메뉴 건너뛰기




Volumn 73, Issue 3, 2007, Pages 427-439

Dicoumarol impairs mitochondrial electron transport and pyrimidine biosynthesis in human myeloid leukemia HL-60 cells

Author keywords

Cell cycle; Dicoumarol; Mitochondria; NQO1; Pyrimidines biosynthesis; Superoxide

Indexed keywords

5 METHOXY 1,2 DIMETHYL 3 [(4 NITROPHENOL)METHYL]INDOLE 4,7 DIONE; CYTOCHROME B560; DECYLUBIQUINOL; DICOUMAROL; DIHYDROOROTATE DEHYDROGENASE; ES 936; OROTIC ACID; PYRIMIDINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE) INHIBITOR; SUCCINIC ACID; SUPEROXIDE; THENOYLTRIFLUOROACETONE; UBIQUINOL CYTOCHROME C REDUCTASE; URIDINE;

EID: 33845757115     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2006.10.016     Document Type: Article
Times cited : (37)

References (45)
  • 2
    • 13244275245 scopus 로고    scopus 로고
    • A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73
    • Asher G., Tsvetkov P., Kahana C., and Shaul Y. A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73. Genes Dev 19 (2005) 316-321
    • (2005) Genes Dev , vol.19 , pp. 316-321
    • Asher, G.1    Tsvetkov, P.2    Kahana, C.3    Shaul, Y.4
  • 3
    • 0022968955 scopus 로고
    • Dicoumarol-sensitive glucuronidation of bezo(a)pyrene metabolites in rat liver microsomes
    • Segura-Aguilar J.E., Barreiro V., and Lind C. Dicoumarol-sensitive glucuronidation of bezo(a)pyrene metabolites in rat liver microsomes. Arch Biochem Biophys 251 (1986) 266-275
    • (1986) Arch Biochem Biophys , vol.251 , pp. 266-275
    • Segura-Aguilar, J.E.1    Barreiro, V.2    Lind, C.3
  • 4
    • 0026699018 scopus 로고
    • Inhibition of mouse glutathione transferases and glutathione peroxidase II by dicoumarol and other ligands
    • Mays J.B., and Benson A.M. Inhibition of mouse glutathione transferases and glutathione peroxidase II by dicoumarol and other ligands. Biochem Pharmacol 44 (1992) 921-925
    • (1992) Biochem Pharmacol , vol.44 , pp. 921-925
    • Mays, J.B.1    Benson, A.M.2
  • 5
    • 0037444278 scopus 로고    scopus 로고
    • Dicoumarol: a unique microtubule stabilizing natural product that is synergistic with Taxol
    • Madari H., Panda D., Wilson L., and Jacobs R.S. Dicoumarol: a unique microtubule stabilizing natural product that is synergistic with Taxol. Cancer Res 63 (2003) 1214-1220
    • (2003) Cancer Res , vol.63 , pp. 1214-1220
    • Madari, H.1    Panda, D.2    Wilson, L.3    Jacobs, R.S.4
  • 6
    • 0014439545 scopus 로고
    • Inhibition of mitochondrial respiration by uncouplers of oxidative phosphorylation. II. The site of inhibition of succinate oxidation by the uncouplers
    • Wilson D.H., and Merz R. Inhibition of mitochondrial respiration by uncouplers of oxidative phosphorylation. II. The site of inhibition of succinate oxidation by the uncouplers. Arch Biochem Biophys 129 (1969) 79-85
    • (1969) Arch Biochem Biophys , vol.129 , pp. 79-85
    • Wilson, D.H.1    Merz, R.2
  • 7
    • 0038433339 scopus 로고    scopus 로고
    • The mitochondrial uncoupler dicumarol disrupts the MTT assay
    • Collier A.B., and Pritsos C.A. The mitochondrial uncoupler dicumarol disrupts the MTT assay. Biochem Pharmacol 66 (2003) 281-287
    • (2003) Biochem Pharmacol , vol.66 , pp. 281-287
