • Cooperation between complexes that regulate chromatin structure and transcription
    • Nalikar GJ, Fan HY, Kingston RE. Cooperation between complexes that regulate chromatin structure and transcription. Cell 2002; 108: 475-87.
    • (2002) Cell , vol.108 , pp. 475-487
    • Nalikar, G.J.1    Fan, H.Y.2    Kingston, R.E.3
  • 4
    • 33746457753 scopus 로고    scopus 로고
    • Enhanced histone acetylation and transcription: A dynamic perspective
    • Clayton AL, Hazzalin CA, Mahadevan LC. Enhanced histone acetylation and transcription: A dynamic perspective. Mol Cell 2006; 23: 289-96.
    • (2006) Mol Cell , vol.23 , pp. 289-296
    • Clayton, A.L.1    Hazzalin, C.A.2    Mahadevan, L.C.3
  • 5
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • Kuo MH, Allis CD. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays 1998; 20: 615-26.
    • (1998) Bioessays , vol.20 , pp. 615-626
    • Kuo, M.H.1    Allis, C.D.2
  • 6
    • 4744344066 scopus 로고    scopus 로고
    • Epigenetics and cancer
    • Lund AH, van Lohuizen M. Epigenetics and cancer. Genes Dev 2004; 18: 2315-35.
    • (2004) Genes Dev , vol.18 , pp. 2315-2335
    • Lund, A.H.1    van Lohuizen, M.2
  • 7
    • 1042278765 scopus 로고    scopus 로고
    • The history of cancer epigenetics
    • Feinberg AP, Tycko B. The history of cancer epigenetics. Nat Rev Cancer 2004; 4: 143-53.
    • (2004) Nat Rev Cancer , vol.4 , pp. 143-153
    • Feinberg, A.P.1    Tycko, B.2
  • 8
    • 0035755974 scopus 로고    scopus 로고
    • Histone deacetylase and cancer: Cause and therapies
    • Marks PA, Rifkind RA, Richon VM et al. Histone deacetylase and cancer: cause and therapies. Nat Rev Cancer 2001; 1: 194-202.
    • (2001) Nat Rev Cancer , vol.1 , pp. 194-202
    • Marks, P.A.1    Rifkind, R.A.2    Richon, V.M.3
  • 9
    • 2342603414 scopus 로고    scopus 로고
    • Induction of HDAC2 expression upon loss of APC in colorectal tumorigenesis
    • Zhu P, Martin E, Mengwasser J et al. Induction of HDAC2 expression upon loss of APC in colorectal tumorigenesis. Cancer Cell 2004; 5: 455-63.
    • (2004) Cancer Cell , vol.5 , pp. 455-463
    • Zhu, P.1    Martin, E.2    Mengwasser, J.3
  • 10
    • 0036527775 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Novel drugs for treatment of cancer
    • Johnstone RW. Histone deacetylase inhibitors: Novel drugs for treatment of cancer. Nat Rev Drug Discov 2002; 1: 287-99.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 12
    • 13444274622 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylases induce tumor-selective apoptosis through activation of the death receptor pathway
    • Insinga A, Monestiroli S, Ronzoni S et al. Inhibitors of histone deacetylases induce tumor-selective apoptosis through activation of the death receptor pathway. Nat Med 2005; 11: 71-6.
    • (2005) Nat Med , vol.11 , pp. 71-76
    • Insinga, A.1    Monestiroli, S.2    Ronzoni, S.3
  • 13
    • 13444306459 scopus 로고    scopus 로고
    • Tumor-selective action of HDAC inhibitors involves TRAIL induction in acute myeloid leukemia cells
    • Nebbioso A, Clarke N, Voltz E et al. Tumor-selective action of HDAC inhibitors involves TRAIL induction in acute myeloid leukemia cells. Nat Med 2005; 11: 77-84.
    • (2005) Nat Med , vol.11 , pp. 77-84
    • Nebbioso, A.1    Clarke, N.2    Voltz, E.3
  • 14
    • 29044446185 scopus 로고    scopus 로고
    • Blockade of the ERK pathway markedly sensitizes tumor cells to HDAC inhibitor-induced cell death
    • Ozaki K, Minoda A, Kishikawa F, Kohno M. Blockade of the ERK pathway markedly sensitizes tumor cells to HDAC inhibitor-induced cell death. Biochem Biophys Res Commun 2006; 339: 1171-7.
