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Volumn 71, Issue 3, 2006, Pages 257-267

Differential toxicity of antimonial compounds and their effects on glutathione homeostasis in a human leukaemia monocyte cell line

Author keywords

Antimonials; Apoptosis; Glutathione; Leukaemia; Macrophage; Oxidative stress

Indexed keywords

ANTIMONY TARTRATE; DIAMIDE; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE REDUCTASE; REACTIVE OXYGEN METABOLITE; STIBOGLUCONATE SODIUM;

EID: 29144473741     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2005.10.043     Document Type: Article
Times cited : (68)

References (36)
  • 1
    • 0042528608 scopus 로고    scopus 로고
    • Opportunities for Trisenox (arsenic trioxide) in the treatment of myelodysplastic syndromes
    • A. List, M. Beran, J. DiPersio, J. Slack, N. Vey, and C.S. Rosenfeld Opportunities for Trisenox (arsenic trioxide) in the treatment of myelodysplastic syndromes Leukemia 17 2003 1499 1507
    • (2003) Leukemia , vol.17 , pp. 1499-1507
    • List, A.1    Beran, M.2    Dipersio, J.3    Slack, J.4    Vey, N.5    Rosenfeld, C.S.6
  • 2
    • 0035041127 scopus 로고    scopus 로고
    • Clinical trials of arsenic trioxide in hematologic and solid tumors: Overview of the National Cancer Institute Cooperative Research and Development Studies
    • A.J. Murgo Clinical trials of arsenic trioxide in hematologic and solid tumors: overview of the National Cancer Institute Cooperative Research and Development Studies Oncologist 6 Suppl. 2 2001 22 28
    • (2001) Oncologist , vol.6 , Issue.2 SUPPL. , pp. 22-28
    • Murgo, A.J.1
  • 3
    • 0037225985 scopus 로고    scopus 로고
    • Arsenic trioxide inhibits the growth of A498 renal cell carcinoma cells via cell cycle arrest or apoptosis
    • P.W. Hyun, C.Y. Hee, J.C. Won, P.J. Oh, K. Kim, and I.Y. Hyuck Arsenic trioxide inhibits the growth of A498 renal cell carcinoma cells via cell cycle arrest or apoptosis Biochem Biophys Res Commun 300 2003 230 235
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 230-235
    • Hyun, P.W.1    Hee, C.Y.2    Won, J.C.3    Oh, P.J.4    Kim, K.5    Hyuck, I.Y.6
  • 4
    • 0037772194 scopus 로고    scopus 로고
    • Arsenic trioxide-induced apoptosis in myeloma cells: P53-dependent G1 or G2/M cell cycle arrest, activation of caspase-8 or caspase-9, and synergy with APO2/TRAIL
    • Q. Liu, S. Hilsenbeck, and Y. Gazitt Arsenic trioxide-induced apoptosis in myeloma cells: p53-dependent G1 or G2/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
  • 5
    • 0029982119 scopus 로고    scopus 로고
    • Arsenite induces apoptosis in Chinese hamster ovary cells by generation of reactive oxygen species
    • T.S. Wang, C.F. Kuo, K.Y. Jan, and H. Huang Arsenite induces apoptosis in Chinese hamster ovary cells by generation of reactive oxygen species J Cell Physiol 169 1996 256 268
    • (1996) J Cell Physiol , vol.169 , pp. 256-268
    • Wang, T.S.1    Kuo, C.F.2    Jan, K.Y.3    Huang, H.4
  • 6
    • 0032933610 scopus 로고    scopus 로고
    • Malignant cells can be sensitized to undergo growth inhibition and apoptosis by arsenic trioxide through modulation of the glutathione redox system
    • J. Dai, R.S. Weinberg, S. Waxman, and Y. Jing Malignant cells can be sensitized to undergo growth inhibition and apoptosis by arsenic trioxide through modulation of the glutathione redox system Blood 93 1999 268 277
