메뉴 건너뛰기




Volumn 19, Issue 4, 1999, Pages 221-228

Response of the olfactory bulb antioxidant system following diethyldithiocarbamate (DDTC) administration in rats

Author keywords

Antioxidant system; Brain; Diethyldithiocarbamate; Free radicals; Lipid peroxidation; Olfactory bulb; Reactive oxygen species

Indexed keywords

ANTIOXIDANT; CATALASE; DIETHYLDITHIOCARBAMIC ACID; GLUTATHIONE; GLUTATHIONE REDUCTASE; MALONALDEHYDE; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE;

EID: 0032777710     PISSN: 0260437X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1263(199907/08)19:4<221::AID-JAT574>3.0.CO;2-3     Document Type: Article
Times cited : (9)

References (47)
  • 1
    • 0017750112 scopus 로고
    • Denervation in the primary olfactory pathway of mice. IV. Biochemical and morphological evidence for neuronal replacement following nerve section
    • J. Harding, P. P. C. Graziadei, G. A. Monti Graziadei and F. L. Margolis, Denervation in the primary olfactory pathway of mice. IV. Biochemical and morphological evidence for neuronal replacement following nerve section. Brain Res. 132, 11-28 (1977).
    • (1977) Brain Res. , vol.132 , pp. 11-28
    • Harding, J.1    Graziadei, P.P.C.2    Monti Graziadei, G.A.3    Margolis, F.L.4
  • 2
    • 0018404034 scopus 로고
    • Neurogenesis and neuron regeneration in the olfactory system of mammals
    • P. P. C. Graziadei and G. A. Monti Graziadei, Neurogenesis and neuron regeneration in the olfactory system of mammals. J. Neurocytol. 8, 1-18 (1979).
    • (1979) J. Neurocytol. , vol.8 , pp. 1-18
    • Graziadei, P.P.C.1    Monti Graziadei, G.A.2
  • 3
    • 0028959768 scopus 로고
    • Olfactory toxicity of diethyldithiocarbamate (DDTC) and disulfiram and the protective effect of DDTC against the olfactory toxicity of dichlobenil
    • N. J. Deamer and M. B. Genter, Olfactory toxicity of diethyldithiocarbamate (DDTC) and disulfiram and the protective effect of DDTC against the olfactory toxicity of dichlobenil. Chem.-Biol. Interact. 95, 215-226 (1995).
    • (1995) Chem.-biol. Interact. , vol.95 , pp. 215-226
    • Deamer, N.J.1    Genter, M.B.2
  • 4
    • 0030914821 scopus 로고    scopus 로고
    • Olfactory mucosal lesions following subcutaneous diethyldithiocarbamate (DDTC)
    • R. Ravi, A. Krall, L. P. Rybak and R. G. Struble, Olfactory mucosal lesions following subcutaneous diethyldithiocarbamate (DDTC). J. Neurotoxicol. 18, 123-128 (1997).
    • (1997) J. Neurotoxicol. , vol.18 , pp. 123-128
    • Ravi, R.1    Krall, A.2    Rybak, L.P.3    Struble, R.G.4
  • 5
    • 0032484499 scopus 로고    scopus 로고
    • Beta amyloid precursor protein-like immunoreactivity is upregulated during olfactory nerve regeneration in adult rats
    • R. G. Struble, D. N. Dhanraj, U. Mei, M. Wilson, R. Wang and V. Ramkumar, Beta amyloid precursor protein-like immunoreactivity is upregulated during olfactory nerve regeneration in adult rats. Brain Res. 780, 129-137 (1998).
    • (1998) Brain Res. , vol.780 , pp. 129-137
    • Struble, R.G.1    Dhanraj, D.N.2    Mei, U.3    Wilson, M.4    Wang, R.5    Ramkumar, V.6
  • 6
    • 77957179384 scopus 로고
    • Mechanism of protection by diethyldithiocarbonate against cis-platin ototoxicity: Antioxidant system
    • L. P. Rybak, R. Ravi and S. M. Somani, Mechanism of protection by diethyldithiocarbonate against cis-platin ototoxicity: antioxidant system. Fundam. Appl. Toxicol. 26, 293-300 (1995).