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 1171-1177
    • Ozaki, K.1    Minoda, A.2    Kishikawa, F.3    Kohno, M.4
  • 15
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci S, Pelicci PG. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat Rev Cancer 2006; 6: 38-51.
    • (2006) Nat Rev Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 17
    • 14044250159 scopus 로고    scopus 로고
    • Enhancement of in vitro and in vivo tumor cell radiosensitivity by valproic acid
    • Camphausen K, Cerna D, Scott T et al. Enhancement of in vitro and in vivo tumor cell radiosensitivity by valproic acid. Int J Cancer 2005; 114: 380-6.
    • (2005) Int J Cancer , vol.114 , pp. 380-386
    • Camphausen, K.1    Cerna, D.2    Scott, T.3
  • 18
    • 33646562250 scopus 로고    scopus 로고
    • Modulation of cellular radiation responses by histone deacetylase inhibitors
    • Karagiannis TC, El-Osta A. Modulation of cellular radiation responses by histone deacetylase inhibitors. Oncogene 2006; 25: 3885-93.
    • (2006) Oncogene , vol.25 , pp. 3885-3893
    • Karagiannis, T.C.1    El-Osta, A.2
  • 19
    • 18844415633 scopus 로고    scopus 로고
    • Sensitization to UV-induced apoptosis by the histone deacetylase inhibitor trichostatin A (TSA)
    • Kim MS, Baek JH, Chakravarty D, Sidransky D, Carrier F. Sensitization to UV-induced apoptosis by the histone deacetylase inhibitor trichostatin A (TSA). Exp Cell Res 2005; 306: 94-102.
    • (2005) Exp Cell Res , vol.306 , pp. 94-102
    • Kim, M.S.1    Baek, J.H.2    Chakravarty, D.3    Sidransky, D.4    Carrier, F.5
  • 20
    • 0242610850 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase increases cytotoxicity to anticancer drugs targeting DNA
    • Kim MS, Blake M, Baek JH, Kohlhagen G, Pommier Y, Carrier F. Inhibition of histone deacetylase increases cytotoxicity to anticancer drugs targeting DNA. Cancer Res 2003; 63: 7291-300.
    • (2003) Cancer Res , vol.63 , pp. 7291-7300
    • Kim, M.S.1    Blake, M.2    Baek, J.H.3    Kohlhagen, G.4    Pommier, Y.5    Carrier, F.6
  • 21
    • 33744749272 scopus 로고    scopus 로고
    • Trichostatin A enhances the response of chemotherapeutic agents in inhibiting pancreatic cancer cell proliferation
    • Piacentini P, Donadelli M, Costanzo C, Moore PS, Palmieri M, Scarpa A. Trichostatin A enhances the response of chemotherapeutic agents in inhibiting pancreatic cancer cell proliferation. Virchows Arch 2006; 448: 797-804.
    • (2006) Virchows Arch , vol.448 , pp. 797-804
    • Piacentini, P.1    Donadelli, M.2    Costanzo, C.3    Moore, P.S.4    Palmieri, M.5    Scarpa, A.6
  • 22
    • 0036519363 scopus 로고    scopus 로고
    • DNA and its associated processes as targets for cancer therapy
    • Hurley LH. DNA and its associated processes as targets for cancer therapy. Nat Rev Cancer 2002; 2: 188-200.
    • (2002) Nat Rev Cancer , vol.2 , pp. 188-200
    • Hurley, L.H.1
  • 23
    • 0033590636 scopus 로고    scopus 로고
    • Constitutive activation of the 41-/43-kDa mitogen-activated protein kinase signaling pathway in human tumors
    • Hoshino R, Chatani Y, Yamori T et al. Constitutive activation of the 41-/ 43-kDa mitogen-activated protein kinase signaling pathway in human tumors. Oncogene 1999; 18: 813-22.
    • (1999) Oncogene , vol.18 , pp. 813-822
    • Hoshino, R.1    Chatani, Y.2    Yamori, T.3
  • 24
    • 0037008732 scopus 로고    scopus 로고
    • Prolonged nuclear retention of activated extracellular signal-regulated kinase 1/2 is required for hepatocyte growth factor-induced cell motility
    • Tanimura S, Nomura K, Ozaki K, Tsujimoto M, Kondo T, Kohno M. Prolonged nuclear retention of activated extracellular signal-regulated kinase 1/2 is required for hepatocyte growth factor-induced cell motility. J Biol Chem 2002; 277: 28256-64.
