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Volumn 22, Issue 4, 1998, Pages 235-246

Induction of apoptosis by thiuramdisulfides, the reactive metabolites of dithiocarbamates, through coordinative modulation of NFκB, c-fos/c-jun, and p53 proteins

Author keywords

AP 1; Apoptosis; Dithiocarbamate; G1 arrest; NF B; P53; Thiuramdisulfide

Indexed keywords

DIETHYLDITHIOCARBAMIC ACID; DISULFIDE; DISULFIRAM;

EID: 0031855760     PISSN: 08991987     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1098-2744(199808)22:4<235::AID-MC5>3.0.CO;2-I     Document Type: Article
Times cited : (53)

References (53)
  • 1
    • 0017339888 scopus 로고
    • Inhibition of dimethylnitrosamine-induced strand breaks in liver DNA and liver cell necrosis by diethyldithiocarbamate
    • Abanobi SE, Popp JA, Chang SK, et al. Inhibition of dimethylnitrosamine-induced strand breaks in liver DNA and liver cell necrosis by diethyldithiocarbamate. J Natl Cancer Inst 58:263-271, 1977.
    • (1977) J Natl Cancer Inst , vol.58 , pp. 263-271
    • Abanobi, S.E.1    Popp, J.A.2    Chang, S.K.3
  • 2
    • 0021733954 scopus 로고
    • Effects of disulfiram on metabolism of nitrosodiethylamine during liver carcinogenesis
    • Hadjiolov D, Frank N, Mundt D, et al. Effects of disulfiram on metabolism of nitrosodiethylamine during liver carcinogenesis. J Cancer Res Clin Oncol 108:281-285, 1984.
    • (1984) J Cancer Res Clin Oncol , vol.108 , pp. 281-285
    • Hadjiolov, D.1    Frank, N.2    Mundt, D.3
  • 3
    • 0023810808 scopus 로고
    • Diethyldithiocarbamate inhibition of murine bone marrow toxicity caused by cisdiammine-dichloroplatinum (II) or diammine (1, 1-cyclobutanedicarboxylato) platinum (II)
    • Gringeri A, Keng PC, Borch RF. Diethyldithiocarbamate inhibition of murine bone marrow toxicity caused by cisdiammine-dichloroplatinum (II) or diammine (1, 1-cyclobutanedicarboxylato) platinum (II). Cancer Res 48:5708-5712, 1988.
    • (1988) Cancer Res , vol.48 , pp. 5708-5712
    • Gringeri, A.1    Keng, P.C.2    Borch, R.F.3
  • 4
    • 0024598937 scopus 로고
    • Effect of diethyl-dithiocarbamate on toxicity of doxorubicin, cyclophosphamide and cisdiamminedichloroplatinum (II) on mice haemopoietic progenitor cells
    • Pannacciulli IM, Lerza RA, Bogliolo GV, et al. Effect of diethyl-dithiocarbamate on toxicity of doxorubicin, cyclophosphamide and cisdiamminedichloroplatinum (II) on mice haemopoietic progenitor cells. Br J Cancer 59:371-374, 1989.
    • (1989) Br J Cancer , vol.59 , pp. 371-374
    • Pannacciulli, I.M.1    Lerza, R.A.2    Bogliolo, G.V.3
  • 5
    • 0021742344 scopus 로고
    • Influence of disulfiram on the metabolism of N-nitrosodiethylamine
    • Frank N, Wiessler M, Hadjiolov D. Influence of disulfiram on the metabolism of N-nitrosodiethylamine. IARC Sci Publ 57:519-523, 1984.
    • (1984) IARC Sci Publ , vol.57 , pp. 519-523
    • Frank, N.1    Wiessler, M.2    Hadjiolov, D.3
  • 6
    • 0019848509 scopus 로고
    • Wirkung von Disulfiram auf die Toxizität und Carcinogenitet von N-Methyl-N-nitrosobenzylamin bei Ratten
    • Schweinsberg F, Bu̇rkle V. Wirkung von Disulfiram auf die Toxizität und Carcinogenitet von N-Methyl-N-nitrosobenzylamin bei Ratten. J Cancer Res Clin Oncol 102:43-47, 1981.
