메뉴 건너뛰기




Volumn 15, Issue 12, 2011, Pages 2911-2921

Inhibition of mitochondrial respiration and rapid depletion of mitochondrial glutathione by β-phenethyl isothiocyanate: Mechanisms for anti-leukemia activity

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE; NITRIC OXIDE; PHENETHYL ISOTHIOCYANATE; PROTEIN KINASE FES; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; ROTENONE;

EID: 80155134262     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2011.4170     Document Type: Article
Times cited : (68)

References (48)
  • 1
    • 0036673665 scopus 로고    scopus 로고
    • Glutathione depletion enforces the mitochondrial permeability transition and causes cell death in Bcl-2 overexpressing HL60 cells
    • Armstrong JS and Jones DP. Glutathione depletion enforces the mitochondrial permeability transition and causes cell death in Bcl-2 overexpressing HL60 cells. FASEB J 16: 1263-1265, 2002.
    • (2002) FASEB J , vol.16 , pp. 1263-1265
    • Armstrong, J.S.1    Jones, D.P.2
  • 2
    • 0030744048 scopus 로고    scopus 로고
    • Bcl-xL overexpression attenuates glutathione depletion in FL5.12 cells following interleukin-3 withdrawal
    • Bojes HK, et al. Bcl-xL overexpression attenuates glutathione depletion in FL5.12 cells following interleukin-3 withdrawal. Biochem J 325 (Pt 2): 315-319, 1997.
    • (1997) Biochem J , vol.325 , Issue.PART 2 , pp. 315-319
    • Bojes, H.K.1
  • 3
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH:quinone oxidoreductase (complex I)
    • Brandt U. Energy converting NADH:quinone oxidoreductase (complex I). Annu Rev Biochem 75: 69-92, 2006.
    • (2006) Annu Rev Biochem , vol.75 , pp. 69-92
    • Brandt, U.1
  • 4
    • 77956604712 scopus 로고    scopus 로고
    • Kinetics and regulation of mammalian NADHubiquinone oxidoreductase (Complex I)
    • Chen X, et al. Kinetics and regulation of mammalian NADHubiquinone oxidoreductase (Complex I). Biophys J 99: 1426-1436, 2010.
    • (2010) Biophys J , vol.99 , pp. 1426-1436
    • Chen, X.1
  • 5
    • 53849093043 scopus 로고    scopus 로고
    • PEITC induces G1 cell cycle arrest on HT-29 cells through the activation of p38 MAPK signaling pathway
    • Cheung KL, et al. PEITC induces G1 cell cycle arrest on HT-29 cells through the activation of p38 MAPK signaling pathway. AAPS J 10: 277-281, 2008.
    • (2008) AAPS J , vol.10 , pp. 277-281
    • Cheung, K.L.1
  • 6
    • 77449106593 scopus 로고    scopus 로고
    • Molecular targets of dietary phenethyl isothiocyanate and sulforaphane for cancer chemoprevention
    • Cheung KL and Kong AN. Molecular targets of dietary phenethyl isothiocyanate and sulforaphane for cancer chemoprevention. AAPS J 12: 87-97, 2010.
    • (2010) AAPS J , vol.12 , pp. 87-97
    • Cheung, K.L.1    Kong, A.N.2
  • 7
    • 77952055601 scopus 로고    scopus 로고
    • Mitochondrial complex i in the network of known and unknown facts
    • Chomova M and Racay P. Mitochondrial complex I in the network of known and unknown facts. Gen Physiol Biophys 29: 3-11, 2010.
    • (2010) Gen Physiol Biophys , vol.29 , pp. 3-11
    • Chomova, M.1    Racay, P.2
  • 8
    • 18844427352 scopus 로고    scopus 로고
    • S-glutathionylation in human platelets by a thiol-disulfide exchange-independent mechanism
    • Dalle-Donne I, et al. S-glutathionylation in human platelets by a thiol-disulfide exchange-independent mechanism. Free Radic Biol Med 38: 1501-1510, 2005.
    • (2005) Free Radic Biol Med , vol.38 , pp. 1501-1510
    • Dalle-Donne, I.1
  • 9
    • 0037155862 scopus 로고    scopus 로고
    • Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion
    • Eaton P, et al. Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion. J Biol Chem 277: 9806-9811, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 9806-9811
    • Eaton, P.1
  • 10
    • 0032406895 scopus 로고    scopus 로고
    • Mitochondrial glutathione: Importance and transport
    • Fernandez-Checa JC, et al. Mitochondrial glutathione: importance and transport. Semin Liver Dis 18: 389-401, 1998.