    • Collier, A.B.1    Pritsos, C.A.2
  • 8
    • 0141592795 scopus 로고    scopus 로고
    • Dicumarol inhibition of NADPH:quinone oxidoreductase induces growth inhibition of pancreatic cancer via a superoxide-mediated mechanism
    • Cullen J.J., Hinkhouse M.M., Grady M., Gaut A.W., Liu J., Zhang Y.P., et al. Dicumarol inhibition of NADPH:quinone oxidoreductase induces growth inhibition of pancreatic cancer via a superoxide-mediated mechanism. Cancer Res 63 (2003) 5513-5520
    • (2003) Cancer Res , vol.63 , pp. 5513-5520
    • Cullen, J.J.1    Hinkhouse, M.M.2    Grady, M.3    Gaut, A.W.4    Liu, J.5    Zhang, Y.P.6
  • 9
    • 3042856798 scopus 로고    scopus 로고
    • Treatment of pancreatic cancer cells with dicumarol induces cytotoxicity and oxidative stress
    • Lewis A., Ough M., Li L., Hinkhouse M.M., Ritchie J.M., Spitz D.R., et al. Treatment of pancreatic cancer cells with dicumarol induces cytotoxicity and oxidative stress. Clin Cancer Res 10 (2004) 4550-4558
    • (2004) Clin Cancer Res , vol.10 , pp. 4550-4558
    • Lewis, A.1    Ough, M.2    Li, L.3    Hinkhouse, M.M.4    Ritchie, J.M.5    Spitz, D.R.6
  • 12
    • 33748313433 scopus 로고    scopus 로고
    • 5-Methoxy-1,2-dimethyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione, a mechanism-based inhibitor of NAD(P)H:quinone oxidoreductase 1, exhibits activity against human pancreatic cancer in vitro and in vivo
    • Dehn D.L., Siegel D., Zafar K.S., Reigan P., Swann E., Moody C.J., et al. 5-Methoxy-1,2-dimethyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione, a mechanism-based inhibitor of NAD(P)H:quinone oxidoreductase 1, exhibits activity against human pancreatic cancer in vitro and in vivo. Mol Cancer Ther 5 (2006) 1702-1709
    • (2006) Mol Cancer Ther , vol.5 , pp. 1702-1709
    • Dehn, D.L.1    Siegel, D.2    Zafar, K.S.3    Reigan, P.4    Swann, E.5    Moody, C.J.6
  • 13
    • 0036139856 scopus 로고    scopus 로고
    • The mitochondrial production of reactive oxygen species: mechanisms and implications in human pathology
    • Lenaz G. The mitochondrial production of reactive oxygen species: mechanisms and implications in human pathology. IUBMB Life 52 (2001) 159-164
    • (2001) IUBMB Life , vol.52 , pp. 159-164
    • Lenaz, G.1
  • 14
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • Muller F.L., Liu Y., and Van Remmen H. Complex III releases superoxide to both sides of the inner mitochondrial membrane. J Biol Chem 279 (2004) 49064-49073
    • (2004) J Biol Chem , vol.279 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3
  • 17
    • 0035977034 scopus 로고    scopus 로고
    • Expression of NAD(P)H:quinone oxidoreductase 1 in HeLa cells: role of hydrogen peroxide and growth phase
    • Bello R.I., Gómez-Díaz C., Navarro F., Alcaín F.J., and Villalba J.M. Expression of NAD(P)H:quinone oxidoreductase 1 in HeLa cells: role of hydrogen peroxide and growth phase. J Biol Chem 276 (2001) 44379-44384
    • (2001) J Biol Chem , vol.276 , pp. 44379-44384
    • Bello, R.I.1    Gómez-Díaz, C.2    Navarro, F.3    Alcaín, F.J.4    Villalba, J.M.5
  • 18
    • 17644394600 scopus 로고    scopus 로고
    • Detection and characterization of the product of hydroethidine and intracellular superoxide by HPLC and limitations of fluorescence