    • (1981) J Cancer Res Clin Oncol , vol.102 , pp. 43-47
    • Schweinsberg, F.1    Burkle, V.2
  • 7
    • 0022451460 scopus 로고
    • Modifying effects of disulfiram on DNA adduct formation and persistence of benzaldehyde in N-nitroso-N-methylbenzylamine-induced carcinogenesis in rats
    • Schweinsberg F, Danecki S, Grotzke J, et al. Modifying effects of disulfiram on DNA adduct formation and persistence of benzaldehyde in N-nitroso-N-methylbenzylamine-induced carcinogenesis in rats. J Cancer Res Clin Oncol 112:75-80, 1986.
    • (1986) J Cancer Res Clin Oncol , vol.112 , pp. 75-80
    • Schweinsberg, F.1    Danecki, S.2    Grotzke, J.3
  • 8
    • 0018849528 scopus 로고
    • Tumor induced in Fischer F344 rats by the feeding of disulfiram together with sodium nitrite
    • Lijinsky W, Reuber MD. Tumor induced in Fischer F344 rats by the feeding of disulfiram together with sodium nitrite. Food Chem Toxicol 18:85-87, 1980.
    • (1980) Food Chem Toxicol , vol.18 , pp. 85-87
    • Lijinsky, W.1    Reuber, M.D.2
  • 9
    • 0026650040 scopus 로고
    • Proline dithiocarbamate inhibits N-nitrosodiethylamine induced liver carcinogenesis
    • Hadjiolov D, Frank N, Moog C. Proline dithiocarbamate inhibits N-nitrosodiethylamine induced liver carcinogenesis. J Cancer Res Clin Oncol 118:401-404, 1992.
    • (1992) J Cancer Res Clin Oncol , vol.118 , pp. 401-404
    • Hadjiolov, D.1    Frank, N.2    Moog, C.3
  • 10
    • 0028909052 scopus 로고
    • Compaction studies on the pharmacokinetics of hydrophilic prolinedithiocarbamate, sarcosinedithiocarbamate and the less hydrophilic diethyldithiocarbamate
    • Frank N, Christmann A, Frei E. Compaction studies on the pharmacokinetics of hydrophilic prolinedithiocarbamate, sarcosinedithiocarbamate and the less hydrophilic diethyldithiocarbamate. Toxicology 95:113-122, 1995.
    • (1995) Toxicology , vol.95 , pp. 113-122
    • Frank, N.1    Christmann, A.2    Frei, E.3
  • 11
    • 0023000572 scopus 로고
    • Fate and distribution of radioactive sodium diethyldithiocarbamate (imuthiol) in the mouse
    • Guillaumin JM, Lepape A, Renoux G. Fate and distribution of radioactive sodium diethyldithiocarbamate (imuthiol) in the mouse. Int J Immunopharmacol 8:859-865, 1986.
    • (1986) Int J Immunopharmacol , vol.8 , pp. 859-865
    • Guillaumin, J.M.1    Lepape, A.2    Renoux, G.3
  • 12
    • 0025967522 scopus 로고
    • Densitometric analysis of the local bleaching of the Neo-Timm staining pattern following intrahippocampal injection of diethyldithiocarbamate
    • Holm IE, Andreasen A, Danscher G. Densitometric analysis of the local bleaching of the Neo-Timm staining pattern following intrahippocampal injection of diethyldithiocarbamate. Histochem J 23:63-68, 1991.
    • (1991) Histochem J , vol.23 , pp. 63-68
    • Holm, I.E.1    Andreasen, A.2    Danscher, G.3
  • 13
    • 0025098423 scopus 로고
    • Influence of ditniocarbamates on the metabolism and toxicity of N-nitrosodimethylamine in rats
    • Frank N, Bertram B, Scherf HR, et al. Influence of ditniocarbamates on the metabolism and toxicity of N-nitrosodimethylamine in rats. Carcinogenesis 11:199-203, 1990.
