메뉴 건너뛰기




Volumn 76, Issue 9, 2008, Pages 1097-1109

The thioredoxin reductase inhibitor auranofin triggers apoptosis through a Bax/Bak-dependent process that involves peroxiredoxin 3 oxidation

Author keywords

Apoptosis; Mitochondria; Peroxiredoxin; Thiols; Thioredoxin reductase

Indexed keywords

ANTINEOPLASTIC AGENT; ANTIOXIDANT; AURANOFIN; CYTOCHROME C; PEROXIREDOXIN; PEROXIREDOXIN 3; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; SELENOPROTEIN; THIOREDOXIN REDUCTASE; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 53649092133     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2008.08.021     Document Type: Article
Times cited : (133)

References (81)
  • 1
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arnér E.S.J., and Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 267 (2000) 6102-6109
    • (2000) Eur J Biochem , vol.267 , pp. 6102-6109
    • Arnér, E.S.J.1    Holmgren, A.2
  • 2
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • Nordberg J., and Arner E.S.J. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 31 (2001) 1287-1312
    • (2001) Free Radic Biol Med , vol.31 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.J.2
  • 4
    • 33749993246 scopus 로고    scopus 로고
    • Disruption of mitochondrial redox circuitry in oxidative stress
    • Jones D.P. Disruption of mitochondrial redox circuitry in oxidative stress. Chem Biol Interact 163 (2006) 38-53
    • (2006) Chem Biol Interact , vol.163 , pp. 38-53
    • Jones, D.P.1
  • 5
    • 0037076433 scopus 로고    scopus 로고
    • The c-Myc target gene PRDX3 is required for mitochondrial homeostasis and neoplastic transformation
    • Wonsey D.R., Zeller K.I., and Dang C.V. The c-Myc target gene PRDX3 is required for mitochondrial homeostasis and neoplastic transformation. Proc Natl Acad Sci USA 99 (2002) 6649-6654
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6649-6654
    • Wonsey, D.R.1    Zeller, K.I.2    Dang, C.V.3
  • 6
    • 0042731713 scopus 로고    scopus 로고
    • Mitochondrial peroxiredoxin-3 protects hippocampal neurons from excitotoxic injury in vivo
    • Hattori F., Murayama N., Noshita T., and Oikawa S. Mitochondrial peroxiredoxin-3 protects hippocampal neurons from excitotoxic injury in vivo. J Neurochem 86 (2003) 860-868
    • (2003) J Neurochem , vol.86 , pp. 860-868
    • Hattori, F.1    Murayama, N.2    Noshita, T.3    Oikawa, S.4
  • 7
    • 0037827160 scopus 로고    scopus 로고
    • Increased expression-of mitochondrial peroxiredoxin-3 (thioredoxin peroxidase-2) protects cancer cells against hypoxia and drug-induced hydrogen peroxide-dependent apoptosis
    • Nonn L., Berggren M., and Powis G. Increased expression-of mitochondrial peroxiredoxin-3 (thioredoxin peroxidase-2) protects cancer cells against hypoxia and drug-induced hydrogen peroxide-dependent apoptosis. Mol Cancer Res 1 (2003) 682-689
    • (2003) Mol Cancer Res , vol.1 , pp. 682-689
    • Nonn, L.1    Berggren, M.2    Powis, G.3
  • 8
    • 4744373181 scopus 로고    scopus 로고
    • Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria
    • Chang T.S., Cho C.S., Park S., Yu S.Q., Kang S.W., and Rhee S.G. Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria. J Biol Chem 279 (2004) 41975-41984
    • (2004) J Biol Chem , vol.279 , pp. 41975-41984
    • Chang, T.S.1    Cho, C.S.2    Park, S.3    Yu, S.Q.4    Kang, S.W.5    Rhee, S.G.6
  • 9
    • 39949084758 scopus 로고    scopus 로고
    • Mitochondrial peroxiredoxin III protects pancreatic beta cells against apoptosis
    • Aumann N., Wolf G., and Walther R. Mitochondrial peroxiredoxin III protects pancreatic beta cells against apoptosis. Diabetologia 48 (2005) A186-A190
    • (2005) Diabetologia , vol.48
    • Aumann, N.1    Wolf, G.2    Walther, R.3
  • 10
    • 39949083765 scopus 로고    scopus 로고
    • Oxidation of mitochondrial peroxiredoxin 3 during the initiation of receptor-mediated apoptosis
    • Cox A.G., Pullar J.M., Hughes G., Ledgerwood E.C., and Hampton M.B. Oxidation of mitochondrial peroxiredoxin 3 during the initiation of receptor-mediated apoptosis. Free Radic Biol Med 44 (2008) 1001-1009