    • (1999) Blood , vol.93 , pp. 268-277
    • Dai, J.1    Weinberg, R.S.2    Waxman, S.3    Jing, Y.4
  • 7
    • 0030271714 scopus 로고    scopus 로고
    • Mutagenicity, carcinogenicity and teratogenicity of antimony compounds
    • A. Leonard, and G.B. Gerber Mutagenicity, carcinogenicity and teratogenicity of antimony compounds Mutat Res 366 1996 1 8
    • (1996) Mutat Res , vol.366 , pp. 1-8
    • Leonard, A.1    Gerber, G.B.2
  • 8
    • 0032402135 scopus 로고    scopus 로고
    • Trivalent antimonials induce degradation of the PML-RARα oncoprotein and reorganization of the promyelocytic leukemia nuclear bodies in acute promyelocytic leukemia NB4 cells
    • S. Muller, W.H. Miller Jr., and A. Dejean Trivalent antimonials induce degradation of the PML-RARα oncoprotein and reorganization of the promyelocytic leukemia nuclear bodies in acute promyelocytic leukemia NB4 cells Blood 92 1998 4308 4316
    • (1998) Blood , vol.92 , pp. 4308-4316
    • Muller, S.1    Miller Jr., W.H.2    Dejean, A.3
  • 9
    • 0036584920 scopus 로고    scopus 로고
    • Potassium antimonyl tartrate induces reactive oxygen species-related apoptosis in human myeloid leukemic HL60 cells
    • V. Lecureur, D. Lagadic-Gossmann, and O. Fardel Potassium antimonyl tartrate induces reactive oxygen species-related apoptosis in human myeloid leukemic HL60 cells Int J Oncol 20 2002 1071 1076
    • (2002) Int J Oncol , vol.20 , pp. 1071-1076
    • Lecureur, V.1    Lagadic-Gossmann, D.2    Fardel, O.3
  • 11
    • 4544289321 scopus 로고    scopus 로고
    • Dual action of antimonial drugs on thiol redox metabolism in the human pathogen Leishmania donovani
    • S. Wyllie, M.L. Cunningham, and A.H. Fairlamb Dual action of antimonial drugs on thiol redox metabolism in the human pathogen Leishmania donovani J Biol Chem 279 2004 39925 39932
    • (2004) J Biol Chem , vol.279 , pp. 39925-39932
    • Wyllie, S.1    Cunningham, M.L.2    Fairlamb, A.H.3
  • 12
    • 0028263005 scopus 로고
    • Mechanism of inhibition of trypanothione reductase and glutathione reductase by trivalent organic arsenicals
    • M.L. Cunningham, M.J.J.M. Zvelebil, and A.H. Fairlamb Mechanism of inhibition of trypanothione reductase and glutathione reductase by trivalent organic arsenicals Eur J Biochem 221 1994 285 295
    • (1994) Eur J Biochem , vol.221 , pp. 285-295
    • Cunningham, M.L.1    Zvelebil, M.J.J.M.2    Fairlamb, A.H.3
  • 13
    • 0024562098 scopus 로고
    • DNA amplification in arsenite-resistant Leishmania
    • S. Detke, K. Katakura, and K.-P. Chang DNA amplification in arsenite-resistant Leishmania Exp Cell Res 180 1989 161 170
    • (1989) Exp Cell Res , vol.180 , pp. 161-170
    • Detke, S.1    Katakura, K.2    Chang, K.-P.3
  • 14
    • 0028822932 scopus 로고
    • New mechanisms of drug resistance in parasitic protozoa
    • P. Borst, and M. Ouellette New mechanisms of drug resistance in parasitic protozoa Annu Rev Microbiol 49 1995 427 460
    • (1995) Annu Rev Microbiol , vol.49 , pp. 427-460
    • Borst, P.1    Ouellette, M.2
  • 15
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • F.Q. Schafer, and G.R. Buettner Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple Free Radic Biol Med 30 2001 1191 1212