    • (1990) Carcinogenesis , vol.11 , pp. 199-203
    • Frank, N.1    Bertram, B.2    Scherf, H.R.3
  • 14
    • 0025195687 scopus 로고
    • Sarcosine- and proline-dithiocarbamate pretreatment increases the therapeutic efficacy of doxorubicin, methotrexate, teniposide, mitoxantrone or cyclohexylchloroethylnitrosourea in leukemia L1210
    • Osswald H, Frank N. Sarcosine-and proline-dithiocarbamate pretreatment increases the therapeutic efficacy of doxorubicin, methotrexate, teniposide, mitoxantrone or cyclohexylchloroethylnitrosourea in leukemia L1210. J Cancer Res Clin Oncol 116:448-452, 1990.
    • (1990) J Cancer Res Clin Oncol , vol.116 , pp. 448-452
    • Osswald, H.1    Frank, N.2
  • 15
    • 0142239095 scopus 로고
    • Effects of alcohol on workers with carbon disulfide
    • Williams EE. Effects of alcohol on workers with carbon disulfide. JAMA 109:1472-1473, 1937.
    • (1937) JAMA , vol.109 , pp. 1472-1473
    • Williams, E.E.1
  • 16
    • 0020504341 scopus 로고
    • Mechanism of inactivation of sheep liver cytoplasmic aldehyde dehydrogenase by disulfiram
    • Kitson TM. Mechanism of inactivation of sheep liver cytoplasmic aldehyde dehydrogenase by disulfiram. Biochem J 213:551-554, 1983.
    • (1983) Biochem J , vol.213 , pp. 551-554
    • Kitson, T.M.1
  • 17
    • 0018072614 scopus 로고
    • A comparative study on the effects of disulfiram, cyanamide and 1-aminocyclopropanol on the acetaldehyde metabolism in rats
    • Marchner H, Tottmar O. A comparative study on the effects of disulfiram, cyanamide and 1-aminocyclopropanol on the acetaldehyde metabolism in rats. Acta Pharmacol Toxicol 43:219-232, 1978.
    • (1978) Acta Pharmacol Toxicol , vol.43 , pp. 219-232
    • Marchner, H.1    Tottmar, O.2
  • 19
    • 0000446057 scopus 로고
    • Inhibition of dopamine-β-hydroxylase by disulfiram
    • Goldstein M, Anagnoste B, Lauber E, et al. Inhibition of dopamine-β-hydroxylase by disulfiram. Life Sci 3:763-767, 1964.
    • (1964) Life Sci , vol.3 , pp. 763-767
    • Goldstein, M.1    Anagnoste, B.2    Lauber, E.3
  • 20
    • 0029902549 scopus 로고    scopus 로고
    • 30 kDa phosphorylation form of Bcl-2 protein in human colon
    • Guan RJ, Moss SF, Arber N, et al. 30 kDa phosphorylation form of Bcl-2 protein in human colon. Oncogene 12:2605-2609, 1996.
    • (1996) Oncogene , vol.12 , pp. 2605-2609
    • Guan, R.J.1    Moss, S.F.2    Arber, N.3
  • 21
    • 0026712117 scopus 로고
    • Human placental alkaline phosphatase: An improved purification procedure and kinetic studies
    • Chang TC, Huang SM, Huang TM, et al. Human placental alkaline phosphatase: An improved purification procedure and kinetic studies. Eur J Biochem 209:241-247, 1992.
    • (1992) Eur J Biochem , vol.209 , pp. 241-247
    • Chang, T.C.1    Huang, S.M.2    Huang, T.M.3
  • 22
    • 0027301324 scopus 로고
    • Subunit rearrangement of the cyclin-dependent kinases is associated with cellular transformation
    • Xiong Y, Zhang H, Beach D. Subunit rearrangement of the cyclin-dependent kinases is associated with cellular transformation. Genes Dev 7:1572-1583, 1993.