    • (2008) Free Radic Biol Med , vol.44 , pp. 1001-1009
    • Cox, A.G.1    Pullar, J.M.2    Hughes, G.3    Ledgerwood, E.C.4    Hampton, M.B.5
  • 11
    • 46649084593 scopus 로고    scopus 로고
    • Mitochondrial peroxiredoxin 3 is rapidly oxidised in cells treated with isothiocyanates
    • Brown K.K., Eriksson S.E., Arner E.S.J., and Hampton M.B. Mitochondrial peroxiredoxin 3 is rapidly oxidised in cells treated with isothiocyanates. Free Radic Biol Med 45 (2008) 494-502
    • (2008) Free Radic Biol Med , vol.45 , pp. 494-502
    • Brown, K.K.1    Eriksson, S.E.2    Arner, E.S.J.3    Hampton, M.B.4
  • 12
    • 18444365267 scopus 로고    scopus 로고
    • Thioredoxin-2 (TRX-2) is an essential gene regulating mitochondria-dependent apoptosis
    • Tanaka T., Hosoi F., Yamaguchi-Iwai Y., Nakamura H., Masutani H., Ueda S., et al. Thioredoxin-2 (TRX-2) is an essential gene regulating mitochondria-dependent apoptosis. EMBO J 21 (2002) 1695-1703
    • (2002) EMBO J , vol.21 , pp. 1695-1703
    • Tanaka, T.1    Hosoi, F.2    Yamaguchi-Iwai, Y.3    Nakamura, H.4    Masutani, H.5    Ueda, S.6
  • 13
    • 0037305881 scopus 로고    scopus 로고
    • The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice
    • Nonn L., Williams R.R., Erickson R.P., and Powis G. The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice. Mol Cell Biol 23 (2003) 916-922
    • (2003) Mol Cell Biol , vol.23 , pp. 916-922
    • Nonn, L.1    Williams, R.R.2    Erickson, R.P.3    Powis, G.4
  • 14
    • 6344277918 scopus 로고    scopus 로고
    • Essential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development, and heart function
    • Conrad M., Jakupoglu C., Moreno S.G., Lippl S., Banjac A., Schneider M., et al. Essential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development, and heart function. Mol Cell Biol 24 (2004) 9414-9423
    • (2004) Mol Cell Biol , vol.24 , pp. 9414-9423
    • Conrad, M.1    Jakupoglu, C.2    Moreno, S.G.3    Lippl, S.4    Banjac, A.5    Schneider, M.6
  • 15
    • 26244466587 scopus 로고    scopus 로고
    • Bcl-x(L)-mediated changes in metabolic pathways of breast cancer cells: from survival in the blood stream to organ-specific metastasis
    • España L., Martín B., Aragüés R., Chiva C., Oliva B., Andreu D., et al. Bcl-x(L)-mediated changes in metabolic pathways of breast cancer cells: from survival in the blood stream to organ-specific metastasis. Am J Pathol 167 (2005) 1125-1137
    • (2005) Am J Pathol , vol.167 , pp. 1125-1137
    • España, L.1    Martín, B.2    Aragüés, R.3    Chiva, C.4    Oliva, B.5    Andreu, D.6
  • 16
    • 33645982243 scopus 로고    scopus 로고
    • Expression of peroxiredoxin and thioredoxin in human lung cancer and paired normal lung
    • Park J.H., Kim Y.S., Lee H.L., Shim J.Y., Lee K.S., Oh Y.J., et al. Expression of peroxiredoxin and thioredoxin in human lung cancer and paired normal lung. Respirology 11 (2006) 269-275
    • (2006) Respirology , vol.11 , pp. 269-275
    • Park, J.H.1    Kim, Y.S.2    Lee, H.L.3    Shim, J.Y.4    Lee, K.S.5    Oh, Y.J.6
  • 18
    • 0036870093 scopus 로고    scopus 로고
    • Overexpression of mitochondrial thioredoxin reductase and peroxiredoxin III in hepatocellular carcinomas
    • Choi J.H., Kim T.N., Kim S.Y., Baek S.H., Kim J.H., Lee S.R., et al. Overexpression of mitochondrial thioredoxin reductase and peroxiredoxin III in hepatocellular carcinomas. Anticancer Res 22 (2002) 3331-3335
    • (2002) Anticancer Res , vol.22 , pp. 3331-3335
    • Choi, J.H.1    Kim, T.N.2    Kim, S.Y.3    Baek, S.H.4    Kim, J.H.5    Lee, S.R.6
  • 19
    • 33750378214 scopus 로고    scopus 로고
    • Defective mitochondrial peroxiredoxin-3 results in sensitivity to oxidative stress in Fanconi anemia
    • Mukhopadhyay S.S., Leung K.S., Hicks M.J., Hastings P.J., Youssoufian H., and Plon S.E. Defective mitochondrial peroxiredoxin-3 results in sensitivity to oxidative stress in Fanconi anemia. J Cell Biol 175 (2006) 225-235
    • (2006) J Cell Biol , vol.175 , pp. 225-235
    • Mukhopadhyay, S.S.1    Leung, K.S.2    Hicks, M.J.3    Hastings, P.J.4    Youssoufian, H.5    Plon, S.E.6
