메뉴 건너뛰기




Volumn 1773, Issue 11, 2007, Pages 1653-1663

Arsenic trioxide sensitizes promonocytic leukemia cells to TNFα-induced apoptosis via p38-MAPK-regulated activation of both receptor-mediated and mitochondrial pathways

Author keywords

Apoptosis; Arsenic trioxide; Mitochondrial pathway; Myeloid leukemia cell; Receptor mediated pathway; TNF

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; 2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 MORPHOLINO 8 PHENYLCHROMONE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 5 (2 AMINO 4 PYRIMIDINYL) 4 (4 FLUOROPHENYL) 1 (4 PIPERIDINYL)IMIDAZOLE; ANTHRA[1,9 CD]PYRAZOL 6(2H) ONE; ARSENIC TRIOXIDE; BENZYLOXYCARBONYLISOLEUCYLGLUTAMYLTHREONYLASPARTYL FLUOROMETHYL KETONE; BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; CASPASE 3; CASPASE 9; CYTOCHROME C; FLICE INHIBITORY PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN BAX; PROTEIN BCL 2; TRANSCRIPTION FACTOR RELA; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR 1; X LINKED INHIBITOR OF APOPTOSIS;

EID: 35548998655     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2007.06.003     Document Type: Article
Times cited : (21)

References (43)
  • 2
    • 0742289410 scopus 로고    scopus 로고
    • Oxidative mechanisms of arsenic toxicity and carcinogenesis
    • Shi H., Shi X., and Liu K.J. Oxidative mechanisms of arsenic toxicity and carcinogenesis. Mol. Cell. Biochem. 255 (2004) 67-78
    • (2004) Mol. Cell. Biochem. , vol.255 , pp. 67-78
    • Shi, H.1    Shi, X.2    Liu, K.J.3
  • 3
    • 3242666928 scopus 로고    scopus 로고
    • The potential role of arsenic trioxide in the treatment of malignant disease: past, present and future
    • Evens A.M., Tallman M.S., and Gartenhaus R.B. The potential role of arsenic trioxide in the treatment of malignant disease: past, present and future. Leuk. Res. 28 (2004) 891-900
    • (2004) Leuk. Res. , vol.28 , pp. 891-900
    • Evens, A.M.1    Tallman, M.S.2    Gartenhaus, R.B.3
  • 5
    • 0141509869 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiration. A novel strategy to enhance drug-induced apoptosis in human leukaemia cells by reactive oxygen species-mediated mechanism
    • Pelicano H., Feng L., Zhou Y., Carew J.S., Hileman E.O., Plunkett W., Keating M.J., and Heng P. Inhibition of mitochondrial respiration. A novel strategy to enhance drug-induced apoptosis in human leukaemia cells by reactive oxygen species-mediated mechanism. J. Biol. Chem. 278 (2003) 37832-37839
    • (2003) J. Biol. Chem. , vol.278 , pp. 37832-37839
    • Pelicano, H.1    Feng, L.2    Zhou, Y.3    Carew, J.S.4    Hileman, E.O.5    Plunkett, W.6    Keating, M.J.7    Heng, P.8
  • 6
    • 33746886979 scopus 로고    scopus 로고
    • Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy
    • Fulda S., and Debatin K.M. Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy. Oncogene 25 (2006) 4798-4811
    • (2006) Oncogene , vol.25 , pp. 4798-4811
    • Fulda, S.1    Debatin, K.M.2
  • 7
    • 16644372319 scopus 로고    scopus 로고
    • Following a TRAIL: update on a ligand and its five receptors
    • Kimberley F.C., and Screaton G.R. Following a TRAIL: update on a ligand and its five receptors. Cell Res. 14 (2004) 359-372
    • (2004) Cell Res. , vol.14 , pp. 359-372
    • Kimberley, F.C.1    Screaton, G.R.2
  • 8
    • 0013601339 scopus 로고
    • The toxic effect of tumour necrosis factor in vivo and their prevention by cyclooxygenase inhibitors