    • Zhao H., Joseph J., Fales H.M., Sokoloski E.A., Levine R.L., Vasquez-Vivar J., et al. Detection and characterization of the product of hydroethidine and intracellular superoxide by HPLC and limitations of fluorescence. Proc Natl Acad Sci USA 102 (2005) 5727-5732
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5727-5732
    • Zhao, H.1    Joseph, J.2    Fales, H.M.3    Sokoloski, E.A.4    Levine, R.L.5    Vasquez-Vivar, J.6
  • 20
    • 0037044847 scopus 로고    scopus 로고
    • Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase
    • Messner K.R., and Imlay J.A. Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase. J Biol Chem 277 (2002) 42563-42571
    • (2002) J Biol Chem , vol.277 , pp. 42563-42571
    • Messner, K.R.1    Imlay, J.A.2
  • 21
    • 0029964226 scopus 로고    scopus 로고
    • Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines
    • Trounce I.A., Kim Y.L., Jun A.S., and Wallace D.C. Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines. Methods Enzymol 264 (1996) 484-509
    • (1996) Methods Enzymol , vol.264 , pp. 484-509
    • Trounce, I.A.1    Kim, Y.L.2    Jun, A.S.3    Wallace, D.C.4
  • 22
    • 0025239273 scopus 로고
    • Isolation of subcellular organelles
    • Storrie B., and Madden E.A. Isolation of subcellular organelles. Methods Enzymol 182 (1990) 203-225
    • (1990) Methods Enzymol , vol.182 , pp. 203-225
    • Storrie, B.1    Madden, E.A.2
  • 23
    • 0042856414 scopus 로고    scopus 로고
    • Biochemical, cytotoxic, and genotoxic effects of ES936, a mechanism-based inhibitor of NAD(P)H:quinone oxidoreductase 1, in cellular systems
    • Dehn D.L., Siegel D., Swann E., Moody C.J., and Ross D. Biochemical, cytotoxic, and genotoxic effects of ES936, a mechanism-based inhibitor of NAD(P)H:quinone oxidoreductase 1, in cellular systems. Mol Pharmacol 64 (2003) 714-720
    • (2003) Mol Pharmacol , vol.64 , pp. 714-720
    • Dehn, D.L.1    Siegel, D.2    Swann, E.3    Moody, C.J.4    Ross, D.5
  • 24
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • Boveris A., Oshino N., and Chance B. The cellular production of hydrogen peroxide. Biochem J 128 (1972) 617-630
    • (1972) Biochem J , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 25
    • 0033369476 scopus 로고    scopus 로고
    • Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity, and relation to aging and longevity
    • Barja G. Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity, and relation to aging and longevity. J Bioenerg Biomembr 31 (1999) 347-366
    • (1999) J Bioenerg Biomembr , vol.31 , pp. 347-366
    • Barja, G.1
  • 26
    • 24144493814 scopus 로고    scopus 로고
    • Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing
    • Guzy R.D., Hoyos B., Robin E., Chen H., Liu L., Mansfield K.D., et al. Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing. Cell Metab 1 (2005) 401-408
    • (2005) Cell Metab , vol.1 , pp. 401-408
    • Guzy, R.D.1    Hoyos, B.2    Robin, E.3    Chen, H.4    Liu, L.5    Mansfield, K.D.6
  • 28
    • 21244503033 scopus 로고    scopus 로고
    • Crystal structure of mitochondrial respiratory membrane protein complex II