  • 20
    • 33751181030 scopus 로고    scopus 로고
    • On the potential of thioredoxin reductase inhibitors for cancer therapy
    • Urig S., and Becker K. On the potential of thioredoxin reductase inhibitors for cancer therapy. Semin Cancer Biol 16 (2006) 452-465
    • (2006) Semin Cancer Biol , vol.16 , pp. 452-465
    • Urig, S.1    Becker, K.2
  • 21
    • 0035890009 scopus 로고    scopus 로고
    • Analysis of the inhibition of mammalian thioredoxin, thioredoxin reductase, and glutaredoxin by cis-diamminedichloroplatinum (II) and its major metabolite, the glutathione-platinum complex
    • Arnér E.S.J., Nakamura H., Sasada T., Yodoi J., Holmgren A., and Spyrou G. Analysis of the inhibition of mammalian thioredoxin, thioredoxin reductase, and glutaredoxin by cis-diamminedichloroplatinum (II) and its major metabolite, the glutathione-platinum complex. Free Radic Biol Med 31 (2001) 1170-1178
    • (2001) Free Radic Biol Med , vol.31 , pp. 1170-1178
    • Arnér, E.S.J.1    Nakamura, H.2    Sasada, T.3    Yodoi, J.4    Holmgren, A.5    Spyrou, G.6
  • 22
    • 33744956073 scopus 로고    scopus 로고
    • Motexafin gadolinium, a tumor-selective drug targeting thioredoxin reductase and ribonucleotide reductase
    • Hashemy S.I., Ungerstedt J.S., Avval F.Z., and Holmgren A. Motexafin gadolinium, a tumor-selective drug targeting thioredoxin reductase and ribonucleotide reductase. J Biol Chem 281 (2006) 10691-10697
    • (2006) J Biol Chem , vol.281 , pp. 10691-10697
    • Hashemy, S.I.1    Ungerstedt, J.S.2    Avval, F.Z.3    Holmgren, A.4
  • 23
    • 34547644483 scopus 로고    scopus 로고
    • Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide
    • Lu J., Chew E.H., and Holmgren A. Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide. Proc Natl Acad Sci USA 104 (2007) 12288-12293
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 12288-12293
    • Lu, J.1    Chew, E.H.2    Holmgren, A.3
  • 24
    • 33845914554 scopus 로고    scopus 로고
    • Cyclophosphamide as a potent inhibitor of tumor thioredoxin reductase in vivo
    • Wang X.F., Zhang J.S., and Xu T.W. Cyclophosphamide as a potent inhibitor of tumor thioredoxin reductase in vivo. Toxicol Appl Pharmacol 218 (2007) 88-95
    • (2007) Toxicol Appl Pharmacol , vol.218 , pp. 88-95
    • Wang, X.F.1    Zhang, J.S.2    Xu, T.W.3
  • 25
    • 23444435104 scopus 로고    scopus 로고
    • Inhibition of thioredoxin reductase but not of glutathione reductase by the major classes of alkylating and platinum-containing anticancer compounds
    • Witte A.B., Anestal K., Jerremalm E., Ehrsson H., and Arner E.S.J. Inhibition of thioredoxin reductase but not of glutathione reductase by the major classes of alkylating and platinum-containing anticancer compounds. Free Radic Biol Med 39 (2005) 696-703
    • (2005) Free Radic Biol Med , vol.39 , pp. 696-703
    • Witte, A.B.1    Anestal, K.2    Jerremalm, E.3    Ehrsson, H.4    Arner, E.S.J.5
  • 27
    • 0021970996 scopus 로고
    • Evaluation of the in vivo antitumor-activity and in vitro cyto-toxic properties of auranofin, a coordinated gold compound, in murine tumor-models
    • Mirabelli C.K., Johnson R.K., Sung C.M., Faucette L., Muirhead K., and Crooke S.T. Evaluation of the in vivo antitumor-activity and in vitro cyto-toxic properties of auranofin, a coordinated gold compound, in murine tumor-models. Cancer Res 45 (1985) 32-39
    • (1985) Cancer Res , vol.45 , pp. 32-39
    • Mirabelli, C.K.1    Johnson, R.K.2    Sung, C.M.3    Faucette, L.4    Muirhead, K.5    Crooke, S.T.6
  • 28
    • 34250652117 scopus 로고    scopus 로고
    • Targeting the mitochondrial cell death pathway with gold compounds
    • Barnard P.J., and Berners-Price S.J. Targeting the mitochondrial cell death pathway with gold compounds. Coordin Chem Rev 251 (2007) 1889-1902
    • (2007) Coordin Chem Rev , vol.251 , pp. 1889-1902
    • Barnard, P.J.1    Berners-Price, S.J.2
  • 29
    • 0036268977 scopus 로고    scopus 로고
    • Gold derivatives for the treatment of cancer
    • Tiekink E.R.T. Gold derivatives for the treatment of cancer. Crit Rev Oncol Hemat 42 (2002) 225-248
