메뉴 건너뛰기




Volumn 17, Issue 2, 1997, Pages 227-234

Induction of Cystine Transport and Other Stress Proteins by Disulfiram: Effects on Glutathione Levels in Cultured Cells

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; BOVINAE; CRICETINAE; CRICETULUS GRISEUS;

EID: 0031203731     PISSN: 10441549     EISSN: None     Source Type: Journal    
DOI: 10.1165/ajrcmb.17.2.2764     Document Type: Article
Times cited : (8)

References (47)
  • 2
  • 3
    • 0018973023 scopus 로고
    • Mechanism for the potentiation of oxygen toxicity by disulfiram
    • Forman, H. J., J. L. York, and A. B. Fisher. 1980. Mechanism for the potentiation of oxygen toxicity by disulfiram. J. Pharmacol. Exp. Ther. 212:452-455.
    • (1980) J. Pharmacol. Exp. Ther. , vol.212 , pp. 452-455
    • Forman, H.J.1    York, J.L.2    Fisher, A.B.3
  • 4
    • 0017926321 scopus 로고
    • Effect of diethyldithiocarbamate on oxygen toxicity and lung enzyme activity in immature and adult rats
    • Frank, L., D. L. Wood, and R. J. Roberts. 1977. Effect of diethyldithiocarbamate on oxygen toxicity and lung enzyme activity in immature and adult rats. Biochem. Pharmacol. 27:251-254.
    • (1977) Biochem. Pharmacol. , vol.27 , pp. 251-254
    • Frank, L.1    Wood, D.L.2    Roberts, R.J.3
  • 5
    • 0016090446 scopus 로고
    • An examination of the role of G-aminobutyric acid (GABA) in hyperbaric oxygen-induced convulsions in the rat. I. Effects of increased G-aminobutyric acid and protective agents
    • Alderman, J. L., B. W. Culver, and M. K. Shellenberger. 1974. An examination of the role of G-aminobutyric acid (GABA) in hyperbaric oxygen-induced convulsions in the rat. I. Effects of increased G-aminobutyric acid and protective agents. J. Pharmacol. Exp. Ther. 190:334-340.
    • (1974) J. Pharmacol. Exp. Ther. , vol.190 , pp. 334-340
    • Alderman, J.L.1    Culver, B.W.2    Shellenberger, M.K.3
  • 6
    • 0000359956 scopus 로고
    • Effects of various substances on survival times of mice exposed to different high oxygen tensions
    • Gerschman, R., D. L. Gilbert, and D. Caccamise. 1958. Effects of various substances on survival times of mice exposed to different high oxygen tensions. Am. J. Physiol. 192:563-571.
    • (1958) Am. J. Physiol. , vol.192 , pp. 563-571
    • Gerschman, R.1    Gilbert, D.L.2    Caccamise, D.3
  • 7
    • 0015156597 scopus 로고
    • Protection with disulfiram from central and pulmonary oxygen toxicity
    • Faiman, M. D., R. G. Mehl, and F. W. Oehme. 1971. Protection with disulfiram from central and pulmonary oxygen toxicity. Biochem. Pharmacol. 20:3059-3067.
    • (1971) Biochem. Pharmacol. , vol.20 , pp. 3059-3067
    • Faiman, M.D.1    Mehl, R.G.2    Oehme, F.W.3
  • 8
    • 0015954212 scopus 로고
    • Effect of disulfiram on oxygen toxicity in beagle dogs
    • Faiman, M. D., R. J. Nolan, and F. W. Oehme. 1974. Effect of disulfiram on oxygen toxicity in beagle dogs. Aerospace Med. 45:29-32.
    • (1974) Aerospace Med. , vol.45 , pp. 29-32
    • Faiman, M.D.1    Nolan, R.J.2    Oehme, F.W.3
  • 9
    • 0015806964 scopus 로고
    • Comparison of protective agents against hyperbaric oxygen in large animals
    • Currie, W. D., R. M. Gelein, Jr., and A. P. Sanders. 1973. Comparison of protective agents against hyperbaric oxygen in large animals. Aerospace Med. 44:996-998.