    • Sun F., Huo X., Zhai Y., Wang A., Xu J., Su D., et al. Crystal structure of mitochondrial respiratory membrane protein complex II. Cell 121 (2005) 1043-1057
    • (2005) Cell , vol.121 , pp. 1043-1057
    • Sun, F.1    Huo, X.2    Zhai, Y.3    Wang, A.4    Xu, J.5    Su, D.6
  • 29
    • 44049124728 scopus 로고
    • Two-site property of thenoyltrifluoroacetone inhibiting succinate-ubiquinone reductase
    • Xu J.X., and King T.E. Two-site property of thenoyltrifluoroacetone inhibiting succinate-ubiquinone reductase. Sci Chin B 35 (1992) 162-168
    • (1992) Sci Chin B , vol.35 , pp. 162-168
    • Xu, J.X.1    King, T.E.2
  • 30
    • 4043064372 scopus 로고    scopus 로고
    • Mammalian pyrimidine biosynthesis: fresh insights into an ancient pathway
    • Evans D.R., and Guy H.I. Mammalian pyrimidine biosynthesis: fresh insights into an ancient pathway. J Biol Chem 279 (2004) 33035-33038
    • (2004) J Biol Chem , vol.279 , pp. 33035-33038
    • Evans, D.R.1    Guy, H.I.2
  • 32
    • 0019277437 scopus 로고
    • Facilitated transport of uracil and 5-fluorouracil, and permeation of orotic acid into cultured mammalian cells
    • Wohlhueter R.M., McIvor R.S., and Plagemann P.G.W. Facilitated transport of uracil and 5-fluorouracil, and permeation of orotic acid into cultured mammalian cells. J Cell Physiol 104 (1980) 309-319
    • (1980) J Cell Physiol , vol.104 , pp. 309-319
    • Wohlhueter, R.M.1    McIvor, R.S.2    Plagemann, P.G.W.3
  • 33
    • 0347419376 scopus 로고    scopus 로고
    • Antioxidant response induced by serum withdrawal protects HL-60 cells against inhibition of NAD(P)H:quinone oxidoreductase 1
    • Gómez-Díaz C., Bello R.I., López-Lluch G., Forthoffer N., Navas P., and Villalba J.M. Antioxidant response induced by serum withdrawal protects HL-60 cells against inhibition of NAD(P)H:quinone oxidoreductase 1. Biofactors 18 (2003) 219-228
    • (2003) Biofactors , vol.18 , pp. 219-228
    • Gómez-Díaz, C.1    Bello, R.I.2    López-Lluch, G.3    Forthoffer, N.4    Navas, P.5    Villalba, J.M.6
  • 34
    • 0036494316 scopus 로고    scopus 로고
    • Subcellular localization of NAD(P)H:quinone oxidoreductase 1 in human cancer cells
    • Winski S.L., Koutalos Y., Bentley D.L., and Ross D. Subcellular localization of NAD(P)H:quinone oxidoreductase 1 in human cancer cells. Cancer Res 62 (2002) 1420-1424
    • (2002) Cancer Res , vol.62 , pp. 1420-1424
    • Winski, S.L.1    Koutalos, Y.2    Bentley, D.L.3    Ross, D.4
  • 35
    • 77957001185 scopus 로고
    • Assays of Intermediates of the citric acid cycle and related compounds by fluorometric enzyme methods
    • Williamson J.R., and Corkey B.E. Assays of Intermediates of the citric acid cycle and related compounds by fluorometric enzyme methods. Methods Enzymol 13 (1969) 434-513
    • (1969) Methods Enzymol , vol.13 , pp. 434-513
    • Williamson, J.R.1    Corkey, B.E.2
  • 36
    • 11244279161 scopus 로고    scopus 로고
    • A mutation in the SDHC gene of complex II increases oxidative stress, resulting in apoptosis and tumorigenesis
    • Ishii T., Yasuda K., Akatsuka A., Hino O., Hartman P.S., and Ishii N. A mutation in the SDHC gene of complex II increases oxidative stress, resulting in apoptosis and tumorigenesis. Cancer Res 65 (2005) 203-209