    • (2002) Crit Rev Oncol Hemat , vol.42 , pp. 225-248
    • Tiekink, E.R.T.1
  • 30
    • 0036687855 scopus 로고    scopus 로고
    • Gold opens mitochondrial pathways to apoptosis
    • McKeage M.J. Gold opens mitochondrial pathways to apoptosis. Br J Pharm 136 (2002) 1081-1082
    • (2002) Br J Pharm , vol.136 , pp. 1081-1082
    • McKeage, M.J.1
  • 31
    • 0032493647 scopus 로고    scopus 로고
    • Human placenta thioredoxin reductase-isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds
    • Gromer S., Arscott L.D., Williams C.H., Schirmer R.H., and Becker K. Human placenta thioredoxin reductase-isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds. J Biol Chem 273 (1998) 20096-20101
    • (1998) J Biol Chem , vol.273 , pp. 20096-20101
    • Gromer, S.1    Arscott, L.D.2    Williams, C.H.3    Schirmer, R.H.4    Becker, K.5
  • 32
    • 5344266051 scopus 로고    scopus 로고
    • Gold complexes inhibit mitochondrial thioredoxin reductase: consequences on mitochondrial functions
    • Rigobello M.P., Messori L., Marcon G., Cinellu M.A., Bragadin M., Folda A., et al. Gold complexes inhibit mitochondrial thioredoxin reductase: consequences on mitochondrial functions. J Inorg Biochem 98 (2004) 1634-1641
    • (2004) J Inorg Biochem , vol.98 , pp. 1634-1641
    • Rigobello, M.P.1    Messori, L.2    Marcon, G.3    Cinellu, M.A.4    Bragadin, M.5    Folda, A.6
  • 33
    • 34347213728 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain and thioredoxin reductase regulate intermembrane Cu,Zn-superoxide dismutase activity: implications for mitochondrial energy metabolism and apoptosis
    • Iñarrea P., Moini H., Han D., Rettori D., Aguiló I., Alava M.A., et al. Mitochondrial respiratory chain and thioredoxin reductase regulate intermembrane Cu,Zn-superoxide dismutase activity: implications for mitochondrial energy metabolism and apoptosis. Biochem J 405 (2007) 173-179
    • (2007) Biochem J , vol.405 , pp. 173-179
    • Iñarrea, P.1    Moini, H.2    Han, D.3    Rettori, D.4    Aguiló, I.5    Alava, M.A.6
  • 34
    • 22044444840 scopus 로고    scopus 로고
    • Effect of Auranofin on the mitochondrial generation of hydrogen peroxide. Role of thioredoxin reductase
    • Rigobello M.P., Folda A., Baldoin M.C., Scutari G., and Bindoli A. Effect of Auranofin on the mitochondrial generation of hydrogen peroxide. Role of thioredoxin reductase. Free Radic Res 39 (2005) 687-695
    • (2005) Free Radic Res , vol.39 , pp. 687-695
    • Rigobello, M.P.1    Folda, A.2    Baldoin, M.C.3    Scutari, G.4    Bindoli, A.5
  • 35
    • 39149124133 scopus 로고    scopus 로고
    • Gold(I) complexes determine apoptosis with limited oxidative stress in Jurkat T cells
    • Rigobello M.P., Folda A., Dani B., Menabò R., Scutari G., and Bindoli A. Gold(I) complexes determine apoptosis with limited oxidative stress in Jurkat T cells. Eur J Pharmacol 582 (2008) 26-34
    • (2008) Eur J Pharmacol , vol.582 , pp. 26-34
    • Rigobello, M.P.1    Folda, A.2    Dani, B.3    Menabò, R.4    Scutari, G.5    Bindoli, A.6
  • 36
    • 0036688034 scopus 로고    scopus 로고
    • Induction of mitochondrial permeability transition by auranofin, a gold(I)-phosphine derivative
    • Rigobello M.P., Scutari G., Boscolo R., and Bindoli A. Induction of mitochondrial permeability transition by auranofin, a gold(I)-phosphine derivative. Br J Pharm 136 (2002) 1162-1168
    • (2002) Br J Pharm , vol.136 , pp. 1162-1168
    • Rigobello, M.P.1    Scutari, G.2    Boscolo, R.3    Bindoli, A.4
  • 37
    • 1642452655 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin reductase inhibition by gold(I) compounds and concurrent stimulation of permeability transition and release of cytochrome c
    • Rigobello M.P., Scutari G., Folda A., and Bindoli A. Mitochondrial thioredoxin reductase inhibition by gold(I) compounds and concurrent stimulation of permeability transition and release of cytochrome c. Biochem Pharm 67 (2004) 689-696
    • (2004) Biochem Pharm , vol.67 , pp. 689-696
    • Rigobello, M.P.1    Scutari, G.2    Folda, A.3    Bindoli, A.4
  • 38
