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Volumn 417, Issue 3, 2009, Pages 717-726

Inhibition of energy-producing pathways of HepG2 cells by 3-bromopyruvate

Author keywords

3 bromopyruvate; Glycolysis; Hepatocellular carcinoma; HepG2 cell; Mitochondrion; Oxygen consumption; Tumour cell

Indexed keywords

3-BROMOPYRUVATE; GLYCOLYSIS; HEPATOCELLULAR CARCINOMA; HEPG2 CELL; OXYGEN CONSUMPTION; TUMOUR CELL;

EID: 59849092584     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20080805     Document Type: Article
Times cited : (148)

References (47)
  • 1
    • 11444255268 scopus 로고
    • On respiratory impairment in cancer cells
    • Warburg, O. (1956) On respiratory impairment in cancer cells. Science 124, 269-270
    • (1956) Science , vol.124 , pp. 269-270
    • Warburg, O.1
  • 5
    • 34249945104 scopus 로고    scopus 로고
    • The cancer cell's 'power plants' as promising therapeutic targets: An overview
    • Pedersen, P. L. (2007) The cancer cell's 'power plants' as promising therapeutic targets: an overview. J. Bioenerg. Biomembr. 39, 1-12
    • (2007) J. Bioenerg. Biomembr , vol.39 , pp. 1-12
    • Pedersen, P.L.1
  • 6
    • 0015217110 scopus 로고
    • The inactivation of succinate dehydrogenase by bromopyruvate
    • Sanborn, B. M, Felberg, N. T and Hollocher, T. C. (1971) The inactivation of succinate dehydrogenase by bromopyruvate. Biochim. Biophys. Acta 227, 219-231
    • (1971) Biochim. Biophys. Acta , vol.227 , pp. 219-231
    • Sanborn, B.M.1    Felberg, N.T.2    Hollocher, T.C.3
  • 7
    • 0017580293 scopus 로고
    • Mechanism of pigeon liver malic enzyme: Kinetics, specificity, and half-site stoichiometry of the alkylation of a cysteinyl residue by the substrate-inhibitor bromopyruvate
    • Chang, G. G. and Hsu, R. Y. (1977) Mechanism of pigeon liver malic enzyme: kinetics, specificity, and half-site stoichiometry of the alkylation of a cysteinyl residue by the substrate-inhibitor bromopyruvate. Biochemistry 16, 311-320
    • (1977) Biochemistry , vol.16 , pp. 311-320
    • Chang, G.G.1    Hsu, R.Y.2
  • 8
    • 0017802302 scopus 로고
    • Mechanism of inactivation of brain glutamic decarboxylase by 3-bromopyruvate
    • Tunnicliff, G. and Ngo, T. T. (1978) Mechanism of inactivation of brain glutamic decarboxylase by 3-bromopyruvate. Int. J. Biochem. 9, 249-252
    • (1978) Int. J. Biochem , vol.9 , pp. 249-252
    • Tunnicliff, G.1    Ngo, T.T.2
  • 9
    • 0025866317 scopus 로고
    • Duck liver malic enzyme: Sequence of a tryptic peptide containing the cysteine residue labeled by the substrate analog bromopyruvate
    • Satterlee, J. and Hsu, R. Y. (1991) Duck liver malic enzyme: sequence of a tryptic peptide containing the cysteine residue labeled by the substrate analog bromopyruvate. Biochim. Biophys. Acta 1079, 247-252
    • (1991) Biochim. Biophys. Acta , vol.1079 , pp. 247-252
    • Satterlee, J.1    Hsu, R.Y.2
  • 10
    • 0345493676 scopus 로고    scopus 로고
    • Involvement of a-cysteine-62 and β-tryptophan-135 in human pyruvate dehydrogenase catalysis
    • Korotchkina, L. G., Showkat, A. M. and Patel, M. S. (1999) Involvement of a-cysteine-62 and β-tryptophan-135 in human pyruvate dehydrogenase catalysis. Arch. Biochem. Biophys. 369, 277-287
    • (1999) Arch. Biochem. Biophys , vol.369 , pp. 277-287
    • Korotchkina, L.G.1    Showkat, A.M.2    Patel, M.S.3
  • 11
    • 0035829074 scopus 로고    scopus 로고