    • (1995) Fundam. Appl. Toxicol. , vol.26 , pp. 293-300
    • Rybak, L.P.1    Ravi, R.2    Somani, S.M.3
  • 7
    • 0029118680 scopus 로고
    • Diethyldithiocarbonate protection against cis-platin nephrotoxicity: Antioxidant system
    • S. M. Somani, R. Ravi and L. P. Rybak, Diethyldithiocarbonate protection against cis-platin nephrotoxicity: antioxidant system. Drug Chem. Toxicol. 18, 151-170 (1995).
    • (1995) Drug Chem. Toxicol. , vol.18 , pp. 151-170
    • Somani, S.M.1    Ravi, R.2    Rybak, L.P.3
  • 8
    • 0028890599 scopus 로고
    • The effects of disulfiram on the hippocampus and cerebellum of the rat brain: A study on oxidative stress
    • E. Delmaestro and L. D. Trombetta. The effects of disulfiram on the hippocampus and cerebellum of the rat brain: a study on oxidative stress. Toxicol. Lett. 75, 235-243 (1995).
    • (1995) Toxicol. Lett. , vol.75 , pp. 235-243
    • Delmaestro, E.1    Trombetta, L.D.2
  • 9
    • 0017294656 scopus 로고
    • In vivo inhibition of superoxide dismutase in mice by diethyldithiocarbamate
    • R. E. Heikkila, F. S. Cabbat and G. Cohen, In vivo inhibition of superoxide dismutase in mice by diethyldithiocarbamate. J. Biol. Chem. 251, 2182-2185 (1976).
    • (1976) J. Biol. Chem. , vol.251 , pp. 2182-2185
    • Heikkila, R.E.1    Cabbat, F.S.2    Cohen, G.3
  • 10
    • 0019877295 scopus 로고
    • Reexamination of the reaction of diethyldithiocarbamate with the copper of superoxide dismutase
    • D. Cocco, L. Calabrese, A. Rigo, E. Argese and G. Rotilio, Reexamination of the reaction of diethyldithiocarbamate with the copper of superoxide dismutase. J. Biol. Chem. 256, 8983-8986 (1981).
    • (1981) J. Biol. Chem. , vol.256 , pp. 8983-8986
    • Cocco, D.1    Calabrese, L.2    Rigo, A.3    Argese, E.4    Rotilio, G.5
  • 11
    • 0029921770 scopus 로고    scopus 로고
    • Diethyldithiocarbamate, a superoxide dismutase inhibitor, reduces indomethacin-induced gastric lesions in rats
    • K. Takeuchi, K. Takehara and T. Ohuchi, Diethyldithiocarbamate, a superoxide dismutase inhibitor, reduces indomethacin-induced gastric lesions in rats. Digestion 57, 201-209 (1996).
    • (1996) Digestion , vol.57 , pp. 201-209
    • Takeuchi, K.1    Takehara, K.2    Ohuchi, T.3
  • 12
    • 0023951787 scopus 로고
    • Protective effect of glutathione on diethyldithiocarbamate (DDC) cytotoxicity: A possible mechanism
    • L. D. Trombetta, M. Toulon and S. Jamall, Protective effect of glutathione on diethyldithiocarbamate (DDC) cytotoxicity: a possible mechanism. Toxicol. Appl. Pharmacol. 93, 154-164 (1988).
    • (1988) Toxicol. Appl. Pharmacol. , vol.93 , pp. 154-164
    • Trombetta, L.D.1    Toulon, M.2    Jamall, S.3
  • 13
    • 0343878530 scopus 로고
    • Reconstitution of the olfactory epithelium and re-innervation of the olfactory bulb after methyl bromide lesions
    • J. E. Schwob and S. L. Youngentob, Reconstitution of the olfactory epithelium and re-innervation of the olfactory bulb after methyl bromide lesions. Soc. Neurosci. Abst. 17, 635 (1991).
    • (1991) Soc. Neurosci. Abst. , vol.17 , pp. 635
    • Schwob, J.E.1    Youngentob, S.L.2
  • 14
    • 0029166123 scopus 로고
    • Reconstitution of the rat olfactory epithelium after methyl bromide-induced lesion
    • J. E. Schwob, S. L. Youngentob and R. C. Mezza, Reconstitution of the rat olfactory epithelium after methyl bromide-induced lesion. J. Comp. Neurol. 359, 15-37 (1995).