    • 50949084067 scopus 로고    scopus 로고
    • Inhibition of receptor-mediated apoptosis upon Bcl-2 overexpression is not associated with increased antioxidant status
    • Thomson S.J., Cox A.G., Cuddihy S.L., Pullar J.M., and Hampton M.B. Inhibition of receptor-mediated apoptosis upon Bcl-2 overexpression is not associated with increased antioxidant status. Biochem Biophys Res Commun 375 (2008) 145-150
    • (2008) Biochem Biophys Res Commun , vol.375 , pp. 145-150
    • Thomson, S.J.1    Cox, A.G.2    Cuddihy, S.L.3    Pullar, J.M.4    Hampton, M.B.5
  • 39
    • 0031773474 scopus 로고    scopus 로고
    • Preparation and assay of mammalian thioredoxin and thioredoxin reductase
    • Arnér E.S.J., Zhong L.W., and Holmgren A. Preparation and assay of mammalian thioredoxin and thioredoxin reductase. Methods Enzymol 300 (1999) 226-239
    • (1999) Methods Enzymol , vol.300 , pp. 226-239
    • Arnér, E.S.J.1    Zhong, L.W.2    Holmgren, A.3
  • 41
    • 28544437074 scopus 로고    scopus 로고
    • Flow cytometric determination of mitochondrial membrane potential changes during apoptosis of T lymphocytic and pancreatic beta cell lines: comparison of tetramethylrhodamineethylester (TMRE), chloromethyl-X-rosamine (H2-CMX-Ros) and MitoTracker Red 580 (MTR580)
    • Jayaraman S. Flow cytometric determination of mitochondrial membrane potential changes during apoptosis of T lymphocytic and pancreatic beta cell lines: comparison of tetramethylrhodamineethylester (TMRE), chloromethyl-X-rosamine (H2-CMX-Ros) and MitoTracker Red 580 (MTR580). J Immunol Methods 306 (2005) 68-79
    • (2005) J Immunol Methods , vol.306 , pp. 68-79
    • Jayaraman, S.1
  • 42
    • 34347215518 scopus 로고    scopus 로고
    • Analysis of apoptosis by propidium iodide staining and flow cytometry
    • Riccardi C., and Nicoletti I. Analysis of apoptosis by propidium iodide staining and flow cytometry. Nat Protocols 1 (2006) 1458-1461
    • (2006) Nat Protocols , vol.1 , pp. 1458-1461
    • Riccardi, C.1    Nicoletti, I.2
  • 43
    • 0032080238 scopus 로고    scopus 로고
    • Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalobenzenes by alkylation of both the redox active selenocysteine and its neighboring cysteine residue
    • Nordberg J., Zhong L., Holmgren A., and Arnér E.S.J. Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalobenzenes by alkylation of both the redox active selenocysteine and its neighboring cysteine residue. J Biol Chem 273 (1998) 10835-10842
    • (1998) J Biol Chem , vol.273 , pp. 10835-10842
    • Nordberg, J.1    Zhong, L.2    Holmgren, A.3    Arnér, E.S.J.4
  • 44
    • 0000466588 scopus 로고
    • Respiratory chain linked H(2)O(2) production in pigeon heart mitochondria
    • Loschen G., Flohé L., and Chance B. Respiratory chain linked H(2)O(2) production in pigeon heart mitochondria. FEBS Lett 18 (1971) 261-264
    • (1971) FEBS Lett , vol.18 , pp. 261-264
    • Loschen, G.1    Flohé, L.2    Chance, B.3
  • 45
    • 33744958179 scopus 로고    scopus 로고
    • Thioredoxin reductase 1 deficiency reverses tumor phenotype and tumorigenicity of lung carcinoma cells
    • Yoo M.H., Xu X.M., Carlson B.A., Gladyshev V.N., and Hatfield D.L. Thioredoxin reductase 1 deficiency reverses tumor phenotype and tumorigenicity of lung carcinoma cells. J Biol Chem 281 (2006) 13005-13008
    • (2006) J Biol Chem , vol.281 , pp. 13005-13008
    • Yoo, M.H.1    Xu, X.M.2    Carlson, B.A.3    Gladyshev, V.N.4    Hatfield, D.L.5
  • 46
    • 39749177838 scopus 로고    scopus 로고
    • Targeting thioredoxin reductase 1 reduction in cancer cells inhibits self-sufficient growth and DNA replication
    • Yoo M.H., Xu X.M., Carlson B.A., Patterson A.D., Gladyshev V.N., and Hatfield D.L. Targeting thioredoxin reductase 1 reduction in cancer cells inhibits self-sufficient growth and DNA replication. PLOS One 2 (2007) e1112
    • (2007) PLOS One , vol.2
    • Yoo, M.H.1    Xu, X.M.2    Carlson, B.A.3    Patterson, A.D.4    Gladyshev, V.N.5    Hatfield, D.L.6
  • 47
    • 44949114211 scopus 로고    scopus 로고
    • Thioredoxin reductase inhibition by antitumor quinols: a quinol pharmacophore effect correlating to antiproliferative activity