    • (1998) Semin Liver Dis , vol.18 , pp. 389-401
    • Fernandez-Checa, J.C.1
  • 11
    • 0031852094 scopus 로고    scopus 로고
    • Oxidative stress: Role of mitochondria and protection by glutathione
    • Fernandez-Checa JC, et al. Oxidative stress: role of mitochondria and protection by glutathione. Biofactors 8: 7-11, 1998.
    • (1998) Biofactors , vol.8 , pp. 7-11
    • Fernandez-Checa, J.C.1
  • 12
    • 70349172938 scopus 로고    scopus 로고
    • Apoptosis and glutathione: Beyond an antioxidant
    • Franco R and Cidlowski JA. Apoptosis and glutathione: beyond an antioxidant. Cell Death Differ 16: 1303-1314, 2009.
    • (2009) Cell Death Differ , vol.16 , pp. 1303-1314
    • Franco, R.1    Cidlowski, J.A.2
  • 13
    • 18344390036 scopus 로고    scopus 로고
    • Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes
    • Fratelli M, et al. Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes. Proc Natl Acad Sci USA 99: 3505-3510, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3505-3510
    • Fratelli, M.1
  • 14
    • 0042665896 scopus 로고    scopus 로고
    • Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells
    • Fratelli M, et al. Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells. Proteomics 3: 1154-1161, 2003.
    • (2003) Proteomics , vol.3 , pp. 1154-1161
    • Fratelli, M.1
  • 15
    • 4344625883 scopus 로고    scopus 로고
    • A critical role of glutathione in determining apoptosis sensitivity and resistance in leukemia cells
    • Friesen C, Kiess Y, and Debatin KM. A critical role of glutathione in determining apoptosis sensitivity and resistance in leukemia cells. Cell Death Differ 11 Suppl 1: S73-S85, 2004.
    • (2004) Cell Death Differ 11 Suppl , vol.1
    • Friesen, C.1    Kiess, Y.2    Debatin, K.M.3
  • 16
    • 79959982112 scopus 로고    scopus 로고
    • Phenethyl isothiocyanate exhibits antileukemic activity in vitro and in vivo by inactivation of Akt and activation of JNK pathways
    • Gao N, et al. Phenethyl isothiocyanate exhibits antileukemic activity in vitro and in vivo by inactivation of Akt and activation of JNK pathways. Cell Death Dis 2: e140, 2011.
    • (2011) Cell Death Dis , vol.2
    • Gao, N.1
  • 17
    • 68149167106 scopus 로고    scopus 로고
    • Phenethyl isothiocyanate inhibits STAT3 activation in prostate cancer cells
    • Gong A, et al. Phenethyl isothiocyanate inhibits STAT3 activation in prostate cancer cells. Mol Nutr Food Res 53: 878-886, 2009.
    • (2009) Mol Nutr Food Res , vol.53 , pp. 878-886
    • Gong, A.1
  • 18
    • 29644436194 scopus 로고    scopus 로고
    • Involvement of mitochondrial aggregation in arsenic trioxide (As2O3)-induced apoptosis in human glioblastoma cells
    • Haga N, Fujita N, and Tsuruo T. Involvement of mitochondrial aggregation in arsenic trioxide (As2O3)-induced apoptosis in human glioblastoma cells. Cancer Sci 96: 825-833, 2005.
    • (2005) Cancer Sci , vol.96 , pp. 825-833
    • Haga, N.1    Fujita, N.2    Tsuruo, T.3
  • 19
    • 24644469955 scopus 로고    scopus 로고
    • Sites and mechanisms of aconitase inactivation by peroxynitrite: Modulation by citrate and glutathione
    • Han D, et al. Sites and mechanisms of aconitase inactivation by peroxynitrite: modulation by citrate and glutathione. Biochemistry 44: 11986-11996, 2005.
    • (2005) Biochemistry , vol.44 , pp. 11986-11996
    • Han, D.1
  • 20
    • 33745791542 scopus 로고    scopus 로고
    • Mechanisms of liver injury. III. Role of glutathione redox status in liver injury
    • Han D, et al. Mechanisms of liver injury. III. Role of glutathione redox status in liver injury. Am J Physiol Gastrointest Liver Physiol 291: G1-G7, 2006.