    • (1995) J. Comp. Neurol. , vol.359 , pp. 15-37
    • Schwob, J.E.1    Youngentob, S.L.2    Mezza, R.C.3
  • 15
    • 0023079953 scopus 로고
    • High performance liquid chromatography of thiols and disulfides: Dinitrophenol derivatives
    • W. M. Farris and D. J. Reed, High performance liquid chromatography of thiols and disulfides: dinitrophenol derivatives. Methods Enzymol. 143, 101-109 (1987).
    • (1987) Methods Enzymol. , vol.143 , pp. 101-109
    • Farris, W.M.1    Reed, D.J.2
  • 16
    • 0015523099 scopus 로고
    • The role of superoxide anion in the autooxidation of epinephrine and a simple assay for superoxide dismutase
    • H. P. Misra and H. P. Fridovich, The role of superoxide anion in the autooxidation of epinephrine and a simple assay for superoxide dismutase. J. Biol. Chem. 247, 3170-3175 (1972).
    • (1972) J. Biol. Chem. , vol.247 , pp. 3170-3175
    • Misra, H.P.1    Fridovich, H.P.2
  • 17
    • 0000524408 scopus 로고
    • Catalase
    • H. Aebi, Catalase. Methods Enzymol. 105, 125-126 (1984).
    • (1984) Methods Enzymol. , vol.105 , pp. 125-126
    • Aebi, H.1
  • 18
  • 20
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animals and tissues by thiobarbituric acid reaction
    • H. Ohkawa, N. Ohishi and K. Yagi, Assay for lipid peroxides in animals and tissues by thiobarbituric acid reaction. Anal. Biochem. 95, 351-358 (1979).
    • (1979) Anal. Biochem. , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 21
    • 0019776662 scopus 로고
    • Minimization of variation in the response to different protein of the Coomassie blue G dye-binding assay for protein
    • S. M. Read and D. H. Northcote, Minimization of variation in the response to different protein of the Coomassie blue G dye-binding assay for protein. Anal. Biochem. 116, 53-64 (1981).
    • (1981) Anal. Biochem. , vol.116 , pp. 53-64
    • Read, S.M.1    Northcote, D.H.2
  • 22
    • 0027918558 scopus 로고
    • Olfactory neuroblasts from Alzheimer donors: Studies on APP processing and cell regulation
    • B. Wolozin, P. Lesch, R. Lebovics and T. Sunderland, Olfactory neuroblasts from Alzheimer donors: studies on APP processing and cell regulation. Biol. Psychiat. 34, 824-838 (1993).
    • (1993) Biol. Psychiat. , vol.34 , pp. 824-838
    • Wolozin, B.1    Lesch, P.2    Lebovics, R.3    Sunderland, T.4
  • 23
    • 0029970099 scopus 로고    scopus 로고
    • Depletion of brain glutathione results in a decrease of glutathione reductase activity; an enzyme susceptible to oxidative damage
    • J. E. Barker, S. J. Heales, A. Cassidy, J. P. Bolanos, J. M. Land and J. B. Clark, Depletion of brain glutathione results in a decrease of glutathione reductase activity; an enzyme susceptible to oxidative damage. Brain Res. 716, 118-122 (1996).
    • (1996) Brain Res. , vol.716 , pp. 118-122
    • Barker, J.E.1    Heales, S.J.2    Cassidy, A.3    Bolanos, J.P.4    Land, J.M.5    Clark, J.B.6
  • 25
    • 0030222337 scopus 로고    scopus 로고
    • Manganese and copper-zinc superoxide dismutases in the human olfactory mucosa: Increased immunoreactivity in Alzheimer's disease
    • A. Kulkarni-Narla, T. V. Getchell, F. A. Schmitt and M. L. Getchell, Manganese and copper-zinc superoxide dismutases in the human olfactory mucosa: increased immunoreactivity in Alzheimer's disease. Exp. Neurol. 140, 115-125 (1996).
    • (1996) Exp. Neurol. , vol.140 , pp. 115-125
    • Kulkarni-Narla, A.1    Getchell, T.V.2    Schmitt, F.A.3    Getchell, M.L.4
  • 26
    • 0026773281 scopus 로고
    • Oxygen free radicals as key mediators in neurological diseases: Fact or fiction
    • B. Halliwell, Oxygen free radicals as key mediators in neurological diseases: fact or fiction. Ann. Neurol. 32, 510-515 (1992).