    • (2002) J Biol Chem , vol.277 , pp. 28256-28264
    • Tanimura, S.1    Nomura, K.2    Ozaki, K.3    Tsujimoto, M.4    Kondo, T.5    Kohno, M.6
  • 26
    • 29644442524 scopus 로고    scopus 로고
    • Inhibition of the PI3 kinase/Akt pathway enhances doxorubicin-induced apoptotic cell death in tumor cells in a p53-dependent manner
    • Fujiwara Y, Kawada K, Takano D, Tanimura S, Ozaki K, Kohno M. Inhibition of the PI3 kinase/Akt pathway enhances doxorubicin-induced apoptotic cell death in tumor cells in a p53-dependent manner. Biochem Biophys Res Commun 2006; 340: 560-6.
    • (2006) Biochem Biophys Res Commun , vol.340 , pp. 560-566
    • Fujiwara, Y.1    Kawada, K.2    Takano, D.3    Tanimura, S.4    Ozaki, K.5    Kohno, M.6
  • 27
    • 30644457873 scopus 로고    scopus 로고
    • Efficient suppression of FGF-2-induced ERK activation by the cooperative interaction among mammalian Sprouty isoforms
    • Ozaki K, Miyazaki S, Tanimura S, Kohno M. Efficient suppression of FGF-2-induced ERK activation by the cooperative interaction among mammalian Sprouty isoforms. J Cell Sci 2005; 118: 5861-71.
    • (2005) J Cell Sci , vol.118 , pp. 5861-5871
    • Ozaki, K.1    Miyazaki, S.2    Tanimura, S.3    Kohno, M.4
  • 28
    • 34147168761 scopus 로고    scopus 로고
    • Blockade of the phosphatidylinositol-3-kinase Akt signaling pathway enhances the induction of apoptosis by microtubule-destabilizing agents in tumor cells in which the pathway is constitutively activated
    • Fujiwara Y, Hosokawa Y, Watanabe K, Tanimura S, Ozaki K, Kohno M. Blockade of the phosphatidylinositol-3-kinase Akt signaling pathway enhances the induction of apoptosis by microtubule-destabilizing agents in tumor cells in which the pathway is constitutively activated. Mol Cancer Ther 2007; 6: 1133-42.
    • (2007) Mol Cancer Ther , vol.6 , pp. 1133-1142
    • Fujiwara, Y.1    Hosokawa, Y.2    Watanabe, K.3    Tanimura, S.4    Ozaki, K.5    Kohno, M.6
  • 29
    • 0025233861 scopus 로고
    • Metallothionein gene expression and resistance to cisplatin in human ovarian cancer
    • Schilder RJ, Hall L, Monks A et al. Metallothionein gene expression and resistance to cisplatin in human ovarian cancer. Int J Cancer 1990; 45: 416-22.
    • (1990) Int J Cancer , vol.45 , pp. 416-422
    • Schilder, R.J.1    Hall, L.2    Monks, A.3
  • 30
    • 0031036984 scopus 로고    scopus 로고
    • Cytometry in cell necrobiology: Analysis of apoptosis and accidental cell death (necrosis)
    • Darzynkiewicz Z, Juan G, Li X, Gorczyca W, Murakami T, Traganos F. Cytometry in cell necrobiology: Analysis of apoptosis and accidental cell death (necrosis). Cytometry 1999; 27: 1-20.
    • (1999) Cytometry , vol.27 , pp. 1-20
    • Darzynkiewicz, Z.1    Juan, G.2    Li, X.3    Gorczyca, W.4    Murakami, T.5    Traganos, F.6
  • 31
    • 0032970132 scopus 로고    scopus 로고
    • Phosphatidylserine externalization during differentiation-triggered apoptosis of erythroleukemic cells
    • Diaz C, Lee AT, McConkey DJ, Schroit AJ. Phosphatidylserine externalization during differentiation-triggered apoptosis of erythroleukemic cells. Cell Death Differ 1999; 6: 218-26.