    • (2006) Am J Physiol Gastrointest Liver Physiol , vol.291
    • Han, D.1
  • 21
    • 0038771142 scopus 로고    scopus 로고
    • The nuclear encoded subunits of complex i from bovine heart mitochondria
    • Hirst J, et al. The nuclear encoded subunits of complex I from bovine heart mitochondria. Biochim Biophys Acta 1604: 135-150, 2003.
    • (2003) Biochim Biophys Acta , vol.1604 , pp. 135-150
    • Hirst, J.1
  • 22
    • 0042388396 scopus 로고    scopus 로고
    • The roles of JNK and apoptotic signaling pathways in PEITC-mediated responses in human HT-29 colon adenocarcinoma cells
    • Hu R, et al. The roles of JNK and apoptotic signaling pathways in PEITC-mediated responses in human HT-29 colon adenocarcinoma cells. Carcinogenesis 24: 1361-1367, 2003.
    • (2003) Carcinogenesis , vol.24 , pp. 1361-1367
    • Hu, R.1
  • 23
    • 54049146740 scopus 로고    scopus 로고
    • Complex i within oxidatively stressed bovine heart mitochondria is glutathionylated on Cys-531 and Cys-704 of the 75-kDa subunit: Potential role of CYS residues in decreasing oxidative damage
    • Hurd TR, et al. Complex I within oxidatively stressed bovine heart mitochondria is glutathionylated on Cys-531 and Cys-704 of the 75-kDa subunit: potential role of CYS residues in decreasing oxidative damage. J Biol Chem 283: 24801-24815, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 24801-24815
    • Hurd, T.R.1
  • 24
    • 23344431898 scopus 로고    scopus 로고
    • Isothiocyanates induce cell cycle arrest, apoptosis and mitochondrial potential depolarization in HL-60 and multidrug-resistant cell lines
    • Jakubikova J, Bao Y, and Sedlak J. Isothiocyanates induce cell cycle arrest, apoptosis and mitochondrial potential depolarization in HL-60 and multidrug-resistant cell lines. Anticancer Res 25: 3375-3386, 2005.
    • (2005) Anticancer Res , vol.25 , pp. 3375-3386
    • Jakubikova, J.1    Bao, Y.2    Sedlak, J.3
  • 26
    • 33747092049 scopus 로고    scopus 로고
    • Combination treatment with arsenic trioxide and sulindac augments their apoptotic potential in lung cancer cells through activation of caspase cascade and mitochondrial dysfunction
    • Kim HR, et al. Combination treatment with arsenic trioxide and sulindac augments their apoptotic potential in lung cancer cells through activation of caspase cascade and mitochondrial dysfunction. Int J Oncol 28: 1401-1408, 2006.
    • (2006) Int J Oncol , vol.28 , pp. 1401-1408
    • Kim, H.R.1
  • 27
    • 33746454283 scopus 로고    scopus 로고
    • Role of oxidative stress in the apoptosis of hepatocellular carcinoma induced by combination of arsenic trioxide and ascorbic acid
    • Li JJ, et al. Role of oxidative stress in the apoptosis of hepatocellular carcinoma induced by combination of arsenic trioxide and ascorbic acid. Acta Pharmacol Sin 27: 1078-1084, 2006.
    • (2006) Acta Pharmacol Sin , vol.27 , pp. 1078-1084
    • Li, J.J.1
  • 28
    • 52049113028 scopus 로고    scopus 로고
    • Covalent binding to tubulin by isothiocyanates. A mechanism of cell growth arrest and apoptosis
    • Mi L, et al. Covalent binding to tubulin by isothiocyanates. A mechanism of cell growth arrest and apoptosis. J Biol Chem 283: 22136-22146, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 22136-22146
    • Mi, L.1
  • 29
    • 67650547972 scopus 로고    scopus 로고
    • Cancer preventive isothiocyanates induce selective degradation of cellular alpha-and beta-tubulins by proteasomes
    • Mi L, et al. Cancer preventive isothiocyanates induce selective degradation of cellular alpha-and beta-tubulins by proteasomes. J Biol Chem 284: 17039-17051, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 17039-17051
    • Mi, L.1
  • 30
    • 79251567380 scopus 로고    scopus 로고
    • Isothiocyanates inhibit proteasome activity and proliferation of multiple myeloma cells
    • Mi L, Gan N, and Chung FL. Isothiocyanates inhibit proteasome activity and proliferation of multiple myeloma cells. Carcinogenesis 32: 216-223, 2011.