    • Kettelhut I.C., Fiers W., and Godberg A.L. The toxic effect of tumour necrosis factor in vivo and their prevention by cyclooxygenase inhibitors. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 4273-4277
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 4273-4277
    • Kettelhut, I.C.1    Fiers, W.2    Godberg, A.L.3
  • 9
    • 0035854706 scopus 로고    scopus 로고
    • Lithium sensitizes tumor cells in a NF-κB-independent way to caspase activation and apoptosis induced by tumor Necrosis Factor (TNF). Evidence for a role of the TNF receptor-associated death domain protein
    • Schotte P., Van Loo G., Carpentier I., Vandenabeele P., and Beyaert R. Lithium sensitizes tumor cells in a NF-κB-independent way to caspase activation and apoptosis induced by tumor Necrosis Factor (TNF). Evidence for a role of the TNF receptor-associated death domain protein. J. Biol. Chem. 276 (2001) 25939-25945
    • (2001) J. Biol. Chem. , vol.276 , pp. 25939-25945
    • Schotte, P.1    Van Loo, G.2    Carpentier, I.3    Vandenabeele, P.4    Beyaert, R.5
  • 10
    • 2942559254 scopus 로고    scopus 로고
    • The anticancer drug mithramycin A sensitizes tumour cells to apoptosis induced by tumour necrosis factor (TNF)
    • Duverger V., Murphy A.M., Sheehan D., England K., Cotter T.G., Hayes I., and Muphy F.J. The anticancer drug mithramycin A sensitizes tumour cells to apoptosis induced by tumour necrosis factor (TNF). Br. J. Cancer 90 (2004) 2025-2031
    • (2004) Br. J. Cancer , vol.90 , pp. 2025-2031
    • Duverger, V.1    Murphy, A.M.2    Sheehan, D.3    England, K.4    Cotter, T.G.5    Hayes, I.6    Muphy, F.J.7
  • 11
    • 0037772194 scopus 로고    scopus 로고
    • 2/M cell cycle arrest, activation of caspase-8 or caspase-9, and synergy with APO2/TRAIL
    • 2/M cell cycle arrest, activation of caspase-8 or caspase-9, and synergy with APO2/TRAIL. Blood 101 (2003) 4078-4087
    • (2003) Blood , vol.101 , pp. 4078-4087
    • Liu, Q.1    Hilsenbeck, S.2    Gazitt, Y.3
  • 12
    • 32544435965 scopus 로고    scopus 로고
    • TRAIL sensitization by arsenic trioxide is caspase-8 dependent and involves modulation of death receptor components and Akt
    • Szegezdi E., Cahill S., Meyer M., O'Dwyer M., and Samali A. TRAIL sensitization by arsenic trioxide is caspase-8 dependent and involves modulation of death receptor components and Akt. Br. J. Cancer 94 (2006) 398-406
    • (2006) Br. J. Cancer , vol.94 , pp. 398-406
    • Szegezdi, E.1    Cahill, S.2    Meyer, M.3    O'Dwyer, M.4    Samali, A.5
  • 13
    • 0033568238 scopus 로고    scopus 로고
    • Arsenic trioxide selectively induces acute promyelocytic leukaemia cell apoptosis via a hydrogen peroxide-dependent pathway
    • Jing Y., Dai J., Chalmers-Redman R.M., Tatton W.G., and Waxman S. Arsenic trioxide selectively induces acute promyelocytic leukaemia cell apoptosis via a hydrogen peroxide-dependent pathway. Blood 94 (1999) 2102-2111
    • (1999) Blood , vol.94 , pp. 2102-2111
    • Jing, Y.1    Dai, J.2    Chalmers-Redman, R.M.3    Tatton, W.G.4    Waxman, S.5
  • 15
    • 0031178835 scopus 로고    scopus 로고
    • Bcl-2 expression in target cells leads to functional inhibition of caspase-3 protease family in human NK and lymphokine-activated killer cell granule-mediated apoptosis