    • Chew E.H., Lu J., Bradshaw T.D., and Holmgren A. Thioredoxin reductase inhibition by antitumor quinols: a quinol pharmacophore effect correlating to antiproliferative activity. FASEB J 22 (2008) 2072-2083
    • (2008) FASEB J , vol.22 , pp. 2072-2083
    • Chew, E.H.1    Lu, J.2    Bradshaw, T.D.3    Holmgren, A.4
  • 48
    • 0037031939 scopus 로고    scopus 로고
    • Overexpressed human mitochondrial thioredoxin confers resistance to oxidant-induced apoptosis in human osteosarcoma cells
    • Chen Y., Cai J., Murphy T.J., and Jones D.P. Overexpressed human mitochondrial thioredoxin confers resistance to oxidant-induced apoptosis in human osteosarcoma cells. J Biol Chem 277 (2002) 33242-33248
    • (2002) J Biol Chem , vol.277 , pp. 33242-33248
    • Chen, Y.1    Cai, J.2    Murphy, T.J.3    Jones, D.P.4
  • 49
    • 33751509841 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin in regulation of oxidant-induced cell death
    • Chen Y., Cai J., and Jones D.P. Mitochondrial thioredoxin in regulation of oxidant-induced cell death. FEBS Lett 580 (2006) 6596-6602
    • (2006) FEBS Lett , vol.580 , pp. 6596-6602
    • Chen, Y.1    Cai, J.2    Jones, D.P.3
  • 50
    • 34548048824 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin-2/peroxiredoxin-3 system functions in parallel with mitochondrial GSH system in protection against oxidative stress
    • Zhang H., Go Y.M., and Jones D.P. Mitochondrial thioredoxin-2/peroxiredoxin-3 system functions in parallel with mitochondrial GSH system in protection against oxidative stress. Arch Biochem Biophys 465 (2007) 119-126
    • (2007) Arch Biochem Biophys , vol.465 , pp. 119-126
    • Zhang, H.1    Go, Y.M.2    Jones, D.P.3
  • 52
    • 45549099735 scopus 로고    scopus 로고
    • Inhibition of human thioredoxin system: a molecular mechanism of mercury toxicity
    • Carvalho C.M., Chew E.H., Hashemy S.I., Lu J., and Holmgren A. Inhibition of human thioredoxin system: a molecular mechanism of mercury toxicity. J Biol Chem 283 (2008) 11713-11723
    • (2008) J Biol Chem , vol.283 , pp. 11713-11723
    • Carvalho, C.M.1    Chew, E.H.2    Hashemy, S.I.3    Lu, J.4    Holmgren, A.5
  • 53
    • 15044349930 scopus 로고    scopus 로고
    • Effect of metal complexes on thioredoxin reductase and the regulation of mitochondrial permeability conditions
    • Bragadin M., Scutari G., Folda A., Bindoli A., and Rigobello M.P. Effect of metal complexes on thioredoxin reductase and the regulation of mitochondrial permeability conditions. Ann N Y Acad Sci 1030 (2004) 348-354
    • (2004) Ann N Y Acad Sci , vol.1030 , pp. 348-354
    • Bragadin, M.1    Scutari, G.2    Folda, A.3    Bindoli, A.4    Rigobello, M.P.5
  • 54
    • 28744434298 scopus 로고    scopus 로고
    • Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions
    • Hansen J.M., Zhang H., and Jones D.P. Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions. Free Radic Biol Med 40 (2006) 138-145
    • (2006) Free Radic Biol Med , vol.40 , pp. 138-145
    • Hansen, J.M.1    Zhang, H.2    Jones, D.P.3
  • 56
    • 34548451974 scopus 로고    scopus 로고
    • Reactive oxygen species in mitochondria-mediated cell death
    • Orrenius S. Reactive oxygen species in mitochondria-mediated cell death. Drug Metab Rev 39 (2007) 443-455
    • (2007) Drug Metab Rev , vol.39 , pp. 443-455
    • Orrenius, S.1
  • 57
    • 2942696470 scopus 로고    scopus 로고
    • Thioredoxin-2 inhibits mitochondria-located ASK1-mediated apoptosis in a JNK-independent manner
    • Zhang R., Al-Lamki R., Bai L., Streb J.W., Miano J.M., Bradley J., et al. Thioredoxin-2 inhibits mitochondria-located ASK1-mediated apoptosis in a JNK-independent manner. Circ Res 94 (2004) 1483-1491
    • (2004) Circ Res , vol.94 , pp. 1483-1491
    • Zhang, R.1    Al-Lamki, R.2    Bai, L.3    Streb, J.W.4    Miano, J.M.5    Bradley, J.6
  • 58
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • Saitoh M., Nishitoh H., Fujii M., Takeda K., Tobiume K., Sawada Y., et al. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J 17 (1998) 2596-2606