    • (2011) Carcinogenesis , vol.32 , pp. 216-223
    • Mi, L.1    Gan, N.2    Chung, F.L.3
  • 31
    • 0345146921 scopus 로고    scopus 로고
    • Reversible inactivation of alphaketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status
    • Nulton-Persson AC, et al. Reversible inactivation of alphaketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status. Biochemistry 42: 4235-4242, 2003.
    • (2003) Biochemistry , vol.42 , pp. 4235-4242
    • Nulton-Persson, A.C.1
  • 32
    • 0034953329 scopus 로고    scopus 로고
    • Bcl-2-dependent oxidation of pyruvate dehydrogenase-E2, a primary biliary cirrhosis autoantigen, during apoptosis
    • Odin JA, et al. Bcl-2-dependent oxidation of pyruvate dehydrogenase-E2, a primary biliary cirrhosis autoantigen, during apoptosis. J Clin Invest 108: 223-232, 2001.
    • (2001) J Clin Invest , vol.108 , pp. 223-232
    • Odin, J.A.1
  • 33
    • 33845718704 scopus 로고    scopus 로고
    • Mitochondrial respiration defects in cancer cells cause activation of Akt survival pathway through a redox-mediated mechanism
    • Pelicano H, et al. Mitochondrial respiration defects in cancer cells cause activation of Akt survival pathway through a redox-mediated mechanism. J Cell Biol 175: 913-923, 2006.
    • (2006) J Cell Biol , vol.175 , pp. 913-923
    • Pelicano, H.1
  • 34
    • 77952776083 scopus 로고    scopus 로고
    • Glutathionylation of adenine nucleotide translocase induced by carbon monoxide prevents mitochondrial membrane permeabilization and apoptosis
    • Queiroga CS, et al. Glutathionylation of adenine nucleotide translocase induced by carbon monoxide prevents mitochondrial membrane permeabilization and apoptosis. J Biol Chem 285: 17077-17088, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 17077-17088
    • Queiroga, C.S.1
  • 35
    • 0346362068 scopus 로고    scopus 로고
    • Nitric oxide and mitochondrial complex IV
    • Sarti P, et al. Nitric oxide and mitochondrial complex IV. IUBMB Life 55: 605-611, 2003.
    • (2003) IUBMB Life , vol.55 , pp. 605-611
    • Sarti, P.1
  • 36
    • 33748146888 scopus 로고    scopus 로고
    • Selective killing of oncogenically transformed cells through a ROS-mediated mechanism by beta-phenylethyl isothiocyanate
    • Trachootham D, et al. Selective killing of oncogenically transformed cells through a ROS-mediated mechanism by beta-phenylethyl isothiocyanate. Cancer Cell 10: 241-252, 2006.
    • (2006) Cancer Cell , vol.10 , pp. 241-252
    • Trachootham, D.1
  • 37
    • 52649153465 scopus 로고    scopus 로고
    • Effective elimination of fludarabineresistant CLL cells by PEITC through a redox-mediated mechanism
    • Trachootham D, et al. Effective elimination of fludarabineresistant CLL cells by PEITC through a redox-mediated mechanism. Blood 112: 1912-1922, 2008.
    • (2008) Blood 112 , pp. 1912-1922
    • Trachootham, D.1
  • 39
    • 77952476911 scopus 로고    scopus 로고
    • Suppression of inflammatory mediators by cruciferous vegetable-derived indole-3-carbinol and phenylethyl isothiocyanate in lipopolysaccharideactivated macrophages
    • 293642
    • Tsai JT, Liu HC, and Chen YH. Suppression of inflammatory mediators by cruciferous vegetable-derived indole-3-carbinol and phenylethyl isothiocyanate in lipopolysaccharideactivated macrophages. Mediators Inflamm 2010: 293642, 2010.
    • Mediators Inflamm , vol.2010 , pp. 2010
    • Tsai, J.T.1    Liu, H.C.2    Chen, Y.H.3
  • 40
    • 0033230015 scopus 로고    scopus 로고
    • BCL-2 and glutathione: Alterations in cellular redox state that regulate apoptosis sensitivity
    • Voehringer DW. BCL-2 and glutathione: alterations in cellular redox state that regulate apoptosis sensitivity. Free Radic Biol Med 27: 945-950, 1999.