    • (1973) Aerospace Med. , vol.44 , pp. 996-998
    • Currie, W.D.1    Gelein Jr., R.M.2    Sanders, A.P.3
  • 10
    • 18144440833 scopus 로고
    • Effects of selenium deficiency on glutathione-induced protection from hyperbaric hyperoxia in the rat
    • Lung Cell. Mol. Physiol.
    • Jenkinson, S. G., J. M. Jordan, and C. A. Duncan. 1989. Effects of selenium deficiency on glutathione-induced protection from hyperbaric hyperoxia in the rat. Am. J. Physiol. 257(Lung Cell. Mol. Physiol.):L393-L398.
    • (1989) Am. J. Physiol. , vol.257
    • Jenkinson, S.G.1    Jordan, J.M.2    Duncan, C.A.3
  • 11
    • 0000688342 scopus 로고
    • Effects of diethyldithiocarbamate and disulfiram on glucose metabolism and glutathione content of human erythrocytes
    • Stromme, J. H. 1963. Effects of diethyldithiocarbamate and disulfiram on glucose metabolism and glutathione content of human erythrocytes. Biochem. Pharmacol. 12:705-715.
    • (1963) Biochem. Pharmacol. , vol.12 , pp. 705-715
    • Stromme, J.H.1
  • 13
    • 0019628628 scopus 로고
    • The inactivation of aldehyde dehydrogenase by disulfiram in the presence of glutathione
    • Kitson, T. M. 1981. The inactivation of aldehyde dehydrogenase by disulfiram in the presence of glutathione. Biochem. J. 199:255-258.
    • (1981) Biochem. J. , vol.199 , pp. 255-258
    • Kitson, T.M.1
  • 14
    • 0015060863 scopus 로고
    • Mechanism of the inhibition of aldehyde dehydrogenase in vivo by disulfiram and diethyldithiocarbamate
    • Deitrich, R. A., and V. G. Erwin. 1975. Mechanism of the inhibition of aldehyde dehydrogenase in vivo by disulfiram and diethyldithiocarbamate. Mol. Pharmacol. 7:301-307.
    • (1975) Mol. Pharmacol. , vol.7 , pp. 301-307
    • Deitrich, R.A.1    Erwin, V.G.2
  • 15
    • 0017294656 scopus 로고
    • In vivo inhibition of superoxide dismutase in mice by diethyldithiocarbamate
    • Heikkila, R. E., F. S. Cabbat, and G. Cohen. 1976. In vivo inhibition of superoxide dismutase in mice by diethyldithiocarbamate. J Biol. Chem. 251:2182-2185.
    • (1976) J Biol. Chem. , vol.251 , pp. 2182-2185
    • Heikkila, R.E.1    Cabbat, F.S.2    Cohen, G.3
  • 16
    • 0018604230 scopus 로고
    • Reaction of copper-zinc superoxide dismutase with diethyldithiocarbamate
    • Misra, H. P. 1979. Reaction of copper-zinc superoxide dismutase with diethyldithiocarbamate. J. Biol. Chem. 254:11623-11628.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11623-11628
    • Misra, H.P.1
  • 17
    • 0018841837 scopus 로고
    • Transition series metals and sulfhydryl reagents induce the synthesis of four proteins in eukaryotic cells
    • Levinson, W., H. Oppermann, and J. Jackson. 1979. Transition series metals and sulfhydryl reagents induce the synthesis of four proteins in eukaryotic cells. Biochim. Biophys. Acta 606:170-180.
    • (1979) Biochim. Biophys. Acta , vol.606 , pp. 170-180
    • Levinson, W.1    Oppermann, H.2    Jackson, J.3
  • 18
    • 0022871192 scopus 로고
    • Induction of 32- and 34-kDa stress proteins by sodium arsenite, heavy metals, and thiol-reactive agents
    • Caltabiano, M. M., T. P. Koestler, and R. G. Poste Gand Greig. 1986. Induction of 32- and 34-kDa stress proteins by sodium arsenite, heavy metals, and thiol-reactive agents. J. Biol. Chem. 261:13381-13386.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13381-13386
    • Caltabiano, M.M.1    Koestler, T.P.2    Poste Gand Greig, R.G.3
  • 19
    • 0022522043 scopus 로고
    • Chemically induced resistance to heat treatment and stress protein synthesis in cultured mammalian cells
    • Haveman, J., G. C. Li, J. Y. Mak, and J. B. A. Kipp. 1986. Chemically induced resistance to heat treatment and stress protein synthesis in cultured mammalian cells. Int. J. Radiat. Biol. 50:51-64.