    • (1993) Genes Dev , vol.7 , pp. 1572-1583
    • Xiong, Y.1    Zhang, H.2    Beach, D.3
  • 23
    • 0028205372 scopus 로고
    • Chronic inhibition of superoxide dismutase produces apoptotic death of spinal neurons
    • Rothstein JD, Bristol LA, Hosler B, et al. Chronic inhibition of superoxide dismutase produces apoptotic death of spinal neurons. Proc Natl Acad Sci USA 91:4155-4159, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4155-4159
    • Rothstein, J.D.1    Bristol, L.A.2    Hosler, B.3
  • 25
    • 0027182223 scopus 로고
    • Crystal structure of cyclin-dependent kinase 2
    • De Sondt HL, Rosenblatt J, Jancarik J, et al. Crystal structure of cyclin-dependent kinase 2. Nature 363:595-602, 1993.
    • (1993) Nature , vol.363 , pp. 595-602
    • De Sondt, H.L.1    Rosenblatt, J.2    Jancarik, J.3
  • 26
    • 0028271690 scopus 로고
    • Protein kinase regulation: Insights from crystal structure analysis
    • Morgan DO, De Bondt HL. Protein kinase regulation: Insights from crystal structure analysis. Curr Opin Cell Biol 6:239-246, 1994.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 239-246
    • Morgan, D.O.1    De Bondt, H.L.2
  • 27
    • 0029737650 scopus 로고    scopus 로고
    • Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E
    • Won KA, Reed S. Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E. EMBO J 15:4182-4193, 1996.
    • (1996) EMBO J , vol.15 , pp. 4182-4193
    • Won, K.A.1    Reed, S.2
  • 28
    • 0029957947 scopus 로고    scopus 로고
    • Turnover of cyclin E by the ubiquitin-proteasome pathway is regulated by cdk2 binding and cyclin phosphorylation
    • Clurman BE, Sheaff RJ, Thress K, et al. Turnover of cyclin E by the ubiquitin-proteasome pathway is regulated by cdk2 binding and cyclin phosphorylation. Genes Dev 10:1979-1990, 1996.
    • (1996) Genes Dev , vol.10 , pp. 1979-1990
    • Clurman, B.E.1    Sheaff, R.J.2    Thress, K.3
  • 29
    • 0030930366 scopus 로고    scopus 로고
    • A model for p53-induced apoptosis
    • Polyak K, Xia Y, Zweier JL, et al. A model for p53-induced apoptosis. Nature 389:300-305, 1997.
    • (1997) Nature , vol.389 , pp. 300-305
    • Polyak, K.1    Xia, Y.2    Zweier, J.L.3
  • 30
    • 0025936623 scopus 로고
    • cdc2 phosphorylation is required for its interaction with cyclin
    • Ducommun B, Brambilla P, Felix MA, et al. cdc2 phosphorylation is required for its interaction with cyclin. EMBO J 10(11):3310-3319, 1991.
    • (1991) EMBO J , vol.10 , Issue.11 , pp. 3310-3319
    • Ducommun, B.1    Brambilla, P.2    Felix, M.A.3
  • 31
    • 0028950016 scopus 로고
    • Effects of phosphorylation by CAK on cyclin binding by CDC2 and CDK2
    • Desai D, Wessling HC, Fisher RP, et al. Effects of phosphorylation by CAK on cyclin binding by CDC2 and CDK2. Mol Cell Biol 15:345-350, 1995.
    • (1995) Mol Cell Biol , vol.15 , pp. 345-350
    • Desai, D.1    Wessling, H.C.2    Fisher, R.P.3
  • 32
    • 0029779280 scopus 로고    scopus 로고
    • Cdc25 cell-cycle phosphatase as a target of c-myc
    • Galaktionov K, Chen X, Beach D. Cdc25 cell-cycle phosphatase as a target of c-myc. Nature 382(6591):511-517, 1996.
    • (1996) Nature , vol.382 , Issue.6591 , pp. 511-517
    • Galaktionov, K.1    Chen, X.2    Beach, D.3
  • 34
    • 0028176483 scopus 로고
    • Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular artimitogenic signals
    • Polyak K, Lee MH, Erdjument-Bromage H, et al. Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular artimitogenic signals. Cell 78(1):59-66, 1994.