    • (1999) Free Radic Biol Med , vol.27 , pp. 945-950
    • Voehringer, D.W.1
  • 41
    • 79851505114 scopus 로고    scopus 로고
    • Selective Depletion of mutant p53 by cancer chemopreventive isothiocyanates and their structure-activity relationships
    • Wang X, et al. Selective Depletion of mutant p53 by cancer chemopreventive isothiocyanates and their structure-activity relationships. J Med Chem 54: 809-816, 2011.
    • (2011) J Med Chem , vol.54 , pp. 809-816
    • Wang, X.1
  • 42
    • 65749104457 scopus 로고    scopus 로고
    • Inhibition of hypoxia inducible factor by phenethyl isothiocyanate
    • Wang XH, et al. Inhibition of hypoxia inducible factor by phenethyl isothiocyanate. Biochem Pharmacol 78: 261-272, 2009.
    • (2009) Biochem Pharmacol , vol.78 , pp. 261-272
    • Wang, X.H.1
  • 43
    • 79958859670 scopus 로고    scopus 로고
    • Benzyl isothiocyanate (BITC) and phenethyl isothiocyanate (PEITC)-mediated generation of reactive oxygen species causes cell cycle arrest and induces apoptosis via activation of caspase-3, mitochondria dysfunction and nitric oxide (NO) in human osteogenic sarcoma U-2 OS cells
    • Wu CL, et al. Benzyl isothiocyanate (BITC) and phenethyl isothiocyanate (PEITC)-mediated generation of reactive oxygen species causes cell cycle arrest and induces apoptosis via activation of caspase-3, mitochondria dysfunction and nitric oxide (NO) in human osteogenic sarcoma U-2 OS cells. J Orthop Res 29: 1199-1209, 2011.
    • (2011) J Orthop Res , vol.29 , pp. 1199-1209
    • Wu, C.L.1
  • 44
    • 77956218104 scopus 로고    scopus 로고
    • Phenethyl isothiocyanate inhibits oxidative phosphorylation to trigger reactive oxygen species-mediated death of human prostate cancer cells
    • Xiao D, et al. Phenethyl isothiocyanate inhibits oxidative phosphorylation to trigger reactive oxygen species-mediated death of human prostate cancer cells. J Biol Chem 285: 26558-26569, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 26558-26569
    • Xiao, D.1
  • 45
    • 77951029200 scopus 로고    scopus 로고
    • P66Shc is indispensable for phenethyl isothiocyanate-induced apoptosis in human prostate cancer cells
    • Xiao D and Singh SV. p66Shc is indispensable for phenethyl isothiocyanate-induced apoptosis in human prostate cancer cells. Cancer Res 70: 3150-3158, 2010.
    • (2010) Cancer Res , vol.70 , pp. 3150-3158
    • Xiao, D.1    Singh, S.V.2
  • 46
    • 0035863273 scopus 로고    scopus 로고
    • Involvement of glutathione metabolism in the cytotoxicity of the phenethyl isothiocyanate and its cysteine conjugate to human leukaemia cells in vitro
    • Xu K and Thornalley PJ. Involvement of glutathione metabolism in the cytotoxicity of the phenethyl isothiocyanate and its cysteine conjugate to human leukaemia cells in vitro. Biochem Pharmacol 61: 165-177, 2001.
    • (2001) Biochem Pharmacol , vol.61 , pp. 165-177
    • Xu, K.1    Thornalley, P.J.2
  • 47
    • 45149100643 scopus 로고    scopus 로고
    • Effective killing of Gleevec-resistant CML cells with T315I mutation by a natural compound PEITC through redox-mediated mechanism
    • Zhang H, et al. Effective killing of Gleevec-resistant CML cells with T315I mutation by a natural compound PEITC through redox-mediated mechanism. Leukemia 22: 1191-1199, 2008.
    • (2008) Leukemia , vol.22 , pp. 1191-1199
    • Zhang, H.1
  • 48
    • 35748976238 scopus 로고    scopus 로고
    • Glutathione binding to the Bcl-2 homology-3 domain groove: A molecular basis for Bcl-2 antioxidant function at mitochondria
    • Zimmermann AK, et al. Glutathione binding to the Bcl-2 homology-3 domain groove: a molecular basis for Bcl-2 antioxidant function at mitochondria. J Biol Chem 282: 29296-29304, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 29296-29304
    • Zimmermann, A.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.