메뉴 건너뛰기




Volumn 40, Issue 8, 2006, Pages 1377-1390

The superoxide dismutase inhibitor diethyldithiocarbamate has antagonistic effects on apoptosis by triggering both cytochrome c release and caspase inhibition

Author keywords

Apoptosis; Bax; Caspases; Cytochrome c; DDC; Free radicals; Mitochondria; Reactive oxygen species; Superoxide; Superoxide dismutase

Indexed keywords

CASPASE; CYTOCHROME C; DIETHYLDITHIOCARBAMIC ACID; PROTEIN BAX; REACTIVE OXYGEN METABOLITE;

EID: 33646030654     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2005.12.005     Document Type: Article
Times cited : (40)

References (76)
  • 1
    • 0036478970 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species in cell death signaling
    • Fleury C., Mignotte B., and Vayssiere J.L. Mitochondrial reactive oxygen species in cell death signaling. Biochimie 84 (2002) 131-141
    • (2002) Biochimie , vol.84 , pp. 131-141
    • Fleury, C.1    Mignotte, B.2    Vayssiere, J.L.3
  • 2
    • 0036644215 scopus 로고    scopus 로고
    • Regulation and measurement of oxidative stress in apoptosis
    • Curtin J.F., Donovan M., and Cotter T.G. Regulation and measurement of oxidative stress in apoptosis. J. Immunol. Methods 265 (2002) 49-72
    • (2002) J. Immunol. Methods , vol.265 , pp. 49-72
    • Curtin, J.F.1    Donovan, M.2    Cotter, T.G.3
  • 3
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1
    • Schreck R., Rieber P., and Baeuerle P.A. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1. EMBO J. 10 (1991) 2247-2258
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 5
    • 0024542475 scopus 로고
    • Inhibition of target cell mitochondrial electron transfer by tumor necrosis factor
    • Lancaster Jr. J.R., Laster S.M., and Gooding L.R. Inhibition of target cell mitochondrial electron transfer by tumor necrosis factor. FEBS Lett. 248 (1989) 169-174
    • (1989) FEBS Lett. , vol.248 , pp. 169-174
    • Lancaster Jr., J.R.1    Laster, S.M.2    Gooding, L.R.3
  • 6
    • 0026713818 scopus 로고
    • Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation
    • Schulze-Osthoff K., Bakker A.C., Vanhaesebroeck B., Beyaert R., Jacob W.A., and Fiers W. Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation. J. Biol. Chem. 267 (1992) 5317-5323
    • (1992) J. Biol. Chem. , vol.267 , pp. 5317-5323
    • Schulze-Osthoff, K.1    Bakker, A.C.2    Vanhaesebroeck, B.3    Beyaert, R.4    Jacob, W.A.5    Fiers, W.6
  • 7
    • 3142604666 scopus 로고    scopus 로고
    • Characterization of H2O2-induced acute apoptosis in cultured neural stem/progenitor cells
    • Lin H.J., Wang X., Shaffer K.M., Sasaki C.Y., and Ma W. Characterization of H2O2-induced acute apoptosis in cultured neural stem/progenitor cells. FEBS Lett. 570 (2004) 102-106
    • (2004) FEBS Lett. , vol.570 , pp. 102-106
    • Lin, H.J.1    Wang, X.2    Shaffer, K.M.3    Sasaki, C.Y.4    Ma, W.5
  • 8
    • 1642493646 scopus 로고    scopus 로고
    • Mitochondria permeability transition-dependent tert-butyl hydroperoxide-induced apoptosis in hepatoma HepG2 cells
    • Piret J.P., Arnould T., Fuks B., Chatelain P., Remacle J., and Michiels C. Mitochondria permeability transition-dependent tert-butyl hydroperoxide-induced apoptosis in hepatoma HepG2 cells. Biochem. Pharmacol. 67 (2004) 611-620
    • (2004) Biochem. Pharmacol. , vol.67 , pp. 611-620
    • Piret, J.P.1    Arnould, T.2    Fuks, B.3    Chatelain, P.4    Remacle, J.5    Michiels, C.6
  • 9
    • 0038241619 scopus 로고    scopus 로고
    • Mechanisms for sensitization to TNF-induced apoptosis by acute glutathione depletion in murine hepatocytes