    • (1999) Cell Death Differ , vol.6 , pp. 218-226
    • Diaz, C.1    Lee, A.T.2    McConkey, D.J.3    Schroit, A.J.4
  • 32
    • 0032489520 scopus 로고    scopus 로고
    • DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
    • Rogakou EP, Pilch DR, Orr AH, Ivanova VH, Bonner WM. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J Biol Chem 1998; 273: 5858-68.
    • (1998) J Biol Chem , vol.273 , pp. 5858-5868
    • Rogakou, E.P.1    Pilch, D.R.2    Orr, A.H.3    Ivanova, V.H.4    Bonner, W.M.5
  • 33
    • 0031011174 scopus 로고    scopus 로고
    • Role of reactive oxygen species in cis-dichlorodiamineplatinum-induced cytotoxicity on bladder cancer cells
    • Miyajima A, Nakashima J, Yoshioka K, Tachibana M, Tazaki H, Murai M. Role of reactive oxygen species in cis-dichlorodiamineplatinum-induced cytotoxicity on bladder cancer cells. Br J Cancer 1997; 76: 206-10.
    • (1997) Br J Cancer , vol.76 , pp. 206-210
    • Miyajima, A.1    Nakashima, J.2    Yoshioka, K.3    Tachibana, M.4    Tazaki, H.5    Murai, M.6
  • 34
    • 0344825072 scopus 로고    scopus 로고
    • DNA-damaging reagents induce apoptosis through reactive oxygen species-dependent Fas aggregation
    • Huang HL, Fang LW, Lu SP, Chou CK, Luh TY, Lai MZ. DNA-damaging reagents induce apoptosis through reactive oxygen species-dependent Fas aggregation. Oncogene 2003; 22: 8168-77.
    • (2003) Oncogene , vol.22 , pp. 8168-8177
    • Huang, H.L.1    Fang, L.W.2    Lu, S.P.3    Chou, C.K.4    Luh, T.Y.5    Lai, M.Z.6
  • 35
    • 0027146423 scopus 로고
    • In vivo cytotoxicity, protein binding, red blood cell partitioning, and biotransformation of oxaliplatin
    • Pendyala L, Creaven PJ. In vivo cytotoxicity, protein binding, red blood cell partitioning, and biotransformation of oxaliplatin. Cancer Res 1993; 53: 5970-6.
    • (1993) Cancer Res , vol.53 , pp. 5970-5976
    • Pendyala, L.1    Creaven, P.J.2
  • 36
    • 0034806972 scopus 로고    scopus 로고
    • Enhanced ROS production in oncogenically transformed cells potentiates c-Jun N-terminal kinase and p38 mitogen-activated protein kinase activation and sensitization to genotoxic stress
    • Benhar M, Dalyot I, Engelberg D, Levitzki A. Enhanced ROS production in oncogenically transformed cells potentiates c-Jun N-terminal kinase and p38 mitogen-activated protein kinase activation and sensitization to genotoxic stress. Mol Cell Biol 2001; 21: 6913-26.
    • (2001) Mol Cell Biol , vol.21 , pp. 6913-6926
    • Benhar, M.1    Dalyot, I.2    Engelberg, D.3    Levitzki, A.4
  • 37
    • 0035845541 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species
    • Ruefli AA, Ausserlechner MJ, Bernhard D et al. The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species. Proc Natl Acad Sci USA 2001; 98: 10833-8.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10833-10838
    • Ruefli, A.A.1    Ausserlechner, M.J.2    Bernhard, D.3
  • 39
    • 0032169105 scopus 로고    scopus 로고
    • Cellular and molecular determinants of cisplatin resistance
    • Perez RP. Cellular and molecular determinants of cisplatin resistance. Eur J Cancer 1998; 34: 1535-42.
    • (1998) Eur J Cancer , vol.34 , pp. 1535-1542
    • Perez, R.P.1
  • 40
    • 0028141961 scopus 로고
    • Messenger RNA levels of XPAC and ERCC1 in ovarian cancer tissue correlated with response to platinum-based chemotherapy
    • Dabholkar M, Vionnet J, Bostick-Bruton F, Yu JJ, Reed E. Messenger RNA levels of XPAC and ERCC1 in ovarian cancer tissue correlated with response to platinum-based chemotherapy. J Clin Invest 1994; 94: 703-8.
    • (1994) J Clin Invest , vol.94 , pp. 703-708
    • Dabholkar, M.1    Vionnet, J.2    Bostick-Bruton, F.3    Yu, J.J.4    Reed, E.5


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