    • Glucose catabolism in the rabbit VX2 tumor model for liver cancer: Characterization and targeting hexokinase
    • Ko, Y. H., Pedersen, P. L. and Geschwind, J. F. (2001) Glucose catabolism in the rabbit VX2 tumor model for liver cancer: characterization and targeting hexokinase. Cancer Lett. 173, 83-91
    • (2001) Cancer Lett , vol.173 , pp. 83-91
    • Ko, Y.H.1    Pedersen, P.L.2    Geschwind, J.F.3
  • 12
    • 13844250595 scopus 로고    scopus 로고
    • Hypoxia stimulates proliferation of human hepatoma cells through the induction of hexokinase II expression
    • Gwak, G., Yoon, J., Kim, K., Lee, H., Chung, J. and Gores, G. (2005) Hypoxia stimulates proliferation of human hepatoma cells through the induction of hexokinase II expression. J. Hepatol. 42, 358-364
    • (2005) J. Hepatol , vol.42 , pp. 358-364
    • Gwak, G.1    Yoon, J.2    Kim, K.3    Lee, H.4    Chung, J.5    Gores, G.6
  • 13
    • 0037099685 scopus 로고    scopus 로고
    • Novel therapy for liver cancer: Direct intra-arterial injection of a potent inhibitor of ATP production
    • Geschwind, J. F., Ko, Y. K., Torbenson, M. S., Magee, C. and Pedersen, P. L. (2002) Novel therapy for liver cancer: direct intra-arterial injection of a potent inhibitor of ATP production. Cancer Res. 62, 3909-3913
    • (2002) Cancer Res , vol.62 , pp. 3909-3913
    • Geschwind, J.F.1    Ko, Y.K.2    Torbenson, M.S.3    Magee, C.4    Pedersen, P.L.5
  • 15
    • 12544256565 scopus 로고    scopus 로고
    • Inhibition of glycolysis in cancer cells: A novel strategy to overcome compound resistance associated with mitochondrial respiratory defect and hypoxia
    • Xu, R., Pelicano, Y. Z, Carew, J. S, Feng, L., Bhalla, K. N, Keating, M. J. and Huang, P. (2005) Inhibition of glycolysis in cancer cells: a novel strategy to overcome compound resistance associated with mitochondrial respiratory defect and hypoxia. Cancer Res. 65, 613-621
    • (2005) Cancer Res , vol.65 , pp. 613-621
    • Xu, R.1    Pelicano, Y.Z.2    Carew, J.S.3    Feng, L.4    Bhalla, K.N.5    Keating, M.J.6    Huang, P.7
  • 16
    • 34748922322 scopus 로고    scopus 로고
    • Apoptosis-inducing antitumor efficacy of hexokinase II inhibitor in hepatocellular carcinoma
    • Kim, W., Yoon, J. H., Jeong, J. M., Cheon, G. J., Lee, T. S., Yang, J. I., Park, S. C. and Lee, H. S. (2007) Apoptosis-inducing antitumor efficacy of hexokinase II inhibitor in hepatocellular carcinoma. Mol. Cancer Ther. 6, 2554-2562
    • (2007) Mol. Cancer Ther , vol.6 , pp. 2554-2562
    • Kim, W.1    Yoon, J.H.2    Jeong, J.M.3    Cheon, G.J.4    Lee, T.S.5    Yang, J.I.6    Park, S.C.7    Lee, H.S.8
  • 17
    • 0028087602 scopus 로고
    • A tetrazolium-based colorimetric MTT assay to quantitate human monocyte mediated cytotoxicity against leukemic cells from cell lines and patients with acute myeloid leukemia
    • Van De Loosdrecht, A. A. (1994) A tetrazolium-based colorimetric MTT assay to quantitate human monocyte mediated cytotoxicity against leukemic cells from cell lines and patients with acute myeloid leukemia. J. Immunol. Methods 174, 311-320
    • (1994) J. Immunol. Methods , vol.174 , pp. 311-320
    • Van De Loosdrecht, A.A.1
  • 20
    • 4544355934 scopus 로고    scopus 로고
    • Mitochondrial bound hexokinase activity as a preventive antioxidant defense: Steady-state ADP formation as a regulatory mechanism of membrane potential and reactive oxygen species generation in mitochondria