    • Matsumaru K., Ji C., and Kaplowitz N. Mechanisms for sensitization to TNF-induced apoptosis by acute glutathione depletion in murine hepatocytes. Hepatology 37 (2003) 1425-1434
    • (2003) Hepatology , vol.37 , pp. 1425-1434
    • Matsumaru, K.1    Ji, C.2    Kaplowitz, N.3
  • 10
    • 0035980154 scopus 로고    scopus 로고
    • Induction of apoptosis in p53-deficient human hepatoma cell line by wild-type p53 gene transduction: inhibition by antioxidant
    • Lee K.H., Kim K.C., Jung Y.J., Ham Y.H., Jang J.J., Kwon H., Sung Y.C., Kim S.H., Han S.K., and Kim C.M. Induction of apoptosis in p53-deficient human hepatoma cell line by wild-type p53 gene transduction: inhibition by antioxidant. Mol. Cells 12 (2001) 17-24
    • (2001) Mol. Cells , vol.12 , pp. 17-24
    • Lee, K.H.1    Kim, K.C.2    Jung, Y.J.3    Ham, Y.H.4    Jang, J.J.5    Kwon, H.6    Sung, Y.C.7    Kim, S.H.8    Han, S.K.9    Kim, C.M.10
  • 11
    • 0037114490 scopus 로고    scopus 로고
    • Role of antioxidants in the O-hydroxyethyl-D-(Ser)8-cyclosporine A (SDZ IMM125)-induced apoptosis in rat hepatocytes
    • Grub S., Trommer W.E., and Wolf A. Role of antioxidants in the O-hydroxyethyl-D-(Ser)8-cyclosporine A (SDZ IMM125)-induced apoptosis in rat hepatocytes. Biochem. Pharmacol. 64 (2002) 1725-1736
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 1725-1736
    • Grub, S.1    Trommer, W.E.2    Wolf, A.3
  • 12
    • 14744274465 scopus 로고    scopus 로고
    • Regulation of Fas (CD95)-induced apoptotic and necrotic cell death by reactive oxygen species in macrophages
    • Medan D., Wang L., Toledo D., Lu B., Stehlik C., Jiang B.H., Shi X., and Rojanasakul Y. Regulation of Fas (CD95)-induced apoptotic and necrotic cell death by reactive oxygen species in macrophages. J. Cell. Physiol. 203 (2005) 78-84
    • (2005) J. Cell. Physiol. , vol.203 , pp. 78-84
    • Medan, D.1    Wang, L.2    Toledo, D.3    Lu, B.4    Stehlik, C.5    Jiang, B.H.6    Shi, X.7    Rojanasakul, Y.8
  • 14
    • 3042771402 scopus 로고    scopus 로고
    • Oxidative stress-associated mitochondrial dysfunction in corticosteroid-treated muscle cells
    • Oshima Y., Kuroda Y., Kunishige M., Matsumoto T., and Mitsui T. Oxidative stress-associated mitochondrial dysfunction in corticosteroid-treated muscle cells. Muscle Nerve 30 (2004) 49-54
    • (2004) Muscle Nerve , vol.30 , pp. 49-54
    • Oshima, Y.1    Kuroda, Y.2    Kunishige, M.3    Matsumoto, T.4    Mitsui, T.5
  • 15
    • 0036703753 scopus 로고    scopus 로고
    • A Bax-induced pro-oxidant state is critical for cytochrome c release during programmed neuronal death
    • Kirkland R.A., Windelborn J.A., Kasprzak J.M., and Franklin J.L. A Bax-induced pro-oxidant state is critical for cytochrome c release during programmed neuronal death. J. Neurosci. 22 (2002) 6480-6490
    • (2002) J. Neurosci. , vol.22 , pp. 6480-6490
    • Kirkland, R.A.1    Windelborn, J.A.2    Kasprzak, J.M.3    Franklin, J.L.4
  • 17
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • Riedl S.J., and Shi Y. Molecular mechanisms of caspase regulation during apoptosis. Nat. Rev. Mol. Cell. Biol. 5 (2004) 897-907
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 18
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang X. The expanding role of mitochondria in apoptosis. Genes Dev. 15 (2001) 2922-2933
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 19
    • 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. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91 (1997) 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
