메뉴 건너뛰기




Volumn 13, Issue 7, 2000, Pages 550-556

The putative benzene metabolite 2,3,5-tris(glutathion-S-yl)hydroquinone depletes glutathione, stimulates sphingomyelin turnover, and induces apoptosis in HL-60 cells

Author keywords

[No Author keywords available]

Indexed keywords

BENZENE DERIVATIVE; CASPASE; CASPASE 3; CASPASE 7; CATALASE; CERAMIDE; GLUTATHIONE PEROXIDASE; HYDROQUINONE DERIVATIVE; REACTIVE OXYGEN METABOLITE; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE;

EID: 0033931806     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx0000015     Document Type: Article
Times cited : (33)

References (50)
  • 2
    • 0019401794 scopus 로고
    • Toxic effects of benzene and benzene metabolites on granulopoietic stem cells and bone marrow cellularity in mice
    • Tunek, A., Olofssan, T., and Berlin, M. (1981) Toxic effects of benzene and benzene metabolites on granulopoietic stem cells and bone marrow cellularity in mice. Toxicol. Appl. Pharmacol. 59, 149-156.
    • (1981) Toxicol. Appl. Pharmacol. , vol.59 , pp. 149-156
    • Tunek, A.1    Olofssan, T.2    Berlin, M.3
  • 6
    • 0023621645 scopus 로고
    • An interaction of benzene metabolites reproduces the myelotoxicity observed with benzene exposure
    • Eastmond, D. A., Smith, M. T., and Irons, R. D. (1987) An interaction of benzene metabolites reproduces the myelotoxicity observed with benzene exposure. Toxicol. Appl. Pharmacol. 91, 85-95.
    • (1987) Toxicol. Appl. Pharmacol. , vol.91 , pp. 85-95
    • Eastmond, D.A.1    Smith, M.T.2    Irons, R.D.3
  • 7
    • 0030744058 scopus 로고    scopus 로고
    • Identification of quinol-thioethers in bone marrow of hydroquinone/phenol-treated rats and mice and their potential role in benzene-mediated hematotoxicity
    • Bratton, S. B., Lau, S. S., and Monks, T. J. (1997) Identification of quinol-thioethers in bone marrow of hydroquinone/phenol-treated rats and mice and their potential role in benzene-mediated hematotoxicity. Chem. Res. Toxicol. 10, 859-865.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 859-865
    • Bratton, S.B.1    Lau, S.S.2    Monks, T.J.3
  • 8
    • 0031796277 scopus 로고    scopus 로고
    • Immunochemical analysis of quinol-thioether-derived covalent protein adducts in rodent species sensitive and resistant to quinol-thioether-mediated nephrotoxicity
    • Kleiner, H. E., Jones, T. W., Monks, T. J., and Lau, S. S. (1998) Immunochemical analysis of quinol-thioether-derived covalent protein adducts in rodent species sensitive and resistant to quinol-thioether-mediated nephrotoxicity. Chem. Res. Toxicol. 11, 1291-1300.
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 1291-1300
    • Kleiner, H.E.1    Jones, T.W.2    Monks, T.J.3    Lau, S.S.4
  • 10
    • 0029826230 scopus 로고    scopus 로고
    • Hydroquinone, a bioreactive metabolite of benzene, inhibits apoptosis in myeloblasts
    • Hazel, B. A., Baum, C., and Kalf, G. F. (1996) Hydroquinone, a bioreactive metabolite of benzene, inhibits apoptosis in myeloblasts. Stem Cells 14, 730-742.
    • (1996) Stem Cells , vol.14 , pp. 730-742
    • Hazel, B.A.1    Baum, C.2    Kalf, G.F.3
  • 11
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson, C. B. (1995) Apoptosis in the pathogenesis and treatment of disease. Science 267, 1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 12
    • 0030448021 scopus 로고    scopus 로고
    • Functions of ceramide in coordinating cellular responses to stress
    • Hannun, Y. A. (1996) Functions of ceramide in coordinating cellular responses to stress. Science 274, 1855-1859.