    • (2001) Free Radic Biol Med , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 16
    • 0031760626 scopus 로고    scopus 로고
    • Axenically grown amastigotes of Leishmania infantum used as an in vitro model to investigate the pentavalent antimony mode of action
    • D. Sereno, M. Cavaleyra, K. Zemzoumi, S. Maquaire, A. Ouaissi, and J.L. Lemesre Axenically grown amastigotes of Leishmania infantum used as an in vitro model to investigate the pentavalent antimony mode of action Antimicrob Agents Chemother 42 1998 3097 3102
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 3097-3102
    • Sereno, D.1    Cavaleyra, M.2    Zemzoumi, K.3    Maquaire, S.4    Ouaissi, A.5    Lemesre, J.L.6
  • 17
    • 0018195287 scopus 로고
    • The glutathione status of cells
    • N.S. Kosower, and E.M. Kosower The glutathione status of cells Int Rev Cytol 54 1978 109 160
    • (1978) Int Rev Cytol , vol.54 , pp. 109-160
    • Kosower, N.S.1    Kosower, E.M.2
  • 18
    • 0033858554 scopus 로고    scopus 로고
    • Interaction of antimony tartrate with the tripeptide glutathione - Implication for its mode of action
    • H.Z. Sun, S.C. Yan, and W.S. Cheng Interaction of antimony tartrate with the tripeptide glutathione - implication for its mode of action Eur J Biochem 267 2000 5450 5457
    • (2000) Eur J Biochem , vol.267 , pp. 5450-5457
    • Sun, H.Z.1    Yan, S.C.2    Cheng, W.S.3
  • 19
    • 0026785607 scopus 로고
    • Increased biliary excretion of glutathione is generated by the glutathione-dependent hepatobiliary transport of antimony and bismuth
    • A. Gyurasics, L. Koszorus, F. Varga, and Z. Gregus Increased biliary excretion of glutathione is generated by the glutathione-dependent hepatobiliary transport of antimony and bismuth Biochem Pharmacol 44 1992 1275 1281
    • (1992) Biochem Pharmacol , vol.44 , pp. 1275-1281
    • Gyurasics, A.1    Koszorus, L.2    Varga, F.3    Gregus, Z.4
  • 20
    • 0031043437 scopus 로고    scopus 로고
    • Induction of nitric oxide synthesis in J774 cells lowers intracellular glutathione: Effect of modulated glutathione redox status on nitric oxide synthase induction
    • J.S. Hothersall, F.Q. Cunha, G.H. Neild, and A.A. Norohna-Dutra Induction of nitric oxide synthesis in J774 cells lowers intracellular glutathione: effect of modulated glutathione redox status on nitric oxide synthase induction Biochem J 322 1997 477 481
    • (1997) Biochem J , vol.322 , pp. 477-481
    • Hothersall, J.S.1    Cunha, F.Q.2    Neild, G.H.3    Norohna-Dutra, A.A.4
  • 21
    • 0017386890 scopus 로고
    • Sensitivity of hemoglobin thiol groups within red blood cells of rat during oxidation of glutathione
    • N.S. Kosower, E.M. Kosower, and R.L. Koppel Sensitivity of hemoglobin thiol groups within red blood cells of rat during oxidation of glutathione Eur J Biochem 77 1977 529 534
    • (1977) Eur J Biochem , vol.77 , pp. 529-534
    • Kosower, N.S.1    Kosower, E.M.2    Koppel, R.L.3
  • 22
    • 0032574808 scopus 로고    scopus 로고
    • Down-regulation of Leishmania donovani trypanothione reductase by heterologous expression of a trans-dominant mutant homologue: Effect on parasite intracellular survival