  • 20
    • 0033396491 scopus 로고    scopus 로고
    • Fas ligand-induced apoptosis
    • Nagata S. Fas ligand-induced apoptosis. Annu. Rev. Genet. 33 (1999) 29-55
    • (1999) Annu. Rev. Genet. , vol.33 , pp. 29-55
    • Nagata, S.1
  • 21
    • 0242656497 scopus 로고    scopus 로고
    • Death receptor-induced cell killing
    • Thorburn A. Death receptor-induced cell killing. Cell Signal. 16 (2004) 139-144
    • (2004) Cell Signal. , vol.16 , pp. 139-144
    • Thorburn, A.1
  • 22
    • 0037276437 scopus 로고    scopus 로고
    • The CD95(APO-1/Fas) DISC and beyond
    • Peter M.E., and Krammer P.H. The CD95(APO-1/Fas) DISC and beyond. Cell Death Differ. 10 (2003) 26-35
    • (2003) Cell Death Differ. , vol.10 , pp. 26-35
    • Peter, M.E.1    Krammer, P.H.2
  • 23
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., and Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94 (1998) 481-490
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 24
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C.J., and Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94 (1998) 491-501
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 25
    • 0027328056 scopus 로고
    • Depletion of the mitochondrial electron transport abrogates the cytotoxic and gene-inductive effects of TNF
    • Schulze-Osthoff K., Beyaert R., Vandevoorde V., Haegeman G., and Fiers W. Depletion of the mitochondrial electron transport abrogates the cytotoxic and gene-inductive effects of TNF. EMBO J. 12 (1993) 3095-3104
    • (1993) EMBO J. , vol.12 , pp. 3095-3104
    • Schulze-Osthoff, K.1    Beyaert, R.2    Vandevoorde, V.3    Haegeman, G.4    Fiers, W.5
  • 26
    • 1842375100 scopus 로고    scopus 로고
    • Implication of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis
    • Quillet-Mary A., Jaffrezou J.P., Mansat V., Bordier C., Naval J., and Laurent G. Implication of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis. J. Biol. Chem. 272 (1997) 21388-21395
    • (1997) J. Biol. Chem. , vol.272 , pp. 21388-21395
    • Quillet-Mary, A.1    Jaffrezou, J.P.2    Mansat, V.3    Bordier, C.4    Naval, J.5    Laurent, G.6
  • 27
    • 0030997261 scopus 로고    scopus 로고
    • Activation of CPP32-like protease in tumor necrosis factor-induced apoptosis is dependent on mitochondrial function
    • Higuchi M., Aggarwal B.B., and Yeh E.T. Activation of CPP32-like protease in tumor necrosis factor-induced apoptosis is dependent on mitochondrial function. J. Clin. Invest. 99 (1997) 1751-1758
    • (1997) J. Clin. Invest. , vol.99 , pp. 1751-1758
    • Higuchi, M.1    Aggarwal, B.B.2    Yeh, E.T.3
  • 28
    • 0025962976 scopus 로고
    • Use of cyanide and diethyldithiocarbamate in the assay of superoxide dismutases
    • Iqbal J., and Whitney P. Use of cyanide and diethyldithiocarbamate in the assay of superoxide dismutases. Free Radic. Biol. Med. 10 (1991) 69-77
    • (1991) Free Radic. Biol. Med. , vol.10 , pp. 69-77
    • Iqbal, J.1    Whitney, P.2
  • 29
    • 0031425652 scopus 로고    scopus 로고
    • Diethyl dithiocarbamate-induced decomposition of S-nitrosothiols
    • Arnelle D.R., Day B.J., and Stamler J.S. Diethyl dithiocarbamate-induced decomposition of S-nitrosothiols. Nitric Oxide 1 (1997) 56-64
    • (1997) Nitric Oxide , vol.1 , pp. 56-64
    • Arnelle, D.R.1    Day, B.J.2    Stamler, J.S.3
  • 30
    • 0033597951 scopus 로고    scopus 로고
    • Inhibition of copper-zinc superoxide dismutase induces cell growth, hypertrophic phenotype, and apoptosis in neonatal rat cardiac myocytes in vitro