    • (1986) Int. J. Radiat. Biol. , vol.50 , pp. 51-64
    • Haveman, J.1    Li, G.C.2    Mak, J.Y.3    Kipp, J.B.A.4
  • 20
    • 0020085191 scopus 로고
    • Modulation of synthesis of specific proteins in endothelial cells by copper, cadmium, and disulfiram: An early response to an angiogenic inducer of cell migration
    • Hannan, G. N., and B. R. McAuslan. 1982. Modulation of synthesis of specific proteins in endothelial cells by copper, cadmium, and disulfiram: an early response to an angiogenic inducer of cell migration. J. Cell. Physiol. 111:207-212.
    • (1982) J. Cell. Physiol. , vol.111 , pp. 207-212
    • Hannan, G.N.1    McAuslan, B.R.2
  • 21
    • 0025303397 scopus 로고
    • Induction in mouse peritoneal macrophages of 34 kDa stress protein and heme oxygenase by sulfhydryl-reactive agents
    • Taketani, S., H. Sato, T. Yoshinaga, T. Ishii, and S. Bannai. 1991. Induction in mouse peritoneal macrophages of 34 kDa stress protein and heme oxygenase by sulfhydryl-reactive agents. J. Biochem. 108:28-32.
    • (1991) J. Biochem. , vol.108 , pp. 28-32
    • Taketani, S.1    Sato, H.2    Yoshinaga, T.3    Ishii, T.4    Bannai, S.5
  • 22
    • 0025752414 scopus 로고
    • Enhancement of glutathione levels in mouse peritoneal macrophages by sodium arsenite, cadmium chloride and glucose/glucose oxidase
    • Bannai, S., H. Sato, T. Ishii, and S. Taketani. 1991. Enhancement of glutathione levels in mouse peritoneal macrophages by sodium arsenite, cadmium chloride and glucose/glucose oxidase. Biochim. Biophys. Acta 1092: 175-179.
    • (1991) Biochim. Biophys. Acta , vol.1092 , pp. 175-179
    • Bannai, S.1    Sato, H.2    Ishii, T.3    Taketani, S.4
  • 23
    • 0001013954 scopus 로고
    • Regulation of cellular glutathione levels
    • Lung Cell. Mol. Physiol.
    • Deneke, S. M., and B. L. Fanburg. 1989. Regulation of cellular glutathione levels. Am. J. Physiol. 257(Lung Cell. Mol. Physiol.):L163-L173.
    • (1989) Am. J. Physiol. , vol.257
    • Deneke, S.M.1    Fanburg, B.L.2
  • 24
    • 0027126243 scopus 로고
    • Induction of cystine transport in bovine pulmonary artery endothelial cells by sodium arsenite
    • Deneke, S. M. 1992. Induction of cystine transport in bovine pulmonary artery endothelial cells by sodium arsenite. Biochim. Biophys. Acta 1109: 127-131.
    • (1992) Biochim. Biophys. Acta , vol.1109 , pp. 127-131
    • Deneke, S.M.1
  • 25
    • 0001673410 scopus 로고
    • Serotonin uptake by bovine pulmonary artery endothelial cells
    • Lee, S. L., and B. L. Fanburg. 1986. Serotonin uptake by bovine pulmonary artery endothelial cells. Am. J. Physiol. 250:C761-C765.
    • (1986) Am. J. Physiol. , vol.250
    • Lee, S.L.1    Fanburg, B.L.2
  • 26
    • 0023572282 scopus 로고
    • Characterization of glutamic acid uptake by bovine pulmonary arterial endothelial cells
    • Steiger, V., S. M. Deneke, and B. L. Fanburg. 1987. Characterization of glutamic acid uptake by bovine pulmonary arterial endothelial cells. J. Appl. Physiol. 63:1961-1965.
    • (1987) J. Appl. Physiol. , vol.63 , pp. 1961-1965
    • Steiger, V.1    Deneke, S.M.2    Fanburg, B.L.3
  • 27
    • 0024444942 scopus 로고
    • Increases in endothelial cell glutathione and precursor amino acid uptake by diethylmaleate and hyperoxia
    • Lung Cell. Mol. Physiol.