    • Renvoize, Roger R., Moulian N., Bertoglio J., and Bréard J. Bcl-2 expression in target cells leads to functional inhibition of caspase-3 protease family in human NK and lymphokine-activated killer cell granule-mediated apoptosis. J. Immunol. 159 (1997) 126-134
    • (1997) J. Immunol. , vol.159 , pp. 126-134
    • Renvoize1    Roger, R.2    Moulian, N.3    Bertoglio, J.4    Bréard, J.5
  • 16
    • 33750522657 scopus 로고    scopus 로고
    • Pharmacologic inhibitors of extracellular signal-regulated kinase (ERKs) and c-Jun NH2-terminal kinase (JNK) decrease glutathione content and sensitize human promonocytic leukemia cells to arsenic trioxide-induced apoptosis
    • Ramos A.M., Fernández C., Amrán D., Esteban D., de Blas E., Palacios M.A., and Aller P. Pharmacologic inhibitors of extracellular signal-regulated kinase (ERKs) and c-Jun NH2-terminal kinase (JNK) decrease glutathione content and sensitize human promonocytic leukemia cells to arsenic trioxide-induced apoptosis. J. Cell. Physiol. 209 (2006) 1006-1015
    • (2006) J. Cell. Physiol. , vol.209 , pp. 1006-1015
    • Ramos, A.M.1    Fernández, C.2    Amrán, D.3    Esteban, D.4    de Blas, E.5    Palacios, M.A.6    Aller, P.7
  • 17
    • 0042164447 scopus 로고    scopus 로고
    • The selection between apoptosis and necrosis is differentially regulated in hydrogen peroxide-treated and glutathione-depleted human promonocytic cells
    • Troyano A., Sancho P., Fernández C., de Blas E., Bernardi P., and Aller P. The selection between apoptosis and necrosis is differentially regulated in hydrogen peroxide-treated and glutathione-depleted human promonocytic cells. Cell Death Differ. 10 (2003) 889-898
    • (2003) Cell Death Differ. , vol.10 , pp. 889-898
    • Troyano, A.1    Sancho, P.2    Fernández, C.3    de Blas, E.4    Bernardi, P.5    Aller, P.6
  • 18
    • 0035861744 scopus 로고    scopus 로고
    • Effect of glutathione depletion on antitumor drug toxicity (apoptosis and necrosis) in U-937 human promonocytic cells
    • Troyano A., Fernández C., Sancho P., de Blas E., and Aller P. Effect of glutathione depletion on antitumor drug toxicity (apoptosis and necrosis) in U-937 human promonocytic cells. J. Biol. Chem. 276 (2001) 14115-47107
    • (2001) J. Biol. Chem. , vol.276 , pp. 14115-47107
    • Troyano, A.1    Fernández, C.2    Sancho, P.3    de Blas, E.4    Aller, P.5
  • 19
    • 0024293495 scopus 로고
    • Identification of a novel lymphoid-specific octamer binding protein (OTF-2B) by proteolytic clipping bandshift assay (PCBA)
    • Schreiber E.P., Matthias P., Müller M.M., and Schaffner W. Identification of a novel lymphoid-specific octamer binding protein (OTF-2B) by proteolytic clipping bandshift assay (PCBA). EMBO J. 7 (1988) 4221-4229
    • (1988) EMBO J. , vol.7 , pp. 4221-4229
    • Schreiber, E.P.1    Matthias, P.2    Müller, M.M.3    Schaffner, W.4
  • 20
    • 0031570386 scopus 로고    scopus 로고
    • An octamer element functions as a regulatory element in the differentiation-responsive CD11c integrin gene promoter: OCT-2 inducibility during myelomononcytic differentiation
    • López-Rodríguez C., Zubiaur M., Sancho J., Concha A., and Corbí A.L. An octamer element functions as a regulatory element in the differentiation-responsive CD11c integrin gene promoter: OCT-2 inducibility during myelomononcytic differentiation. J. Immunol. 158 (1997) 5833-5840
    • (1997) J. Immunol. , vol.158 , pp. 5833-5840
    • López-Rodríguez, C.1    Zubiaur, M.2    Sancho, J.3    Concha, A.4    Corbí, A.L.5