    • Siwik D.A., Tzortzis J.D., Pimental D.R., Chang D.L., Pagano P.J., Singh K., Sawyer D.B., and Colucci W.S. Inhibition of copper-zinc superoxide dismutase induces cell growth, hypertrophic phenotype, and apoptosis in neonatal rat cardiac myocytes in vitro. Circ. Res. 85 (1999) 147-153
    • (1999) Circ. Res. , vol.85 , pp. 147-153
    • Siwik, D.A.1    Tzortzis, J.D.2    Pimental, D.R.3    Chang, D.L.4    Pagano, P.J.5    Singh, K.6    Sawyer, D.B.7    Colucci, W.S.8
  • 31
    • 0034791448 scopus 로고    scopus 로고
    • Superoxide levels and function of cerebral blood vessels after inhibition of CuZn-SOD
    • Didion S.P., Hathaway C.A., and Faraci F.M. Superoxide levels and function of cerebral blood vessels after inhibition of CuZn-SOD. Am. J. Physiol. Heart Circ. Physiol. 281 (2001) H1697-H1703
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.281
    • Didion, S.P.1    Hathaway, C.A.2    Faraci, F.M.3
  • 32
    • 0036888992 scopus 로고    scopus 로고
    • Intracellular superoxide induces apoptosis in VSMCs: role of mitochondrial membrane potential, cytochrome C and caspases
    • Li J., Li P.F., Dietz R., and von Harsdorf R. Intracellular superoxide induces apoptosis in VSMCs: role of mitochondrial membrane potential, cytochrome C and caspases. Apoptosis 7 (2002) 511-517
    • (2002) Apoptosis , vol.7 , pp. 511-517
    • Li, J.1    Li, P.F.2    Dietz, R.3    von Harsdorf, R.4
  • 33
    • 0037053298 scopus 로고    scopus 로고
    • The course of etoposide-induced apoptosis from damage to DNA and p53 activation to mitochondrial release of cytochrome c
    • Karpinich N.O., Tafani M., Rothman R.J., Russo M.A., and Farber J.L. The course of etoposide-induced apoptosis from damage to DNA and p53 activation to mitochondrial release of cytochrome c. J. Biol. Chem. 277 (2002) 16547-16552
    • (2002) J. Biol. Chem. , vol.277 , pp. 16547-16552
    • Karpinich, N.O.1    Tafani, M.2    Rothman, R.J.3    Russo, M.A.4    Farber, J.L.5
  • 34
    • 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. Mechanism of dithiocarbamate inhibition of apoptosis: thiol oxidation by dithiocarbamate disulfides directly inhibits processing of the caspase-3 proenzyme. Chem. Res. Toxicol. 10 (1997) 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
  • 36
    • 0025690822 scopus 로고
    • Analysis of the membrane potential of rat- and mouse-liver mitochondria by flow cytometry and possible applications
    • Petit P.X., O'Connor J.E., Grunwald D., and Brown S.C. Analysis of the membrane potential of rat- and mouse-liver mitochondria by flow cytometry and possible applications. Eur. J. Biochem. 194 (1990) 389-397
    • (1990) Eur. J. Biochem. , vol.194 , pp. 389-397
    • Petit, P.X.1    O'Connor, J.E.2    Grunwald, D.3    Brown, S.C.4
  • 37
    • 0028296066 scopus 로고
    • Flow cytometric detection of hydrogen peroxide production induced by doxorubicin in cancer cells
    • Ubezio P., and Civoli F. Flow cytometric detection of hydrogen peroxide production induced by doxorubicin in cancer cells. Free Radic. Biol. Med. 16 (1994) 509-516
    • (1994) Free Radic. Biol. Med. , vol.16 , pp. 509-516
    • Ubezio, P.1    Civoli, F.2
  • 38
    • 0345426305 scopus 로고    scopus 로고
    • Comparative analysis of apoptosis in HL60 detected by annexin-V and fluorescein-diacetate
    • Bartkowiak D., Hogner S., Baust H., Nothdurft W., and Rottinger E.M. Comparative analysis of apoptosis in HL60 detected by annexin-V and fluorescein-diacetate. Cytometry 37 (1999) 191-196
    • (1999) Cytometry , vol.37 , pp. 191-196