    • (2005) Cancer Res , vol.65 , pp. 203-209
    • Ishii, T.1    Yasuda, K.2    Akatsuka, A.3    Hino, O.4    Hartman, P.S.5    Ishii, N.6
  • 37
    • 0043269302 scopus 로고    scopus 로고
    • Function and structure of complex II of the respiratory chain
    • Cecchini G. Function and structure of complex II of the respiratory chain. Annu Rev Biochem 72 (2003) 77-109
    • (2003) Annu Rev Biochem , vol.72 , pp. 77-109
    • Cecchini, G.1
  • 39
    • 33646846683 scopus 로고    scopus 로고
    • 3-Nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme
    • Huang L.-S., Sun G., Cobessi D., Wang A., Shen J.T., Tung E.Y., et al. 3-Nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme. J Biol Chem 281 (2006) 5965-5972
    • (2006) J Biol Chem , vol.281 , pp. 5965-5972
    • Huang, L.-S.1    Sun, G.2    Cobessi, D.3    Wang, A.4    Shen, J.T.5    Tung, E.Y.6
  • 40
    • 0141757479 scopus 로고    scopus 로고
    • DNA damage checkpoint control in cells exposed to ionizing radiation
    • Iliakis G., Wang Y., Guan J., and Wang H. DNA damage checkpoint control in cells exposed to ionizing radiation. Oncogene 22 (2003) 5834-5847
    • (2003) Oncogene , vol.22 , pp. 5834-5847
    • Iliakis, G.1    Wang, Y.2    Guan, J.3    Wang, H.4
  • 41
    • 0028035447 scopus 로고
    • Regulation of cell proliferation under extreme and moderate hypoxia: the role of pyrimidine (deoxy)nucleotides
    • Åmellem Ø., Löffler M., and Pettersen E.O. Regulation of cell proliferation under extreme and moderate hypoxia: the role of pyrimidine (deoxy)nucleotides. Br J Cancer 70 (1994) 857-866
    • (1994) Br J Cancer , vol.70 , pp. 857-866
    • Åmellem, Ø.1    Löffler, M.2    Pettersen, E.O.3
  • 42
    • 33646129234 scopus 로고    scopus 로고
    • Dicoumarol potentiates cisplatin-induced apoptosis mediated by c-Jun N-terminal kinase in p53 wild-type urogenital cancer cell lines
    • Watanabe J., Nishiyama H., Matsui Y., Ito M., Kawanishi H., Kamoto T., et al. Dicoumarol potentiates cisplatin-induced apoptosis mediated by c-Jun N-terminal kinase in p53 wild-type urogenital cancer cell lines. Oncogene 25 (2006) 2500-2508
    • (2006) Oncogene , vol.25 , pp. 2500-2508
    • Watanabe, J.1    Nishiyama, H.2    Matsui, Y.3    Ito, M.4    Kawanishi, H.5    Kamoto, T.6
  • 43
    • 1242274637 scopus 로고    scopus 로고
    • NAD(P)H:quinone oxidoreductase 1 expression, hydrogen peroxide levels and growth phase in HeLa cells
    • Bello R.I., Gómez-Díaz C., Navas P., and Villalba J.M. NAD(P)H:quinone oxidoreductase 1 expression, hydrogen peroxide levels and growth phase in HeLa cells. Methods Enzymol 382 (2004) 234-243
    • (2004) Methods Enzymol , vol.382 , pp. 234-243
    • Bello, R.I.1    Gómez-Díaz, C.2    Navas, P.3    Villalba, J.M.4
  • 44
    • 0021320276 scopus 로고
    • Effect of plasma concentrations of uridine on pyrimidine biosynthesis in cultured L1210 cells
    • Karle J.M., Anderson L.W., and Cysyk R.L. Effect of plasma concentrations of uridine on pyrimidine biosynthesis in cultured L1210 cells. J Biol Chem 259 (1984) 67-72
    • (1984) J Biol Chem , vol.259 , pp. 67-72
    • Karle, J.M.1    Anderson, L.W.2    Cysyk, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.