    • (1992) Ann. Neurol. , vol.32 , pp. 510-515
    • Halliwell, B.1
  • 27
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • I. Fridovich, Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64, 97-112 (1995).
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 30
    • 0026131493 scopus 로고
    • Molecular structure of a functional rat gene for manganese-containing superoxide dismutase
    • Y. S. Ho, A. J. Howard and J. D. Crapo, Molecular structure of a functional rat gene for manganese-containing superoxide dismutase. Am. J. Respir. Cell. Mol. Biol. 4, 278-286 (1991).
    • (1991) Am. J. Respir. Cell. Mol. Biol. , vol.4 , pp. 278-286
    • Ho, Y.S.1    Howard, A.J.2    Crapo, J.D.3
  • 31
    • 0027394553 scopus 로고
    • Overexpression of mitochondria manganese superoxide dismutase promotes the survival of tumor cells exposed to interleukin-1, tumor necrosis factor, selected anticancer drugs and ionizing radiation
    • K. Hirose, D. Longo, J. J. Oppenheim and K. Matushima, Overexpression of mitochondria manganese superoxide dismutase promotes the survival of tumor cells exposed to interleukin-1, tumor necrosis factor, selected anticancer drugs and ionizing radiation. FASEB J. 7, 361-368 (1993).
    • (1993) FASEB J. , vol.7 , pp. 361-368
    • Hirose, K.1    Longo, D.2    Oppenheim, J.J.3    Matushima, K.4
  • 32
    • 0028800236 scopus 로고
    • Differential regulation of manganese superoxide dismutase activity by alcohol and TNF in human hepatoma cells
    • C. S. Perera, D. K. St. Clair and C. J. McClain, Differential regulation of manganese superoxide dismutase activity by alcohol and TNF in human hepatoma cells. Arch. Biochem. Biophys. 323, 471-476 (1995).
    • (1995) Arch. Biochem. Biophys. , vol.323 , pp. 471-476
    • Perera, C.S.1    St. Clair, D.K.2    McClain, C.J.3
  • 33
    • 0026777313 scopus 로고
    • Differential regulation of manganese and copper/zinc superoxide dismutases by facial nerve transection
    • T. Yoneda, S. Inagaki, Y. Hayashi, T. Nomura and H. Takagi, Differential regulation of manganese and copper/zinc superoxide dismutases by facial nerve transection. Brain Res. 582, 342-345 (1992).
    • (1992) Brain Res. , vol.582 , pp. 342-345
    • Yoneda, T.1    Inagaki, S.2    Hayashi, Y.3    Nomura, T.4    Takagi, H.5
  • 34
    • 0029328620 scopus 로고
    • Inflammatory reaction in experimental autoimmune encephalomyelitis (EAE) is accompanied by a microglial expression of the BA4-amyloid precursor protein (APP)
    • R. B. Banati, J. Gehrmann, J. Lanne-Vieira, H. Wekerle and G. W. Kreutzberg, Inflammatory reaction in experimental autoimmune encephalomyelitis (EAE) is accompanied by a microglial expression of the BA4-amyloid precursor protein (APP). Glia 14, 209-215 (1995).
    • (1995) Glia , vol.14 , pp. 209-215
    • Banati, R.B.1    Gehrmann, J.2    Lanne-Vieira, J.3    Wekerle, H.4    Kreutzberg, G.W.5
  • 36
    • 0021984002 scopus 로고
    • Superoxide dismutase isozyme in normal brains and in brains from patients with dementia of Alzheimer type
    • S. L. Marklund, R. Adolfsson, C. G. Gottfries and B. Winblad, Superoxide dismutase isozyme in normal brains and in brains from patients with dementia of Alzheimer type. J. Neurol. Sci. 67, 319-325 (1985).
    • (1985) J. Neurol. Sci. , vol.67 , pp. 319-325
    • Marklund, S.L.1    Adolfsson, R.2    Gottfries, C.G.3    Winblad, B.4
  • 37
    • 0026641536 scopus 로고
    • Age-related changes in antioxidant enzymes and lipid peroxidation in brains of control and transgenic mice over expressing copper-zinc superoxide dismutase
    • I. Ceballos-Picot, A. Nicole, J. M. Clement, J. M. Bourre and P. M. Sinet, Age-related changes in antioxidant enzymes and lipid peroxidation in brains of control and transgenic mice over expressing copper-zinc superoxide dismutase. Mutat. Res. 275, 281-295 (1992).