    • Bartkowiak, D.1    Hogner, S.2    Baust, H.3    Nothdurft, W.4    Rottinger, E.M.5
  • 39
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata S. Apoptosis by death factor. Cell 88 (1997) 355-365
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 43
    • 0024987513 scopus 로고
    • Effect of butylated hydroxyanisole on electron transport in rat liver mitochondria
    • Ferreira J. Effect of butylated hydroxyanisole on electron transport in rat liver mitochondria. Biochem. Pharmacol. 40 (1990) 677-684
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 677-684
    • Ferreira, J.1
  • 44
    • 0027729673 scopus 로고
    • Effects of inhibition of catalase and superoxide dismutase activity on antioxidant enzyme mRNA levels
    • Maitre B., Jornot L., and Junod A.F. Effects of inhibition of catalase and superoxide dismutase activity on antioxidant enzyme mRNA levels. Am. J. Physiol. 265 (1993) 636-643
    • (1993) Am. J. Physiol. , vol.265 , pp. 636-643
    • Maitre, B.1    Jornot, L.2    Junod, A.F.3
  • 45
    • 0030065418 scopus 로고    scopus 로고
    • Superoxide anion is a natural inhibitor of FAS-mediated cell death
    • Clement M.V., and Stamenkovic I. Superoxide anion is a natural inhibitor of FAS-mediated cell death. EMBO J. 15 (1996) 216-225
    • (1996) EMBO J. , vol.15 , pp. 216-225
    • Clement, M.V.1    Stamenkovic, I.2
  • 46
    • 0036296670 scopus 로고    scopus 로고
    • A permissive apoptotic environment: function of a decrease in intracellular superoxide anion and cytosolic acidification
    • Pervaiz S., and Clement M.V. A permissive apoptotic environment: function of a decrease in intracellular superoxide anion and cytosolic acidification. Biochem. Biophys. Res. Commun. 290 (2002) 1145-1150
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 1145-1150
    • Pervaiz, S.1    Clement, M.V.2
  • 47
    • 7444223594 scopus 로고    scopus 로고
    • Hydrogen peroxide-mediated cytosolic acidification is a signal for mitochondrial translocation of Bax during drug-induced apoptosis of tumor cells
    • Ahmad K.A., Iskandar K.B., Hirpara J.L., Clement M.V., and Pervaiz S. Hydrogen peroxide-mediated cytosolic acidification is a signal for mitochondrial translocation of Bax during drug-induced apoptosis of tumor cells. Cancer Res. 64 (2004) 7867-7878
    • (2004) Cancer Res. , vol.64 , pp. 7867-7878
    • Ahmad, K.A.1    Iskandar, K.B.2    Hirpara, J.L.3    Clement, M.V.4    Pervaiz, S.5
  • 49
    • 0032528118 scopus 로고    scopus 로고
    • Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis
    • Gross A., Jockel J., Wei M.C., and Korsmeyer S.J. Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis. EMBO J. 17 (1998) 3878-3885
    • (1998) EMBO J. , vol.17 , pp. 3878-3885
    • Gross, A.1    Jockel, J.2    Wei, M.C.3    Korsmeyer, S.J.4
  • 50
    • 0032571294 scopus 로고    scopus 로고
    • The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition
    • Pastorino J.G., Chen S.T., Tafani M., Snyder J.W., and Farber J.L. The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition. J. Biol. Chem. 273 (1998) 7770-7775
    • (1998) J. Biol. Chem. , vol.273 , pp. 7770-7775
    • Pastorino, J.G.1    Chen, S.T.2    Tafani, M.3    Snyder, J.W.4    Farber, J.L.5
  • 52
    • 0033498992 scopus 로고    scopus 로고
    • Antioxidants suitable for use with chemiluminescence to identify oxyradical species
    • Oosthuizen M.M., and Greyling D. Antioxidants suitable for use with chemiluminescence to identify oxyradical species. Redox. Rep. 4 (1999) 277-290
    • (1999) Redox. Rep. , vol.4 , pp. 277-290