    • J. Tovar, M.L. Cunningham, A.C. Smith, S.L. Croft, and A.H. Fairlamb Down-regulation of Leishmania donovani trypanothione reductase by heterologous expression of a trans-dominant mutant homologue: effect on parasite intracellular survival Proc Natl Acad Sci USA 95 1998 5311 5316
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5311-5316
    • Tovar, J.1    Cunningham, M.L.2    Smith, A.C.3    Croft, S.L.4    Fairlamb, A.H.5
  • 23
    • 15844416284 scopus 로고    scopus 로고
    • Coordinated induction of MRP/GS-X pump and gamma-glutamylcysteine synthetase by heavy metals in human leukemia cells
    • T. Ishikawa, J.-J. Bao, Y. Yamane, K. Akimaru, K. Frindrich, and C.D. Wright Coordinated induction of MRP/GS-X pump and gamma-glutamylcysteine synthetase by heavy metals in human leukemia cells J Biol Chem 271 1996 14981 14988
    • (1996) J Biol Chem , vol.271 , pp. 14981-14988
    • Ishikawa, T.1    Bao, J.-J.2    Yamane, Y.3    Akimaru, K.4    Frindrich, K.5    Wright, C.D.6
  • 24
    • 0033042159 scopus 로고    scopus 로고
    • Overexpression of the multidrug resistance-associated protein (MRP1) in human heavy metal-selected tumor cells
    • L. Vernhet, A. Courtois, N. Allain, L. Payen, J.P. Anger, and A. Guillouzo Overexpression of the multidrug resistance-associated protein (MRP1) in human heavy metal-selected tumor cells FEBS Lett 443 1999 321 325
    • (1999) FEBS Lett , vol.443 , pp. 321-325
    • Vernhet, L.1    Courtois, A.2    Allain, N.3    Payen, L.4    Anger, J.P.5    Guillouzo, A.6
  • 26
    • 0033230807 scopus 로고    scopus 로고
    • Tissue-specific functions of individual glutathione peroxidases
    • R. Brigelius-Flohe Tissue-specific functions of individual glutathione peroxidases Free Radic Biol Med 27 1999 951 965
    • (1999) Free Radic Biol Med , vol.27 , pp. 951-965
    • Brigelius-Flohe, R.1
  • 27
    • 0021288821 scopus 로고
    • Assays of glutathione peroxidase
    • L. Flohé, and W.A. Günzler Assays of glutathione peroxidase Methods Enzymol 105 1984 114 126
    • (1984) Methods Enzymol , vol.105 , pp. 114-126
    • Flohé, L.1    Günzler, W.A.2
  • 28
    • 2942593991 scopus 로고    scopus 로고
    • ROS stress in cancer cells and therapeutic implications
    • H. Pelicano, D. Carney, and P. Huang ROS stress in cancer cells and therapeutic implications Drug Resist Updat 7 2004 97 110
    • (2004) Drug Resist Updat , vol.7 , pp. 97-110
    • Pelicano, H.1    Carney, D.2    Huang, P.3
  • 29
    • 1842585519 scopus 로고    scopus 로고
    • Role of NADPH oxidase in arsenic-induced reactive oxygen species formation and cytotoxicity in myeloid leukemia cells
    • W.C. Chou, C. Jie, A.A. Kenedy, R.J. Jones, M.A. Trush, and C.V. Dang Role of NADPH oxidase in arsenic-induced reactive oxygen species formation and cytotoxicity in myeloid leukemia cells Proc Natl Acad Sci USA 101 2004 4578 4583
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4578-4583
    • Chou, W.C.1    Jie, C.2    Kenedy, A.A.3    Jones, R.J.4    Trush, M.A.5    Dang, C.V.6
  • 30
    • 0036434902 scopus 로고    scopus 로고
    • Potassium antimonyl tartrate induces caspase- and reactive oxygen species-dependent apoptosis in lymphoid tumoral cells
    • V. Lecureur, A. Le Thiec, A. Le Meur, L. Amiot, B. Drenou, and M. Bernard Potassium antimonyl tartrate induces caspase- and reactive oxygen species-dependent apoptosis in lymphoid tumoral cells Br J Haematol 119 2002 608 615