  • 21
    • 4644280684 scopus 로고    scopus 로고
    • Tumor necrosis factor α sensitizes malignant cells to chemotherapeutic drugs via the mitochondrial apoptosis pathway independently of caspase-8 and NF-κB
    • Schmelz K., Wieder T., Tamm I., Müller A., Essmann F., Geilen C.C., Schulze-Osthoff K., Dörken B., and Daniel P.T. Tumor necrosis factor α sensitizes malignant cells to chemotherapeutic drugs via the mitochondrial apoptosis pathway independently of caspase-8 and NF-κB. Oncogene 23 (2004) 6743-6759
    • (2004) Oncogene , vol.23 , pp. 6743-6759
    • Schmelz, K.1    Wieder, T.2    Tamm, I.3    Müller, A.4    Essmann, F.5    Geilen, C.C.6    Schulze-Osthoff, K.7    Dörken, B.8    Daniel, P.T.9
  • 22
    • 0037631325 scopus 로고    scopus 로고
    • Inhibition of glucose metabolism sensitizes tumor cells to death receptor-triggered apoptosis through enhancement of death-inducing signalling complex formation and apical procaspase-8 processing
    • Muñoz-Pinedo C., Ruiz-Ruiz C., Ruiz de Almodóvar C., Palacios C., and López-Rivas A. Inhibition of glucose metabolism sensitizes tumor cells to death receptor-triggered apoptosis through enhancement of death-inducing signalling complex formation and apical procaspase-8 processing. J. Biol. Chem. 278 (2003) 12759-12768
    • (2003) J. Biol. Chem. , vol.278 , pp. 12759-12768
    • Muñoz-Pinedo, C.1    Ruiz-Ruiz, C.2    Ruiz de Almodóvar, C.3    Palacios, C.4    López-Rivas, A.5
  • 23
    • 0036726570 scopus 로고    scopus 로고
    • Arsenic trioxide-induced apoptosis in U937 cells involve generation of reactive oxygen species and inhibition of Akt
    • Choi Y.J., Park J.W., Suh S.I., Mun K.C., Bar J.H., Song D.K., Kim S.P., and Kwon T.K. Arsenic trioxide-induced apoptosis in U937 cells involve generation of reactive oxygen species and inhibition of Akt. Int. J. Oncol. 21 (2002) 603-610
    • (2002) Int. J. Oncol. , vol.21 , pp. 603-610
    • Choi, Y.J.1    Park, J.W.2    Suh, S.I.3    Mun, K.C.4    Bar, J.H.5    Song, D.K.6    Kim, S.P.7    Kwon, T.K.8
  • 24
    • 33646488373 scopus 로고    scopus 로고
    • Targeting Hsp90 by 17-AGG in leukemia cells: mechanisms for synergistic and antagonistic drug combinations with arsenic trioxide and Ara-C
    • Pelicano H., Carew J.S., McQueen T.J., Andreeff M., Plukett W., Keating M.J., and Huang P. Targeting Hsp90 by 17-AGG in leukemia cells: mechanisms for synergistic and antagonistic drug combinations with arsenic trioxide and Ara-C. Leukemia 20 (2006) 610-619
    • (2006) Leukemia , vol.20 , pp. 610-619
    • Pelicano, H.1    Carew, J.S.2    McQueen, T.J.3    Andreeff, M.4    Plukett, W.5    Keating, M.J.6    Huang, P.7
  • 26
    • 18544374589 scopus 로고    scopus 로고
    • Pharmacologic inhibitors of PI3K/Akt potentiate the apoptotic action of the antileukemic drug arsenic trioxide via glutathione depletion and increased peroxide accumulation in myeloid leukemia cells
    • Ramos A.M., Fernández A., Amrán D., Sancho P., de Blas E., and Aller P. Pharmacologic inhibitors of PI3K/Akt potentiate the apoptotic action of the antileukemic drug arsenic trioxide via glutathione depletion and increased peroxide accumulation in myeloid leukemia cells. Blood 105 (2005) 4013-4025
    • (2005) Blood , vol.105 , pp. 4013-4025
    • Ramos, A.M.1    Fernández, A.2    Amrán, D.3    Sancho, P.4    de Blas, E.5    Aller, P.6
  • 29
    • 1842822873 scopus 로고    scopus 로고