    • Oosthuizen, M.M.1    Greyling, D.2
  • 53
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens J.F., Alexandre A., and Lehninger A.L. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch. Biochem. Biophys. 237 (1985) 408-414
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 54
    • 0023894234 scopus 로고
    • The effect of the NADPH oxidase inhibitor diphenyleneiodonium on aerobic and anaerobic microbicidal activities of human neutrophils
    • Ellis J.A., Mayer S.J., and Jones O.T. The effect of the NADPH oxidase inhibitor diphenyleneiodonium on aerobic and anaerobic microbicidal activities of human neutrophils. Biochem. J. 251 (1988) 887-891
    • (1988) Biochem. J. , vol.251 , pp. 887-891
    • Ellis, J.A.1    Mayer, S.J.2    Jones, O.T.3
  • 55
    • 10644285687 scopus 로고    scopus 로고
    • Molecular basis of the time-dependent inhibition of cyclooxygenases by indomethacin
    • Prusakiewicz J.J., Felts A.S., Mackenzie B.S., and Marnett L.J. Molecular basis of the time-dependent inhibition of cyclooxygenases by indomethacin. Biochemistry 43 (2004) 15439-15445
    • (2004) Biochemistry , vol.43 , pp. 15439-15445
    • Prusakiewicz, J.J.1    Felts, A.S.2    Mackenzie, B.S.3    Marnett, L.J.4
  • 56
    • 0030068484 scopus 로고    scopus 로고
    • A specific inhibitor of cytosolic phospholipase A2 activity, AACOCF3, inhibits glucose-induced insulin secretion from isolated rat islets
    • Loweth A.C., Scarpello J.H., and Morgan N.G. A specific inhibitor of cytosolic phospholipase A2 activity, AACOCF3, inhibits glucose-induced insulin secretion from isolated rat islets. Biochem. Biophys. Res. Commun. 218 (1996) 423-427
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 423-427
    • Loweth, A.C.1    Scarpello, J.H.2    Morgan, N.G.3
  • 58
    • 0028990125 scopus 로고
    • Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari M., Quan L.T., O'Rourke K., Desnoyers S., Zeng Z., Beidler D.R., Poirier G.G., Salvesen G.S., and Dixit V.M. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81 (1995) 801-809
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    O'Rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6    Poirier, G.G.7    Salvesen, G.S.8    Dixit, V.M.9
  • 64
    • 1542602477 scopus 로고    scopus 로고
    • Diethyldithiocarbamate-induced cytotoxicity and apoptosis in leukemia cell lines
    • Kanno S., Matsukawa E., Miura A., Shouji A., Asou K., and Ishikawa M. Diethyldithiocarbamate-induced cytotoxicity and apoptosis in leukemia cell lines. Biol. Pharm. Bull. 26 (2003) 964-968
    • (2003) Biol. Pharm. Bull. , vol.26 , pp. 964-968
    • Kanno, S.1    Matsukawa, E.2    Miura, A.3    Shouji, A.4    Asou, K.5    Ishikawa, M.6
  • 65
    • 0028815621 scopus 로고
    • Dithiocarbamates induce apoptosis in thymocytes by raising the intracellular level of redox-active copper
    • Nobel C.I., Kimland M., Lind B., Orrenius S., and Slater A.F. Dithiocarbamates induce apoptosis in thymocytes by raising the intracellular level of redox-active copper. J. Biol. Chem. 270 (1995) 26202-26208
    • (1995) J. Biol. Chem. , vol.270 , pp. 26202-26208
    • Nobel, C.I.1    Kimland, M.2    Lind, B.3    Orrenius, S.4    Slater, A.F.5
  • 66
    • 16644386249 scopus 로고    scopus 로고
    • Diethyldithiocarbamate can induce two different type of death: apoptosis and necrosis mediating the differential MAP kinase activation and redox regulation in HL60 cells
    • Kimoto-Kinoshita S., Nishida S., and Tomura T.T. Diethyldithiocarbamate can induce two different type of death: apoptosis and necrosis mediating the differential MAP kinase activation and redox regulation in HL60 cells. Mol. Cell. Biochem. 265 (2004) 123-132