    • (1998) EMBO J , vol.17 , pp. 2596-2606
    • Saitoh, M.1    Nishitoh, H.2    Fujii, M.3    Takeda, K.4    Tobiume, K.5    Sawada, Y.6
  • 59
  • 60
    • 33744809562 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin-2 has a key role in determining tumor necrosis factor-alpha-induced reactive oxygen species generation, NF-kappa B activation, and apoptosis
    • Hansen J.M., Zhang H., and Jones D.P. Mitochondrial thioredoxin-2 has a key role in determining tumor necrosis factor-alpha-induced reactive oxygen species generation, NF-kappa B activation, and apoptosis. Toxicol Sci 91 (2006) 643-650
    • (2006) Toxicol Sci , vol.91 , pp. 643-650
    • Hansen, J.M.1    Zhang, H.2    Jones, D.P.3
  • 61
    • 35548998655 scopus 로고    scopus 로고
    • Arsenic trioxide sensitizes promonocytic leukemia cells to TNFalpha-induced apoptosis via p38-MAPK-regulated activation of both receptor-mediated and mitochondrial pathways
    • Amrán D., Sánchez Y., Fernández C., Ramos A.M., de Blas E., Bréard J., et al. Arsenic trioxide sensitizes promonocytic leukemia cells to TNFalpha-induced apoptosis via p38-MAPK-regulated activation of both receptor-mediated and mitochondrial pathways. Biochim Biophys Acta 1773 (2007) 1653-1663
    • (2007) Biochim Biophys Acta , vol.1773 , pp. 1653-1663
    • Amrán, D.1    Sánchez, Y.2    Fernández, C.3    Ramos, A.M.4    de Blas, E.5    Bréard, J.6
  • 62
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • Nakagawa T., Shimizu S., Watanabe T., Yamaguchi O., Otsu K., Yamagata H., et al. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 434 (2005) 652-658
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3    Yamaguchi, O.4    Otsu, K.5    Yamagata, H.6
  • 63
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines C.P., Kaiser R.A., Purcell N.H., Blair N.S., Osinska H., Hambleton M.A., et al. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 434 (2005) 658-662
    • (2005) Nature , vol.434 , pp. 658-662
    • Baines, C.P.1    Kaiser, R.A.2    Purcell, N.H.3    Blair, N.S.4    Osinska, H.5    Hambleton, M.A.6
  • 64
    • 34247485841 scopus 로고    scopus 로고
    • Role of the mitochondrial membrane permeability transition in cell death
    • Tsujimoto Y., and Shimizu S. Role of the mitochondrial membrane permeability transition in cell death. Apoptosis 12 (2007) 835-840
    • (2007) Apoptosis , vol.12 , pp. 835-840
    • Tsujimoto, Y.1    Shimizu, S.2
  • 65
    • 0037507286 scopus 로고    scopus 로고
    • Rapid induction of cell death by selenium-compromised thioredoxin reductase 1 but not by the fully active enzyme containing selenocysteine
    • Anestål K., and Arner E. Rapid induction of cell death by selenium-compromised thioredoxin reductase 1 but not by the fully active enzyme containing selenocysteine. J Biol Chem 278 (2003) 15966-15972
    • (2003) J Biol Chem , vol.278 , pp. 15966-15972
    • Anestål, K.1    Arner, E.2
  • 66
    • 44849125526 scopus 로고    scopus 로고
    • Cell death by SecTRAPs: thioredoxin reductase as a prooxidant killer of cells
    • Anestål K., Prast-Nielsen S., Cenas N., and Arnér E.S. Cell death by SecTRAPs: thioredoxin reductase as a prooxidant killer of cells. PLOS One 3 (2008) 1846
    • (2008) PLOS One , vol.3 , pp. 1846
    • Anestål, K.1    Prast-Nielsen, S.2    Cenas, N.3    Arnér, E.S.4
  • 67
    • 33845357331 scopus 로고    scopus 로고
    • Thioredoxin reductase is required for the inactivation of tumor suppressor p53 and for apoptosis induced by endogenous electrophiles
    • Cassidy P.B., Edes K., Nelson C.C., Parsawar K., Fitzpatrick F.A., and Moos P.J. Thioredoxin reductase is required for the inactivation of tumor suppressor p53 and for apoptosis induced by endogenous electrophiles. Carcinogenesis 27 (2006) 2538-2549
    • (2006) Carcinogenesis , vol.27 , pp. 2538-2549
    • Cassidy, P.B.1    Edes, K.2    Nelson, C.C.3    Parsawar, K.4    Fitzpatrick, F.A.5    Moos, P.J.6
  • 70
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • Benhar M., Forrester M.T., Hess D.T., and Stamler J.S. Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 320 (2008) 1050-1054