    • 12-O-tetradecanoylphorbol-13-acetate may both potentiate and decrease the generation of apoptosis by the antileukemic agent arsenic trioxide in human promonocytic cells. Regulation by extracellular signal-regulated protein kinases and glutathione
    • Fernández C., Ramos A.M., Sancho P., Amrán D., de Blas E., and Aller P. 12-O-tetradecanoylphorbol-13-acetate may both potentiate and decrease the generation of apoptosis by the antileukemic agent arsenic trioxide in human promonocytic cells. Regulation by extracellular signal-regulated protein kinases and glutathione. J. Biol. Chem. 279 (2004) 3877-3884
    • (2004) J. Biol. Chem. , vol.279 , pp. 3877-3884
    • Fernández, C.1    Ramos, A.M.2    Sancho, P.3    Amrán, D.4    de Blas, E.5    Aller, P.6
  • 30
    • 12344305300 scopus 로고    scopus 로고
    • Camptothecin- and etoposide-induced apoptosis in human leukemia cells is independent of cell death receptor-3 and -4 aggregation but accelerates tumour necrosis factor-related apoptosis-inducing ligand-mediated cell death
    • Bergeron S., Beauchmin M., and Bertrand R. Camptothecin- and etoposide-induced apoptosis in human leukemia cells is independent of cell death receptor-3 and -4 aggregation but accelerates tumour necrosis factor-related apoptosis-inducing ligand-mediated cell death. Mol. Cancer Ther. 3 (2004) 1659-1669
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 1659-1669
    • Bergeron, S.1    Beauchmin, M.2    Bertrand, R.3
  • 31
    • 2342624727 scopus 로고    scopus 로고
    • Arsenic trioxide selectively induces early and extensive apoptosis via the APO2/caspase-8 pathway engaging the mitochondrial pathway in myeloma cells with mutant p53
    • Akay C., and Gazitt Y. Arsenic trioxide selectively induces early and extensive apoptosis via the APO2/caspase-8 pathway engaging the mitochondrial pathway in myeloma cells with mutant p53. Cell Cycle 2 (2003) 358-368
    • (2003) Cell Cycle , vol.2 , pp. 358-368
    • Akay, C.1    Gazitt, Y.2
  • 32
    • 34247847895 scopus 로고    scopus 로고
    • Arsenic trioxide induces p53-dependent apoptotic signals in myeloma cells with SiRNA-silenced p53: MAP kinase pathway is preferentially activated in cells expressing inactivated p53
    • Kircelly F., Akay C., and Gazitt Y. Arsenic trioxide induces p53-dependent apoptotic signals in myeloma cells with SiRNA-silenced p53: MAP kinase pathway is preferentially activated in cells expressing inactivated p53. Int. J. Oncol. 30 (2007) 993-1001
    • (2007) Int. J. Oncol. , vol.30 , pp. 993-1001
    • Kircelly, F.1    Akay, C.2    Gazitt, Y.3
  • 33
    • 4043050908 scopus 로고    scopus 로고
    • Susceptibility to cytosine arabinoside (Ara-C)-induced cytotoxicity in human leukaemia cells
    • Kanno S., Higurashi A., Watanabe Y., Shouji A., Asou K., and Ishikawa M. Susceptibility to cytosine arabinoside (Ara-C)-induced cytotoxicity in human leukaemia cells. Toxicol. Lett. 152 (2004) 149-158
    • (2004) Toxicol. Lett. , vol.152 , pp. 149-158
    • Kanno, S.1    Higurashi, A.2    Watanabe, Y.3    Shouji, A.4    Asou, K.5    Ishikawa, M.6
  • 34
    • 33746379603 scopus 로고    scopus 로고
    • JNK- and p38 kinase-mediated phosphorylation of Bax leads to its activation, and mitochondrial translocation and apoptosis of human hepatoma HepG2 cells