    • (2004) Mol. Cell. Biochem. , vol.265 , pp. 123-132
    • Kimoto-Kinoshita, S.1    Nishida, S.2    Tomura, T.T.3
  • 67
    • 0343340396 scopus 로고    scopus 로고
    • Redox control of caspase-3 activity by thioredoxin and other reduced proteins
    • Baker A., Santos B.D., and Powis G. Redox control of caspase-3 activity by thioredoxin and other reduced proteins. Biochem. Biophys. Res. Commun. 268 (2000) 78-81
    • (2000) Biochem. Biophys. Res. Commun. , vol.268 , pp. 78-81
    • Baker, A.1    Santos, B.D.2    Powis, G.3
  • 68
    • 0034523818 scopus 로고    scopus 로고
    • Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c
    • Korsmeyer S.J., Wei M.C., Saito M., Weiler S., Oh K.J., and Schlesinger P.H. Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell Death Differ. 7 (2000) 1166-1173
    • (2000) Cell Death Differ. , vol.7 , pp. 1166-1173
    • Korsmeyer, S.J.1    Wei, M.C.2    Saito, M.3    Weiler, S.4    Oh, K.J.5    Schlesinger, P.H.6
  • 69
    • 0034697365 scopus 로고    scopus 로고
    • Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c
    • Shimizu S., Ide T., Yanagida T., and Tsujimoto Y. Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c. J. Biol. Chem. 275 (2000) 12321-12325
    • (2000) J. Biol. Chem. , vol.275 , pp. 12321-12325
    • Shimizu, S.1    Ide, T.2    Yanagida, T.3    Tsujimoto, Y.4
  • 71
    • 0345529917 scopus 로고    scopus 로고
    • Role of reactive oxygen species and cardiolipin in the release of cytochrome c from mitochondria
    • Petrosillo G., Ruggiero F.M., and Paradies G. Role of reactive oxygen species and cardiolipin in the release of cytochrome c from mitochondria. FASEB J. 17 (2003) 2202-2208
    • (2003) FASEB J. , vol.17 , pp. 2202-2208
    • Petrosillo, G.1    Ruggiero, F.M.2    Paradies, G.3
  • 72
    • 0142117313 scopus 로고    scopus 로고
    • The Bcl-2 family: roles in cell survival and oncogenesis
    • Cory S., Huang D.C., and Adams J.M. The Bcl-2 family: roles in cell survival and oncogenesis. Oncogene 22 (2003) 8590-8607
    • (2003) Oncogene , vol.22 , pp. 8590-8607
    • Cory, S.1    Huang, D.C.2    Adams, J.M.3
  • 73
    • 1442286330 scopus 로고    scopus 로고
    • The role of Bcl-2 family members in tumorigenesis
    • Kirkin V., Joos S., and Zornig M. The role of Bcl-2 family members in tumorigenesis. Biochim. Biophys. Acta 1644 (2004) 229-249
    • (2004) Biochim. Biophys. Acta , vol.1644 , pp. 229-249
    • Kirkin, V.1    Joos, S.2    Zornig, M.3
  • 75
    • 0142139353 scopus 로고    scopus 로고
    • Bax, reactive oxygen, and cytochrome c release in neuronal apoptosis
    • Kirkland R.A., and Franklin J.L. Bax, reactive oxygen, and cytochrome c release in neuronal apoptosis. Antioxid. Redox. Signal. 5 (2003) 589-596
    • (2003) Antioxid. Redox. Signal. , vol.5 , pp. 589-596
    • Kirkland, R.A.1    Franklin, J.L.2
  • 76
    • 1342325422 scopus 로고    scopus 로고
    • Reactive oxygen species are required for hyperoxia-induced Bax activation and cell death in alveolar epithelial cells
    • Buccellato L.J., Tso M., Akinci O.I., Chandel N.S., and Budinger G.R. Reactive oxygen species are required for hyperoxia-induced Bax activation and cell death in alveolar epithelial cells. J. Biol. Chem. 279 (2004) 6753-6760
    • (2004) J. Biol. Chem. , vol.279 , pp. 6753-6760
    • Buccellato, L.J.1    Tso, M.2    Akinci, O.I.3    Chandel, N.S.4    Budinger, G.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.