    • Deneke, S. M., D. F. Baxter, D. T. Phelps, and B. L. Fanburg. 1989. Increases in endothelial cell glutathione and precursor amino acid uptake by diethylmaleate and hyperoxia. Am. J. Physiol. 257(Lung Cell. Mol. Physiol.):L265-L271.
    • (1989) Am. J. Physiol. , vol.257
    • Deneke, S.M.1    Baxter, D.F.2    Phelps, D.T.3    Fanburg, B.L.4
  • 28
    • 0001030010 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione
    • Tietze, F. 1969. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione. Anal. Biochem. 27:205-222.
    • (1969) Anal. Biochem. , vol.27 , pp. 205-222
    • Tietze, F.1
  • 29
    • 0019740345 scopus 로고
    • Assay of glutathione, glutathione disulfide, and glulathione mixed disulfides in biological samples
    • Akerboom, T. P. M., and H. Sies. 1981. Assay of glutathione, glutathione disulfide, and glulathione mixed disulfides in biological samples. Methods Enzymol. 77:373-382.
    • (1981) Methods Enzymol. , vol.77 , pp. 373-382
    • Akerboom, T.P.M.1    Sies, H.2
  • 30
    • 0014691242 scopus 로고
    • Superoxide dismutase on enzymatic function for erythrocupreine
    • McCord, J. M., and I. Fridovich. 1969. Superoxide dismutase on enzymatic function for erythrocupreine. J. Biol. Chem. 244:6049-6055.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 31
    • 0018158892 scopus 로고
    • Preparation and assay of superoxide dismutases
    • Crapo, J. D., J. M. McCord, and I. Fridovich. 1978. Preparation and assay of superoxide dismutases. Methods Enzymol. 53:382-393.
    • (1978) Methods Enzymol. , vol.53 , pp. 382-393
    • Crapo, J.D.1    McCord, J.M.2    Fridovich, I.3
  • 32
    • 0025905225 scopus 로고
    • Hypoxia induces a specific set of stress proteins in cultured endothelial cells
    • Zimmerman, L. H., R. A. Levine, and H. W. Farber. 1991. Hypoxia induces a specific set of stress proteins in cultured endothelial cells. J. Clin. Invest. 87:908-914.
    • (1991) J. Clin. Invest. , vol.87 , pp. 908-914
    • Zimmerman, L.H.1    Levine, R.A.2    Farber, H.W.3
  • 34
    • 0026506535 scopus 로고
    • Endothelial cell cystine uptake and glutathione increase with N,N-bis(2-chloroethyl)-N-nitrosourea exposure
    • Lung Cell. Mol. Physiol.
    • Deneke, S. M., R. A. Lawrence, and S. G. Jenkinson. 1992. Endothelial cell cystine uptake and glutathione increase with N,N-bis(2-chloroethyl)-N-nitrosourea exposure. Am. J. Physiol. 262(Lung Cell. Mol. Physiol.):L301-L304.
    • (1992) Am. J. Physiol. , vol.262
    • Deneke, S.M.1    Lawrence, R.A.2    Jenkinson, S.G.3
  • 35
    • 0021348393 scopus 로고
    • Induction of cystine and glutamate transport activity in human fibroblasts by diethylmaleate and other electrophilic agents
    • Bannai, S. 1984. Induction of cystine and glutamate transport activity in human fibroblasts by diethylmaleate and other electrophilic agents. J. Biol. Chem. 259:2435-2440.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2435-2440
    • Bannai, S.1
  • 36
    • 0021215013 scopus 로고
    • Transport of cystine and cysteine in mammalian cells
    • Bannai, S. 1984. Transport of cystine and cysteine in mammalian cells. Biochim. Biophys. Acta 779:289-306.
    • (1984) Biochim. Biophys. Acta , vol.779 , pp. 289-306
    • Bannai, S.1
  • 37
    • 0029984062 scopus 로고    scopus 로고
    • Antioxidant and redox regulation of gene transcription
    • Sen, C. K., and L. Packer. 1996. Antioxidant and redox regulation of gene transcription. FASEB J. 10:709-720.