    • Kim B.J., Ryu S.W., and Song B.J. JNK- and p38 kinase-mediated phosphorylation of Bax leads to its activation, and mitochondrial translocation and apoptosis of human hepatoma HepG2 cells. J. Biol. Chem. 281 (2006) 21256-21265
    • (2006) J. Biol. Chem. , vol.281 , pp. 21256-21265
    • Kim, B.J.1    Ryu, S.W.2    Song, B.J.3
  • 35
    • 8844228917 scopus 로고    scopus 로고
    • Potent anti-leukemic interactions between flavopiridol and TRAIL/Apo2L involve flavopiridol-mediated XIAP downregulation
    • Rosato R.R., Dai Y., Almenara J.A., Maggio S.C., and Grant S. Potent anti-leukemic interactions between flavopiridol and TRAIL/Apo2L involve flavopiridol-mediated XIAP downregulation. Leukaemia 18 (2004) 1780-1788
    • (2004) Leukaemia , vol.18 , pp. 1780-1788
    • Rosato, R.R.1    Dai, Y.2    Almenara, J.A.3    Maggio, S.C.4    Grant, S.5
  • 37
    • 0037328174 scopus 로고    scopus 로고
    • Constitutively active Akt1 protects HL60 leukaemia cells from TRAIL-induced apoptosis through a mechanisms involving NF-kappaB activation and cFLIP(L) up-regulation
    • Bortul R., Tazzari P.L., Cappellini A., Tabellini G., Billi A.M., Bareggi R., Manzoli L., Cocco L., and Martelli A.M. Constitutively active Akt1 protects HL60 leukaemia cells from TRAIL-induced apoptosis through a mechanisms involving NF-kappaB activation and cFLIP(L) up-regulation. Leukaemia 17 (2003) 379-389
    • (2003) Leukaemia , vol.17 , pp. 379-389
    • Bortul, R.1    Tazzari, P.L.2    Cappellini, A.3    Tabellini, G.4    Billi, A.M.5    Bareggi, R.6    Manzoli, L.7    Cocco, L.8    Martelli, A.M.9
  • 38
    • 4644276707 scopus 로고    scopus 로고
    • Insulin signaling regulates gamma-glutamyl-cysteine ligase catalytic subunit expression in primary cultured rat hepatocytes
    • Kim S.K., Woodcroft K.J., Khodadadeh S.S., and Novak R.F. Insulin signaling regulates gamma-glutamyl-cysteine ligase catalytic subunit expression in primary cultured rat hepatocytes. J. Pharmacol. Exp. Ther. 311 (2004) 99-108
    • (2004) J. Pharmacol. Exp. Ther. , vol.311 , pp. 99-108
    • Kim, S.K.1    Woodcroft, K.J.2    Khodadadeh, S.S.3    Novak, R.F.4
  • 39
    • 1942534018 scopus 로고    scopus 로고
    • Regulation of apoptosis proteins in cancer cells by ubiquitin
    • Zhang H.G., Wang J., Yang X., Hsu H.C., and Mountz J.D. Regulation of apoptosis proteins in cancer cells by ubiquitin. Oncogene 23 (2004) 2009-2015
    • (2004) Oncogene , vol.23 , pp. 2009-2015
    • Zhang, H.G.1    Wang, J.2    Yang, X.3    Hsu, H.C.4    Mountz, J.D.5
  • 40
    • 0034607655 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli
    • Yang Y., Fang S., Jensen J.P., Weissman A.M., and Ashwell J.D. Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 288 (2000) 874-877
    • (2000) Science , vol.288 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3    Weissman, A.M.4    Ashwell, J.D.5
  • 41
    • 3242759139 scopus 로고    scopus 로고
    • Effects of arsenite on UROtsa cells: low-level arsenite causes accumulation of ubiquitinated proteins that is enhanced by reduction in cellular glutathione levels
    • Bredfeldt T., Kopplin M.J., and Gandolfi A.J. Effects of arsenite on UROtsa cells: low-level arsenite causes accumulation of ubiquitinated proteins that is enhanced by reduction in cellular glutathione levels. Toxicol. Appl. Pharmacol. 198 (2004) 412-418
    • (2004) Toxicol. Appl. Pharmacol. , vol.198 , pp. 412-418
    • Bredfeldt, T.1    Kopplin, M.J.2    Gandolfi, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.