    • da-Silva, W. S., Gomez-Puyou, A., de Gomez-Puyou, M. T., Moreno-Sanchez, R., De Felice, F. G., de Meis, L., Oliveira, M. F. and Galina, A. (2004) Mitochondrial bound hexokinase activity as a preventive antioxidant defense: steady-state ADP formation as a regulatory mechanism of membrane potential and reactive oxygen species generation in mitochondria. J. Biol. Chem. 279, 39846-39855
    • (2004) J. Biol. Chem , vol.279 , pp. 39846-39855
    • da-Silva, W.S.1    Gomez-Puyou, A.2    de Gomez-Puyou, M.T.3    Moreno-Sanchez, R.4    De Felice, F.G.5    de Meis, L.6    Oliveira, M.F.7    Galina, A.8
  • 21
    • 0016416451 scopus 로고
    • Phosphoglucose isomerase of human erythrocytes and cardiac tissue
    • Gracy, R. W. and Tilley, B. E. (1975) Phosphoglucose isomerase of human erythrocytes and cardiac tissue. Methods Enzymol. 41, 392-400
    • (1975) Methods Enzymol , vol.41 , pp. 392-400
    • Gracy, R.W.1    Tilley, B.E.2
  • 22
    • 0014799858 scopus 로고
    • Regulation of D-fructose 1-phosphate kinase by potassium ion
    • Sapico, V. and Anderson, R. L. (1970) Regulation of D-fructose 1-phosphate kinase by potassium ion. J. Biol. Chem. 245, 3252-3256
    • (1970) J. Biol. Chem , vol.245 , pp. 3252-3256
    • Sapico, V.1    Anderson, R.L.2
  • 23
    • 0026453106 scopus 로고    scopus 로고
    • Molina y Vedia, L., McDonald, B., Reep, B., Brüne, B., Di Silvio, M., Billiar, T. R. and Lapetina, E. G. (1992) Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation. J. Biol. Chem. 267, 24929-24932
    • Molina y Vedia, L., McDonald, B., Reep, B., Brüne, B., Di Silvio, M., Billiar, T. R. and Lapetina, E. G. (1992) Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation. J. Biol. Chem. 267, 24929-24932
  • 24
    • 0028806739 scopus 로고
    • Purification and properties of the pyruvate kinase isozyme M1 from the pig brain
    • Farrar, G. and Farrar, W. W. (1995) Purification and properties of the pyruvate kinase isozyme M1 from the pig brain. Int. J. Biochem. Cell Biol. 27, 1145-1151
    • (1995) Int. J. Biochem. Cell Biol , vol.27 , pp. 1145-1151
    • Farrar, G.1    Farrar, W.W.2
  • 26
    • 0028848236 scopus 로고
    • Flavinylation of succinate: Ubiquinone oxidoreductase from Saccharomyces cerevisiae
    • Robinson, K. M. and Lemire, B. D. (1995) Flavinylation of succinate: ubiquinone oxidoreductase from Saccharomyces cerevisiae. Methods Enzymol. 256, 34-51
    • (1995) Methods Enzymol , vol.256 , pp. 34-51
    • Robinson, K.M.1    Lemire, B.D.2
  • 28
    • 0021325746 scopus 로고
    • Quantitation of lactate by a kinetic method with an extend range of linearity and low dependence on experimental variables
    • Hamilton, S. D. and Pardue, H.L. (1984) Quantitation of lactate by a kinetic method with an extend range of linearity and low dependence on experimental variables. Clin. Chem. 30, 226-229
    • (1984) Clin. Chem , vol.30 , pp. 226-229
    • Hamilton, S.D.1    Pardue, H.L.2
  • 29
    • 0032407621 scopus 로고    scopus 로고
    • Oxidative stress and cytotoxicity induced by ferric-nitrolotriacetate in HepG2 cells that express cytochrome P450 2E1
    • Sakurai, K. and Cederbaum, A. I. (1998) Oxidative stress and cytotoxicity induced by ferric-nitrolotriacetate in HepG2 cells that express cytochrome P450 2E1. Mol. Pharmacol. 54, 1024-1035
    • (1998) Mol. Pharmacol , vol.54 , pp. 1024-1035
    • Sakurai, K.1    Cederbaum, A.I.2
  • 33
    • 0033584845 scopus 로고    scopus 로고
    • Threshold effect and tissue specificity. Implication for mitochondrial cytopathies