    • (1996) FASEB J. , vol.10 , pp. 709-720
    • Sen, C.K.1    Packer, L.2
  • 38
    • 0029760957 scopus 로고    scopus 로고
    • Redox regulation of transcriptional activators
    • Sun, Y., and L. W. Oberley. 1996. Redox regulation of transcriptional activators. Free Radic. Biol. Med. 21:335-348.
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 335-348
    • Sun, Y.1    Oberley, L.W.2
  • 42
    • 0019746750 scopus 로고
    • The inhibitory action of dithiocarbamates and carbon disulfides on malonaldehyde formation resulting from lipid peroxidation in rat liver microsomes
    • Freind, K. J., K. G. Romer, and A. M. Ramal. 1981. The inhibitory action of dithiocarbamates and carbon disulfides on malonaldehyde formation resulting from lipid peroxidation in rat liver microsomes. J. Appl. Toxicol. 1:215-219.
    • (1981) J. Appl. Toxicol. , vol.1 , pp. 215-219
    • Freind, K.J.1    Romer, K.G.2    Ramal, A.M.3
  • 43
    • 0024822257 scopus 로고
    • The inhibition of lipid peroxidation by disulfiram prevents the killing of cultured hepatocytes by allyl alcohol, tert-butyl hydroperoxide, hydrogen peroxide and diethylmaleate
    • Farber, J. L. 1989. The inhibition of lipid peroxidation by disulfiram prevents the killing of cultured hepatocytes by allyl alcohol, tert-butyl hydroperoxide, hydrogen peroxide and diethylmaleate. Chem. Biol. Interact. 72:269-275.
    • (1989) Chem. Biol. Interact. , vol.72 , pp. 269-275
    • Farber, J.L.1
  • 44
    • 0024822257 scopus 로고
    • The inhibition of lipid peroxidation by disulfiram prevents the killing of cultured hepatocytes by allyl alcohol, terl-butyl hydroperoxide, hydrogen peroxide and diethylmaleate
    • Kyle, M. E., A. Serroni, and J. L. Farber. 1989. The inhibition of lipid peroxidation by disulfiram prevents the killing of cultured hepatocytes by allyl alcohol, terl-butyl hydroperoxide, hydrogen peroxide and diethylmaleate. Chem. Biol. Interact. 72:269-275.
    • (1989) Chem. Biol. Interact. , vol.72 , pp. 269-275
    • Kyle, M.E.1    Serroni, A.2    Farber, J.L.3
  • 45
    • 0024431144 scopus 로고
    • Lipid peroxidation-dependent and -independent protein thiol modifications in isolated rat hepatocytes: Differential effects of vitamin E and disulfiram
    • Dogterom, P., G. J. Mulder, and J. F. Nagelkerke. 1989. Lipid peroxidation-dependent and -independent protein thiol modifications in isolated rat hepatocytes: differential effects of vitamin E and disulfiram. Chem. Biol. Interact. 71:291-306.
    • (1989) Chem. Biol. Interact. , vol.71 , pp. 291-306
    • Dogterom, P.1    Mulder, G.J.2    Nagelkerke, J.F.3
  • 46
    • 0018778879 scopus 로고
    • In vivo and in vitro effects of thiuram disulfides and dithiocarbamates on hepatic microsomal drug metabolism in the rat
    • Zemaitis, M. A., and F. E. Greene. 1979. In vivo and in vitro effects of thiuram disulfides and dithiocarbamates on hepatic microsomal drug metabolism in the rat. Toxicol Appl. Pharmacol. 48:343-350.
    • (1979) Toxicol Appl. Pharmacol. , vol.48 , pp. 343-350
    • Zemaitis, M.A.1    Greene, F.E.2
  • 47
    • 0015298096 scopus 로고
    • The regulation of rat liver xanthine oxidase: Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (Type D) into oxidase (Type O) and purification of the enzyme
    • Della Corte, E., and F. Stirpe. 1972. The regulation of rat liver xanthine oxidase: involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (Type D) into oxidase (Type O) and purification of the enzyme. Biochem. J. 126:739-745.
    • (1972) Biochem. J. , vol.126 , pp. 739-745
    • Della Corte, E.1    Stirpe, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.