    • (2008) Science , vol.320 , pp. 1050-1054
    • Benhar, M.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 71
    • 46949089099 scopus 로고    scopus 로고
    • Bioenergetic differences selectively sensitize tumorigenic liver progenitor cells to a new gold(I) compound
    • Jellicoe M.M., Nichols S.J., Callus B.A., Baker M.V., Barnard P.J., Berners-Price S.J., et al. Bioenergetic differences selectively sensitize tumorigenic liver progenitor cells to a new gold(I) compound. Carcinogenesis 29 (2008) 1124-1133
    • (2008) Carcinogenesis , vol.29 , pp. 1124-1133
    • Jellicoe, M.M.1    Nichols, S.J.2    Callus, B.A.3    Baker, M.V.4    Barnard, P.J.5    Berners-Price, S.J.6
  • 73
    • 34548050479 scopus 로고    scopus 로고
    • A gold(I) phosphine complex selectively induces apoptosis in breast cancer cells: Implications for anticancer therapeutics targeted to mitochondria
    • Rackham O., Nichols S.J., Leedman P.J., Berners-Price S.J., and Filipovska A. A gold(I) phosphine complex selectively induces apoptosis in breast cancer cells: Implications for anticancer therapeutics targeted to mitochondria. Biochem Pharmacol 74 (2007) 992-1002
    • (2007) Biochem Pharmacol , vol.74 , pp. 992-1002
    • Rackham, O.1    Nichols, S.J.2    Leedman, P.J.3    Berners-Price, S.J.4    Filipovska, A.5
  • 74
    • 33846856009 scopus 로고    scopus 로고
    • Mitochondria are primary targets in apoptosis induced by the mixed phosphine gold species chlorotriphenylphosphine-1,3-bis(diphenylphosphino)propanegold(I) in melanoma cell lines
    • Caruso F., Villa R., Rossi M., Pettinari C., Paduano F., Pennati M., et al. Mitochondria are primary targets in apoptosis induced by the mixed phosphine gold species chlorotriphenylphosphine-1,3-bis(diphenylphosphino)propanegold(I) in melanoma cell lines. Biochem Pharm 73 (2007) 773-781
    • (2007) Biochem Pharm , vol.73 , pp. 773-781
    • Caruso, F.1    Villa, R.2    Rossi, M.3    Pettinari, C.4    Paduano, F.5    Pennati, M.6
  • 75
    • 29244451873 scopus 로고    scopus 로고
    • GoldIII porphyrin 1a induced apoptosis by mitochondrial death pathways related to reactive oxygen species
    • Wang Y., He Q.Y., Sun R.W., Che C.M., and Chiu J.F. GoldIII porphyrin 1a induced apoptosis by mitochondrial death pathways related to reactive oxygen species. Cancer Res 65 (2005) 11553-11564
    • (2005) Cancer Res , vol.65 , pp. 11553-11564
    • Wang, Y.1    He, Q.Y.2    Sun, R.W.3    Che, C.M.4    Chiu, J.F.5
  • 76
    • 33847014053 scopus 로고    scopus 로고
    • Inhibition of thioredoxin reductase by auranofin induces apoptosis in cisplatin-resistant human ovarian cancer cells
    • Marzano C., Gandin V., Folda A., Scutari G., Bindoli A., and Rigobello M.P. Inhibition of thioredoxin reductase by auranofin induces apoptosis in cisplatin-resistant human ovarian cancer cells. Free Radic Biol Med 42 (2007) 872-881
    • (2007) Free Radic Biol Med , vol.42 , pp. 872-881
    • Marzano, C.1    Gandin, V.2    Folda, A.3    Scutari, G.4    Bindoli, A.5    Rigobello, M.P.6
  • 77
    • 0033796101 scopus 로고    scopus 로고
    • The role of the redox protein thioredoxin in cell growth and cancer
    • Powis G., Mustacich D., and Coon A. The role of the redox protein thioredoxin in cell growth and cancer. Free Radic Biol Med 29 (2000) 312-322
    • (2000) Free Radic Biol Med , vol.29 , pp. 312-322
    • Powis, G.1    Mustacich, D.2    Coon, A.3
  • 78
    • 33751178410 scopus 로고    scopus 로고
    • The thioredoxin system in cancer
    • Arnér E.S.J., and Holmgren A. The thioredoxin system in cancer. Semin Cancer Biol 16 (2006) 420-426
    • (2006) Semin Cancer Biol , vol.16 , pp. 420-426
    • Arnér, E.S.J.1    Holmgren, A.2
  • 79
    • 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
  • 81
    • 46449096246 scopus 로고    scopus 로고
    • Clinical pharmacology of gold
    • Kean W.F., and Kean I.R. Clinical pharmacology of gold. Inflammopharmacology 16 (2008) 112-125
    • (2008) Inflammopharmacology , vol.16 , pp. 112-125
    • Kean, W.F.1    Kean, I.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.