    • Rossignol, R., Malgat, M., Mazat, J. P. and Letellier, T. (1999) Threshold effect and tissue specificity. Implication for mitochondrial cytopathies. J. Biol. Chem. 274, 33426-33432
    • (1999) J. Biol. Chem , vol.274 , pp. 33426-33432
    • Rossignol, R.1    Malgat, M.2    Mazat, J.P.3    Letellier, T.4
  • 34
    • 33646799069 scopus 로고    scopus 로고
    • Global and regional burden of disease and risk factors, 2001: Systematic analysis of population health data
    • Lopez, A. D., Mathers, C. D., Ezzati, M., Jamison, D. T. and Murray, C. J. (2006) Global and regional burden of disease and risk factors, 2001: systematic analysis of population health data. Lancet 367, 1747-1757
    • (2006) Lancet , vol.367 , pp. 1747-1757
    • Lopez, A.D.1    Mathers, C.D.2    Ezzati, M.3    Jamison, D.T.4    Murray, C.J.5
  • 35
    • 0028879393 scopus 로고
    • The anti-glycolytic activity of 3-bromopyruvate on mature boar spermatozoa in vitro
    • Jones, A. R., Gillan, L. and Milmlow, D. (1995) The anti-glycolytic activity of 3-bromopyruvate on mature boar spermatozoa in vitro. Contraception 52, 317-320
    • (1995) Contraception , vol.52 , pp. 317-320
    • Jones, A.R.1    Gillan, L.2    Milmlow, D.3
  • 36
    • 37449034854 scopus 로고    scopus 로고
    • Beyond aerobic glycolysis: Transformed cells can engage in glutamine metabolism that exceeds the requirement for protein and nucleotide synthesis
    • DeBerardinis, R. J., Mancuso, A., Daikhin, E., Nissim, I., Yudkoff, M., Wehrli, S. and Thompson, C. B. (2007) Beyond aerobic glycolysis: transformed cells can engage in glutamine metabolism that exceeds the requirement for protein and nucleotide synthesis. Proc. Natl. Acad. Sci. U.S.A. 104, 19345-19350
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 19345-19350
    • DeBerardinis, R.J.1    Mancuso, A.2    Daikhin, E.3    Nissim, I.4    Yudkoff, M.5    Wehrli, S.6    Thompson, C.B.7
  • 37
    • 0014600354 scopus 로고
    • Effects of bromopyruvate on the control and catalytic properties of glutamate dehydrogenase
    • Baker, J. P. and Rabin, B. R. (1969) Effects of bromopyruvate on the control and catalytic properties of glutamate dehydrogenase. Eur. J. Biochem. 11, 154-159
    • (1969) Eur. J. Biochem , vol.11 , pp. 154-159
    • Baker, J.P.1    Rabin, B.R.2
  • 38
    • 39449114808 scopus 로고    scopus 로고
    • Akt mediates mitochondrial protection in cardiomyocytes through phosphorylation of mitochondrial hexokinase-II
    • Miyamoto, S., Murphy, A. N. and Brown, J. H. (2008) Akt mediates mitochondrial protection in cardiomyocytes through phosphorylation of mitochondrial hexokinase-II. Cell Death Differ. 15, 521-529
    • (2008) Cell Death Differ , vol.15 , pp. 521-529
    • Miyamoto, S.1    Murphy, A.N.2    Brown, J.H.3
  • 39
    • 32244436232 scopus 로고    scopus 로고
    • Mitochondria: A target for cancer therapy
    • Armstrong, J. S. (2006) Mitochondria: a target for cancer therapy. Br. J. Pharmacol. 147, 239-248
    • (2006) Br. J. Pharmacol , vol.147 , pp. 239-248
    • Armstrong, J.S.1
  • 40
    • 46649106720 scopus 로고    scopus 로고
    • Hexokinase II detachment from mitochondria triggers apoptosis through the permeability transition pore independent of voltage-dependent anion channels
    • Chiara, F., Castellaro, D., Marin, O., Petronilli, V., Brusilow, W. S., Juhaszova, M., Sollott, S. J., Forte, M., Bernardi, P. and Rasola, A. (2008) Hexokinase II detachment from mitochondria triggers apoptosis through the permeability transition pore independent of voltage-dependent anion channels. PLoS ONE 19, e1852