    • (1996) Science , vol.274 , pp. 1855-1859
    • Hannun, Y.A.1
  • 13
    • 0027353039 scopus 로고
    • Sphingomyelinases
    • Spence, M. W. (1993) Sphingomyelinases. Adv. Lipid Res. 26, 3-23.
    • (1993) Adv. Lipid Res. , vol.26 , pp. 3-23
    • Spence, M.W.1
  • 14
    • 0026560014 scopus 로고
    • Tumor necrosis factor-α activates the sphingomyelin signal transduction pathway in a cell-free system
    • Dressler, K. A., Mathias, S., and Kolesnick, R. N. (1992) Tumor necrosis factor-α activates the sphingomyelin signal transduction pathway in a cell-free system. Science 255, 1715-1718.
    • (1992) Science , vol.255 , pp. 1715-1718
    • Dressler, K.A.1    Mathias, S.2    Kolesnick, R.N.3
  • 15
    • 0026726492 scopus 로고
    • Interleukin-1-mediated PGE2 production and sphingomyelin metabolism. Evidence for the regulation of cyclooxygenase gene expression by sphingosine and ceramide
    • Ballou, L. R., Chao, C. P., Holness, M. A., Barker, S. C., and Raghow, R. (1992) Interleukin-1-mediated PGE2 production and sphingomyelin metabolism. Evidence for the regulation of cyclooxygenase gene expression by sphingosine and ceramide. J. Biol. Chem. 267, 20044-20050.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20044-20050
    • Ballou, L.R.1    Chao, C.P.2    Holness, M.A.3    Barker, S.C.4    Raghow, R.5
  • 17
    • 0028176730 scopus 로고
    • 1-β-D-Arabinofuranosylcytosine stimulates ceramide and diglyceride formation in HL-60 cells
    • Strum, J. C., Small, G. W., Pauig, S. B., and Daniel, L. W. (1994) 1-β-D-Arabinofuranosylcytosine stimulates ceramide and diglyceride formation in HL-60 cells. J. Biol. Chem. 269, 15493-15497.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15493-15497
    • Strum, J.C.1    Small, G.W.2    Pauig, S.B.3    Daniel, L.W.4
  • 20
    • 0025889011 scopus 로고
    • Characterization of a ceramide-activated protein kinase: Stimulation by tumor necrosis factor a
    • Mathias, S., Dressler, K. A., and Kolesnick, R. N. (1991) Characterization of a ceramide-activated protein kinase: stimulation by tumor necrosis factor a. Proc. Natl. Acad. Sci. U.S.A. 88, 10009-10013.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10009-10013
    • Mathias, S.1    Dressler, K.A.2    Kolesnick, R.N.3
  • 21
    • 0027162553 scopus 로고
    • Sphingomyelinase and ceramide activate mitogen-activated protein kinase in myeloid HL-60 cells
    • Raines, M. A., Kolesnick, R. N., and Golde, D. W. (1993) Sphingomyelinase and ceramide activate mitogen-activated protein kinase in myeloid HL-60 cells. J. Biol. Chem. 268, 14572-14575.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14572-14575
    • Raines, M.A.1    Kolesnick, R.N.2    Golde, D.W.3
  • 23
    • 0026723048 scopus 로고
    • Ceramide stimulates a cytosolic protein phosphatase
    • Dobrowsky, R. T., and Hannun, Y. A. (1992) Ceramide stimulates a cytosolic protein phosphatase. J. Biol. Chem. 267, 5048-5051.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5048-5051
    • Dobrowsky, R.T.1    Hannun, Y.A.2
  • 24
    • 1842375100 scopus 로고    scopus 로고
    • Implication of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis
    • Quillet-Mary, A., Jaffrézou, J.-P., Mansat, V., Bordier, C., Naval, J., and Laurent, G. (1997) Implication of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis. J. Biol. Chem. 272, 21388-21395.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21388-21395
    • Quillet-Mary, A.1    Jaffrézou, J.-P.2    Mansat, V.3    Bordier, C.4    Naval, J.5    Laurent, G.6
  • 25
    • 0030856714 scopus 로고    scopus 로고
    • Direct inhibition of mitochondrial respiratory chain complex III by cell-permeable ceramide
    • Gudz, T. I., Tserng, K.-Y., and Hoppel, C. L. (1997) Direct inhibition of mitochondrial respiratory chain complex III by cell-permeable ceramide. J. Biol. Chem. 272, 24154-24158.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24154-24158
    • Gudz, T.I.1    Tserng, K.-Y.2    Hoppel, C.L.3
  • 26
    • 0026458406 scopus 로고
    • TNF activates NF-κB by phosphatidylcholine-specific phospholipase C-induced "acidic" sphingomyelin breakdown
    • Schütze, S., Potthoff, K., Machleidt, T., Berkovic, D., Wiegmann, K., and Krönke, M. (1992) TNF activates NF-κB by phosphatidylcholine-specific phospholipase C-induced "acidic" sphingomyelin breakdown. Cell 71, 765-776.
    • (1992) Cell , vol.71 , pp. 765-776
    • Schütze, S.1    Potthoff, K.2    Machleidt, T.3    Berkovic, D.4    Wiegmann, K.5    Krönke, M.6
  • 27
    • 0027183695 scopus 로고
    • Tumor necrosis factor activation of the sphingomyelinase pathway signals nuclear factor-κB translocation in intact HL-60 cells
    • Yang, Z., Costanzo, M., Golde, D. W., and Kolesnick, R. N. (1993) Tumor necrosis factor activation of the sphingomyelinase pathway signals nuclear factor-κB translocation in intact HL-60 cells. J. Biol. Chem. 268, 20520-20523.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20520-20523
    • Yang, Z.1    Costanzo, M.2    Golde, D.W.3    Kolesnick, R.N.4
  • 30
    • 0030960327 scopus 로고    scopus 로고
    • Inhibition of the neutral magnesium-dependent sphingomyelinase by gluthathione
    • Liu, B., and Hannun, Y. A. (1997) Inhibition of the neutral magnesium-dependent sphingomyelinase by gluthathione. J. Biol. Chem. 272, 16281-16287.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16281-16287
    • Liu, B.1    Hannun, Y.A.2
  • 31
    • 0024237151 scopus 로고
    • Sequential oxidation and glutathione addition to 1,4-benzoquinone: Correlation of toxicity with increased glutathione substitution
    • Lau, S. S., Hill, B. A., Highet, R. J., and Monks, T. J. (1988) Sequential oxidation and glutathione addition to 1,4-benzoquinone: correlation of toxicity with increased glutathione substitution. Mol. Pharmacol. 34, 829-836.
    • (1988) Mol. Pharmacol. , vol.34 , pp. 829-836
    • Lau, S.S.1    Hill, B.A.2    Highet, R.J.3    Monks, T.J.4
  • 32
    • 0024322509 scopus 로고
    • Glutathione measurement by high-performance liquid chromatography separation and fluorometric detection of the glutathione-orthophthalaldehyde adduct
    • Neuschwander-Tetri, B. A., and Roll, F. J. (1989) Glutathione measurement by high-performance liquid chromatography separation and fluorometric detection of the glutathione-orthophthalaldehyde adduct. Anal. Biochem. 179, 236-241.