    • (1994) Cell , vol.78 , Issue.1 , pp. 59-66
    • Polyak, K.1    Lee, M.H.2    Erdjument-Bromage, H.3
  • 35
    • 0028220204 scopus 로고
    • p53-dependent inhibition of cyclin-dependent kinase activities in human fibroblasts during radiation-induced G1 arrest
    • Dulic V, Kaufmann WK, Wilson SJ, et al. p53-dependent inhibition of cyclin-dependent kinase activities in human fibroblasts during radiation-induced G1 arrest. Cell 76(6):1013-1023, 1994.
    • (1994) Cell , vol.76 , Issue.6 , pp. 1013-1023
    • Dulic, V.1    Kaufmann, W.K.2    Wilson, S.J.3
  • 36
    • 0030614944 scopus 로고    scopus 로고
    • INK4/CDKN2 and p53 genes cooperated to induce apoptotic tumor cell death
    • INK4/CDKN2 and p53 genes cooperated to induce apoptotic tumor cell death. Nature Med 3:313-319, 1997.
    • (1997) Nature Med , vol.3 , pp. 313-319
    • Sandig, V.1    Brand, K.2    Herwig, S.3
  • 37
    • 0029958381 scopus 로고    scopus 로고
    • Reactive oxygen species are downstream mediators of p53-dependent apoptosis
    • Johnson TM, Yu ZX, Ferrans VJ, et al. Reactive oxygen species are downstream mediators of p53-dependent apoptosis. Proc Natl Acad Sci USA 93:11848-11852, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11848-11852
    • Johnson, T.M.1    Yu, Z.X.2    Ferrans, V.J.3
  • 38
    • 0028978183 scopus 로고
    • Mice lacking p21/WAF1/CIP1 undergo normal development, but are defective in G1 checkpoint control
    • Deng C, Zhang P, Harper JW, et al. Mice lacking p21/WAF1/CIP1 undergo normal development, but are defective in G1 checkpoint control. Cell 82(4):675-684, 1995.
    • (1995) Cell , vol.82 , Issue.4 , pp. 675-684
    • Deng, C.1    Zhang, P.2    Harper, J.W.3
  • 39
    • 0030046508 scopus 로고    scopus 로고
    • Life, death, and the pursuit of apoptosis
    • White E. Life, death, and the pursuit of apoptosis. Genes Dev 10(1):1-15, 1996.
    • (1996) Genes Dev , vol.10 , Issue.1 , pp. 1-15
    • White, E.1
  • 40
    • 0025720735 scopus 로고
    • The role of Jun, Fos and AP-1 complex in cell-proliferation and transformation
    • Angel P, Karin M. The role of Jun, Fos and AP-1 complex in cell-proliferation and transformation. Biochim Biophys Acta 1072:129-157, 1991.
    • (1991) Biochim Biophys Acta , vol.1072 , pp. 129-157
    • Angel, P.1    Karin, M.2
  • 41
    • 0025959674 scopus 로고
    • Stimulus-transcription coupling in the nervous system: Involvement of the inducible proto-oncogenes fos and jun
    • Morgan JL, Curran T. Stimulus-transcription coupling in the nervous system: Involvement of the inducible proto-oncogenes fos and jun. Annu Rev Neurosci 14:421-451, 1991.
    • (1991) Annu Rev Neurosci , vol.14 , pp. 421-451
    • Morgan, J.L.1    Curran, T.2
  • 42
    • 0026341905 scopus 로고
    • Rapid and preferential activation of the c-jun gene during the mammalian UV response
    • Devary Y, Gottlieb RA, Lan LF, et al. Rapid and preferential activation of the c-jun gene during the mammalian UV response. Mol Cell Biol 11:2804-2811, 1991.