    • (2008) PLoS ONE , vol.19
    • Chiara, F.1    Castellaro, D.2    Marin, O.3    Petronilli, V.4    Brusilow, W.S.5    Juhaszova, M.6    Sollott, S.J.7    Forte, M.8    Bernardi, P.9    Rasola, A.10
  • 41
    • 34247485841 scopus 로고    scopus 로고
    • Role of the mitochondrial membrane permeability transition in cell death
    • Tsujimoto, Y. and Shimizu, S. (2007) Role of the mitochondrial membrane permeability transition in cell death. Apoptosis 12, 835-840
    • (2007) Apoptosis , vol.12 , pp. 835-840
    • Tsujimoto, Y.1    Shimizu, S.2
  • 42
    • 0036510541 scopus 로고    scopus 로고
    • Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis
    • Pastorino, J. G., Shulga, N. and Hoek, J. B. (2002) Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis. J. Biol. Chem. 277, 7610-7618
    • (2002) J. Biol. Chem , vol.277 , pp. 7610-7618
    • Pastorino, J.G.1    Shulga, N.2    Hoek, J.B.3
  • 43
    • 0034642510 scopus 로고    scopus 로고
    • Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis
    • Costantini, P., Belzacq, A. S., Vieira, H. L., Larochette, N., de Pablo, M. A., Zamzami, N., Susin, S. A., Brenner, C. and Kroemer, G. (2000) Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis. Oncogene 19, 307-314
    • (2000) Oncogene , vol.19 , pp. 307-314
    • Costantini, P.1    Belzacq, A.S.2    Vieira, H.L.3    Larochette, N.4    de Pablo, M.A.5    Zamzami, N.6    Susin, S.A.7    Brenner, C.8    Kroemer, G.9
  • 44
    • 0020739856 scopus 로고
    • Interconversions between different sulfhydryl-related kinetic states in glucokinase
    • Tippett, P. S. and Neet, K. E. (1983) Interconversions between different sulfhydryl-related kinetic states in glucokinase. Arch. Biochem. Biophys. 222, 285-298
    • (1983) Arch. Biochem. Biophys , vol.222 , pp. 285-298
    • Tippett, P.S.1    Neet, K.E.2
  • 45
    • 0023698329 scopus 로고
    • Structural requirements of alloxan and ninhydrin for glucokinase inhibition and of glucose for protection against inhibition
    • Lenzen, S., Brand, F. H. and Panten, U. (1988) Structural requirements of alloxan and ninhydrin for glucokinase inhibition and of glucose for protection against inhibition. Br. J. Pharmacol. 95, 851-859
    • (1988) Br. J. Pharmacol , vol.95 , pp. 851-859
    • Lenzen, S.1    Brand, F.H.2    Panten, U.3
  • 46
    • 0025344966 scopus 로고
    • Alloxan and ninhydrin inhibition of hexokinase from pancreatic islets and tumoural insulin-secreting cells
    • Lenzen, S., Freytag, S., Panten, U., Flatt, P. R. and Bailey, C. J. (1990) Alloxan and ninhydrin inhibition of hexokinase from pancreatic islets and tumoural insulin-secreting cells. Pharmacol. Toxicol. 66, 157-162
    • (1990) Pharmacol. Toxicol , vol.66 , pp. 157-162
    • Lenzen, S.1    Freytag, S.2    Panten, U.3    Flatt, P.R.4    Bailey, C.J.5
  • 47
    • 0034653920 scopus 로고    scopus 로고
    • Importance of cysteine residues for the stability and catalytic activity of human pancreatic β-cell glucokinase
    • Tiedge, M., Richter, T. and Lenzen, S. (2000) Importance of cysteine residues for the stability and catalytic activity of human pancreatic β-cell glucokinase. Arch. Biochem. Biophys. 375, 251-260
    • (2000) Arch. Biochem. Biophys , vol.375 , pp. 251-260
    • Tiedge, M.1    Richter, T.2    Lenzen, S.3


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