    • (1989) Anal. Biochem. , vol.179 , pp. 236-241
    • Neuschwander-Tetri, B.A.1    Roll, F.J.2
  • 34
    • 0022970190 scopus 로고
    • Quantitative measurement of sn-1,2-diacylglycerols present in platelets, hepatocytes, and ras- And sis-transformed normal rat kidney cells
    • Preiss, J., Loomis, C. R., Bishop, W. R., Stein, R., Niedel, J. E., and Bell, R. M. (1986) Quantitative measurement of sn-1,2-diacylglycerols present in platelets, hepatocytes, and ras- and sis-transformed normal rat kidney cells. J. Biol. Chem. 261, 8597-8600.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8597-8600
    • Preiss, J.1    Loomis, C.R.2    Bishop, W.R.3    Stein, R.4    Niedel, J.E.5    Bell, R.M.6
  • 35
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., and Wang, X. (1997) Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 36
    • 0025213022 scopus 로고
    • 14C]-hydroquinone and the effect of γ-glutamyl transpeptidase inhibition
    • 14C]-hydroquinone and the effect of γ-glutamyl transpeptidase inhibition. Toxicol. Appl. Pharmacol. 103, 121-132.
    • (1990) Toxicol. Appl. Pharmacol. , vol.103 , pp. 121-132
    • Lau, S.S.1    Monks, T.J.2
  • 37
    • 0020530011 scopus 로고
    • Cystathionase: A potential cytoplasmic marker of hematopoietic differentiation
    • Link, D., Drebing, C., and Glode, L. M. (1983) Cystathionase: a potential cytoplasmic marker of hematopoietic differentiation. Blut 47, 31-39.
    • (1983) Blut , vol.47 , pp. 31-39
    • Link, D.1    Drebing, C.2    Glode, L.M.3
  • 39
    • 1842604189 scopus 로고
    • Glutathione export by human lymphoid cells: Depletion of glutathione by inhibition of its synthesis decreases export and increases sensitivity to irradiation
    • Dethmers, J. K., and Meister, A. (1981) Glutathione export by human lymphoid cells: depletion of glutathione by inhibition of its synthesis decreases export and increases sensitivity to irradiation. Proc. Natl Acad. Sci. U.S.A. 78, 7492-7496.
    • (1981) Proc. Natl Acad. Sci. U.S.A. , vol.78 , pp. 7492-7496
    • Dethmers, J.K.1    Meister, A.2
  • 40
    • 0030789179 scopus 로고    scopus 로고
    • The level of intracellular glutathione is a key regulator for the induction of stress-activated signal transduction pathways including Jun N-terminal protein kinases and p38 kinase by alkylating agents
    • Wilhelm, D., Bender, K., Knebel, A., and Angel, P. (1997) The level of intracellular glutathione is a key regulator for the induction of stress-activated signal transduction pathways including Jun N-terminal protein kinases and p38 kinase by alkylating agents. Mol. Cell. Biol. 17, 4792-4800.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4792-4800
    • Wilhelm, D.1    Bender, K.2    Knebel, A.3    Angel, P.4
  • 41
    • 0031781921 scopus 로고    scopus 로고
    • Ceramide accumulation during oxidant renal tubular injury: Mechanisms and potential consequences
    • Zager, R. A., Conrad, D. S., and Burkhart, K. (1998) Ceramide accumulation during oxidant renal tubular injury: mechanisms and potential consequences. J. Am. Soc. Nephrol. 9, 1670-1680.
    • (1998) J. Am. Soc. Nephrol. , vol.9 , pp. 1670-1680
    • Zager, R.A.1    Conrad, D.S.2    Burkhart, K.3
  • 42
    • 0032496143 scopus 로고    scopus 로고
    • Superoxide in apoptosis: Mitochondrial generation triggered by cytochrome c loss
    • Cai, Y., and Jones, D. P. (1998) Superoxide in apoptosis: mitochondrial generation triggered by cytochrome c loss. J. Biol. Chem. 273, 11401-11404.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11401-11404
    • Cai, Y.1    Jones, D.P.2
  • 44
    • 0025938304 scopus 로고
    • The role of y-glutamyl transpeptidase in hydroquinone-glutathione conjugate mediated nephrotoxicity
    • Witmer, C. M., Snyder, R. R., Jollow, D. J., Kalf, G. F., Kocsis, J. J., and Sipes, I. G., Eds. Plenum Press, New York
    • Hill, B. A., Lo, H., Monks, T. J., and Lau, S. S. (1990) The role of y-glutamyl transpeptidase in hydroquinone-glutathione conjugate mediated nephrotoxicity. In Biological Reactive Intermediates IV (Witmer, C. M., Snyder, R. R., Jollow, D. J., Kalf, G. F., Kocsis, J. J., and Sipes, I. G., Eds.) pp 749-751, Plenum Press, New York.