    • (1991) Mol Cell Biol , vol.11 , pp. 2804-2811
    • Devary, Y.1    Gottlieb, R.A.2    Lan, L.F.3
  • 43
    • 0025294971 scopus 로고
    • Ionizing radiation regulates expression of the c-jun proto-oncogene
    • Sherman ML, Datta R, Hallahan DE, et al. Ionizing radiation regulates expression of the c-jun proto-oncogene. Proc Natl Acad Sci USA 87:5663-5666, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5663-5666
    • Sherman, M.L.1    Datta, R.2    Hallahan, D.E.3
  • 45
    • 0031041284 scopus 로고    scopus 로고
    • NFκB/lκB proteins. Their role in cell growth, differentiation and development. Madrid, Spain, July 7-10, 1996
    • Siebenlist U. NFκB/lκB proteins. Their role in cell growth, differentiation and development. Madrid, Spain, July 7-10, 1996. Biochim Biophys Acta 1332:R7-R13, 1997.
    • (1997) Biochim Biophys Acta , vol.1332
    • Siebenlist, U.1
  • 47
    • 0028174061 scopus 로고
    • Function and activation of NF-kappa B in the immune system
    • Baeuerle P, Henkel T. Function and activation of NF-kappa B in the immune system. Annu Rev Immunol 12:141-179, 1994.
    • (1994) Annu Rev Immunol , vol.12 , pp. 141-179
    • Baeuerle, P.1    Henkel, T.2
  • 48
    • 0028971289 scopus 로고
    • Rel/NF-kappa B/I kappa B family: Intimate tales of association and dissociation
    • Verma IM, Stevenson JK, Schwarz EM, et al. Rel/NF-kappa B/I kappa B family: Intimate tales of association and dissociation. Genes Dev 9:2723-2735, 1995.
    • (1995) Genes Dev , vol.9 , pp. 2723-2735
    • Verma, I.M.1    Stevenson, J.K.2    Schwarz, E.M.3
  • 49
    • 0028972845 scopus 로고
    • Mechanistic aspects of NF-kappa B regulation: The emerging role of phosphorylation and proteolysis
    • Finco T, Baldwin A. Mechanistic aspects of NF-kappa B regulation: The emerging role of phosphorylation and proteolysis. Immunity 3:263-272, 1995.
    • (1995) Immunity , vol.3 , pp. 263-272
    • Finco, T.1    Baldwin, A.2
  • 50
    • 0029874138 scopus 로고    scopus 로고
    • The NF-kappa B and I kappa B proteins, new discoveries and insights
    • Baldwin AS-Jr. The NF-kappa B and I kappa B proteins, new discoveries and insights. Annu Rev Immunol 14:649-683, 1996.
    • (1996) Annu Rev Immunol , vol.14 , pp. 649-683
    • Baldwin Jr., A.S.1
  • 51
    • 0029999656 scopus 로고    scopus 로고
    • Bcl-2 down-regulates the activity of transcription factor NFκB induced upon apoptosis
    • Grimm S, Bauer M, Baeuerle PA, et al. Bcl-2 down-regulates the activity of transcription factor NFκB induced upon apoptosis. J Cell Biol 134:13-23, 1996.
    • (1996) J Cell Biol , vol.134 , pp. 13-23
    • Grimm, S.1    Bauer, M.2    Baeuerle, P.A.3
  • 52
    • 0026590541 scopus 로고
    • Dithiocarbamates as potent inhibitors of nuclear factor kappa B activation in intact cells
    • Schreck R, Meier B, Mannel DN, et al. Dithiocarbamates as potent inhibitors of nuclear factor kappa B activation in intact cells. J Exp Med 175:1181-1194, 1992.
    • (1992) J Exp Med , vol.175 , pp. 1181-1194
    • Schreck, R.1    Meier, B.2    Mannel, D.N.3
  • 53
    • 0027729892 scopus 로고
    • High levels of c-rel, expression are associated with programmed cell death in the developing avian embryo and in bone marrow cells in vitro
    • Abbadie C, Kabrun N, Bouali F, et al. High levels of c-rel, expression are associated with programmed cell death in the developing avian embryo and in bone marrow cells in vitro. Cell 75:899-912, 1993.
    • (1993) Cell , vol.75 , pp. 899-912
    • Abbadie, C.1    Kabrun, N.2    Bouali, F.3


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