    • (2002) Br J Haematol , vol.119 , pp. 608-615
    • Lecureur, V.1    Le Thiec, A.2    Le Meur, A.3    Amiot, L.4    Drenou, B.5    Bernard, M.6
  • 31
    • 0036255533 scopus 로고    scopus 로고
    • The MRP1-mediated effluxes of arsenic and antimony do not require arsenic-glutathione and antimony-glutathione complex formation
    • M. Salerno, M. Petroutsa, and A. Garnier-Suillerot The MRP1-mediated effluxes of arsenic and antimony do not require arsenic-glutathione and antimony-glutathione complex formation J Bioenerg Biomembr 34 2002 135 145
    • (2002) J Bioenerg Biomembr , vol.34 , pp. 135-145
    • Salerno, M.1    Petroutsa, M.2    Garnier-Suillerot, A.3
  • 32
    • 0034803806 scopus 로고    scopus 로고
    • Novel bicistronic retroviral vector expressing gamma-glutamylcysteine synthetase and the multidrug resistance protein 1 (MRP1) protects cells from MRP1-effluxed drugs and alkylating agents
    • G. Rappa, A. Lorico, M. Hildinger, O. Fodstad, and C. Baum Novel bicistronic retroviral vector expressing gamma-glutamylcysteine synthetase and the multidrug resistance protein 1 (MRP1) protects cells from MRP1-effluxed drugs and alkylating agents Hum Gene Ther 12 2001 1785 1796
    • (2001) Hum Gene Ther , vol.12 , pp. 1785-1796
    • Rappa, G.1    Lorico, A.2    Hildinger, M.3    Fodstad, O.4    Baum, C.5
  • 33
    • 4143085009 scopus 로고    scopus 로고
    • L-Ascorbic acid induces apoptosis in acute myeloid leukemia cells via hydrogen peroxide-mediated mechanisms
    • S. Park, S.S. Han, C.H. Park, E.R. Hahm, S.J. Lee, and H.K. Park l-Ascorbic acid induces apoptosis in acute myeloid leukemia cells via hydrogen peroxide-mediated mechanisms Int J Biochem Cell Biol 36 2004 2180 2195
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2180-2195
    • Park, S.1    Han, S.S.2    Park, C.H.3    Hahm, E.R.4    Lee, S.J.5    Park, H.K.6
  • 34
    • 4344625883 scopus 로고    scopus 로고
    • A critical role of glutathione in determining apoptosis sensitivity and resistance in leukemia cells
    • C. Friesen, Y. Kiess, and K.M. Debatin A critical role of glutathione in determining apoptosis sensitivity and resistance in leukemia cells Cell Death Differ 11 Suppl. 1 2004 S73 S85
    • (2004) Cell Death Differ , vol.11 , Issue.1 SUPPL.
    • Friesen, C.1    Kiess, Y.2    Debatin, K.M.3
  • 35
    • 0023394624 scopus 로고
    • Leishmania mexicana uptake of sodium stibogluconate (pentostam) and pentamidine by parasite and macrophages
    • J.D. Berman, J.V. Gallalee, and B.D. Hansen Leishmania mexicana uptake of sodium stibogluconate (pentostam) and pentamidine by parasite and macrophages Exp Parasitol 64 1987 127 131
    • (1987) Exp Parasitol , vol.64 , pp. 127-131
    • Berman, J.D.1    Gallalee, J.V.2    Hansen, B.D.3
  • 36
    • 0036848182 scopus 로고    scopus 로고
    • Effects of sodium stibogluconate on differentiation and proliferation of human myeloid leukemia cell lines in vitro
    • M.K. Pathak, X. Hu, and T. Yi Effects of sodium stibogluconate on differentiation and proliferation of human myeloid leukemia cell lines in vitro Leukemia 16 2002 2285 2291
    • (2002) Leukemia , vol.16 , pp. 2285-2291
    • Pathak, M.K.1    Hu, X.2    Yi, T.3


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