    • (1990) Biological Reactive Intermediates IV , pp. 749-751
    • Hill, B.A.1    Lo, H.2    Monks, T.J.3    Lau, S.S.4
  • 45
    • 0031973203 scopus 로고    scopus 로고
    • Importance of the redox state of cytochrome c during caspase activation in cytosolic extracts
    • Hampton, M. B., Zhivotovsky, B., Slater, A. F. G., Burgess, D. H., and Orrenius, S. (1998) Importance of the redox state of cytochrome c during caspase activation in cytosolic extracts. Biochem. J. 329, 95-99.
    • (1998) Biochem. J. , vol.329 , pp. 95-99
    • Hampton, M.B.1    Zhivotovsky, B.2    Slater, A.F.G.3    Burgess, D.H.4    Orrenius, S.5
  • 46
    • 0343376119 scopus 로고    scopus 로고
    • Mechanism of dithiocarbamate inhibition of apoptosis: Thiol oxidation by dithiocarbamate disulfides directly inhibits processing of the caspase-3 proenzyme
    • Nobel, C. S., Burgess, D. H., Zhivotovsky, B., Burkitt, M. J., Orrenius, S., and Slater, A. F. (1997) Mechanism of dithiocarbamate inhibition of apoptosis: thiol oxidation by dithiocarbamate disulfides directly inhibits processing of the caspase-3 proenzyme. Chem. Res. Toxicol. 10, 636-643.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 636-643
    • Nobel, C.S.1    Burgess, D.H.2    Zhivotovsky, B.3    Burkitt, M.J.4    Orrenius, S.5    Slater, A.F.6
  • 47
    • 0032537608 scopus 로고    scopus 로고
    • Cytochrome c release and caspase activation in hydrogen peroxide- And tributyltin-induced apoptosis
    • Stridh, H., Kimland, M., Jones, D. P., Orrenius, S., and Hampton, M. B. (1998) Cytochrome c release and caspase activation in hydrogen peroxide- and tributyltin-induced apoptosis. FEBS Lett. 429, 351-355.
    • (1998) FEBS Lett. , vol.429 , pp. 351-355
    • Stridh, H.1    Kimland, M.2    Jones, D.P.3    Orrenius, S.4    Hampton, M.B.5
  • 48
    • 0033568238 scopus 로고    scopus 로고
    • Arsenic trioxide selectively induces acute promyelocytic leukemia cell apoptosis via a hydrogen peroxide-dependent pathway
    • Jing, Y., Dai, J., Chalmers-Redman, R. M., Tatton, W. G., and Waxman, S. (1999) Arsenic trioxide selectively induces acute promyelocytic leukemia cell apoptosis via a hydrogen peroxide-dependent pathway. Blood 94, 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
  • 49
    • 0032557458 scopus 로고    scopus 로고
    • Overexpression of manganese superoxide dismutase suppresses tumor necrosis factor-induced apoptosis and activation of nuclear transcription factor-κB and activated protein-1
    • Manna, S. K., Zhang, H. J., Yan, T., Oberley, L. W., and Aggarwal, B. B. (1998) Overexpression of manganese superoxide dismutase suppresses tumor necrosis factor-induced apoptosis and activation of nuclear transcription factor-κB and activated protein-1. J. Biol. Chem. 273, 13245-13254.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13245-13254
    • Manna, S.K.1    Zhang, H.J.2    Yan, T.3    Oberley, L.W.4    Aggarwal, B.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.