    • (1992) Mutat. Res. , vol.275 , pp. 281-295
    • Ceballos-Picot, I.1    Nicole, A.2    Clement, J.M.3    Bourre, J.M.4    Sinet, P.M.5
  • 38
    • 0025942074 scopus 로고
    • Age-related elevation of lipid peroxidation products: Diminution of superoxide dismutase activity in the central nervous system of rats
    • A. Gupta, M. Hasan, T. Chander and N. K. Kapoor, Age-related elevation of lipid peroxidation products: diminution of superoxide dismutase activity in the central nervous system of rats. Gerontology 37, 305-309 (1992).
    • (1992) Gerontology , vol.37 , pp. 305-309
    • Gupta, A.1    Hasan, M.2    Chander, T.3    Kapoor, N.K.4
  • 39
    • 0030273295 scopus 로고    scopus 로고
    • Mitochondria, free radicals, and neurodegeneration
    • M. F. Beal, Mitochondria, free radicals, and neurodegeneration. Curr. Opin. Neurobiol. 6, 661-666 (1996).
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 661-666
    • Beal, M.F.1
  • 41
    • 0028830958 scopus 로고
    • Localization of superoxide dismutases in Alzheimer disease and Down's syndrome neocortex and hippocampus
    • A. Furuta, D. L. Price, C. A. Pardo, J. C. Troncoso, Z. Xu, N. Taniguchi and L. J. Martin, Localization of superoxide dismutases in Alzheimer disease and Down's syndrome neocortex and hippocampus. Am. J. Pathol. 146, 357-367 (1995).
    • (1995) Am. J. Pathol. , vol.146 , pp. 357-367
    • Furuta, A.1    Price, D.L.2    Pardo, C.A.3    Troncoso, J.C.4    Xu, Z.5    Taniguchi, N.6    Martin, L.J.7
  • 42
    • 0029073455 scopus 로고
    • Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease
    • M. A. Lovell, W. D. Ehman, S. M. Butler and W. R. Markesbery, Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease. Neurology 45, 1594-1601 (1995).
    • (1995) Neurology , vol.45 , pp. 1594-1601
    • Lovell, M.A.1    Ehman, W.D.2    Butler, S.M.3    Markesbery, W.R.4
  • 44
    • 0029433282 scopus 로고
    • Free radical damage, iron, and Alzheimer's disease
    • M. A. Smith and G. Perry, Free radical damage, iron, and Alzheimer's disease. J. Neurol. Sci. Suppl. 134, 92-94 (1995).
    • (1995) J. Neurol. Sci. Suppl. , vol.134 , pp. 92-94
    • Smith, M.A.1    Perry, G.2
  • 45
    • 0023696009 scopus 로고
    • Preferential expression of copper-zinc superoxide dismutase in the vulnerable cortical neurons in Alzheimer disease
    • A. Delacourte, A. Defossez, I. Ceballos, A. Nicole and P. M. Sinet, Preferential expression of copper-zinc superoxide dismutase in the vulnerable cortical neurons in Alzheimer disease. Neurosci. Lett. 92, 247-253 (1988).
    • (1988) Neurosci. Lett. , vol.92 , pp. 247-253
    • Delacourte, A.1    Defossez, A.2    Ceballos, I.3    Nicole, A.4    Sinet, P.M.5
  • 46
    • 0026823074 scopus 로고
    • Immunohistochemical evidence of antioxidant stress in Alzheimer's disease
    • M. A. Pappolla, R. A. Omar, K. S. Kim and N. K. Robakis. Immunohistochemical evidence of antioxidant stress in Alzheimer's disease. Am. J. Pathol. 140, 621-628 (1992).
    • (1992) Am. J. Pathol. , vol.140 , pp. 621-628
    • Pappolla, M.A.1    Omar, R.A.2    Kim, K.S.3    Robakis, N.K.4
  • 47
    • 0029751104 scopus 로고    scopus 로고
    • Oxidative stress and the pathogenesis of Parkinson's disease
    • P. Jenner and C. W. Olanow, Oxidative stress and the pathogenesis of Parkinson's disease. Neurology 46, S161-S170 (1996).
    • (1996) Neurology , vol.46
    • Jenner, P.1    Olanow, C.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.