메뉴 건너뛰기




Volumn 16, Issue 3, 1997, Pages 177-181

Phenytoin-mediated oxidative stress in serum of female epileptics: A possible pathogenesis in the fetal hydantoin syndrome

Author keywords

glutathione; lipid peroxidation; phenytoin; superoxide dismutase

Indexed keywords

COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; GLUTATHIONE; MALONALDEHYDE; PHENYTOIN; ZINC;

EID: 0030960499     PISSN: 09603271     EISSN: None     Source Type: Journal    
DOI: 10.1177/096032719701600308     Document Type: Article
Times cited : (56)

References (28)
  • 2
    • 0025262246 scopus 로고
    • Covalent binding of phenytoin to protein and modulation of diphenylhydantoin metabolism by thiols in A/J mouse liver microsomes
    • Roy D., Snodgrass WR Covalent binding of phenytoin to protein and modulation of diphenylhydantoin metabolism by thiols in A/J mouse liver microsomes. Journal of Pharmacology and Experimental Therapeutics 1990; 252: 895-900.
    • (1990) Journal of Pharmacology and Experimental Therapeutics , vol.252 , pp. 895-900
    • Roy, D.1    Snodgrass, W.R.2
  • 4
    • 7944239778 scopus 로고
    • Studies on variation in serum copper and copper oxidase activity, together with studies on the copper content of the cerebrospinal fluid, with particular reference to the variations in multiple sclerosis
    • Plum CM, Hansen SE Studies on variation in serum copper and copper oxidase activity, together with studies on the copper content of the cerebrospinal fluid, with particular reference to the variations in multiple sclerosis. Acta Psychiatrica Scandinavica 1960; 148: 41 - 78.
    • (1960) Acta Psychiatrica Scandinavica , vol.148 , pp. 41-78
    • Plum, C.M.1    Hansen, S.E.2
  • 5
    • 0013962823 scopus 로고    scopus 로고
    • Ceruloplasmin rise and PBI fall in serum due to diphenylhydantoin
    • Cantu RC, Schwab RS Ceruloplasmin rise and PBI fall in serum due to diphenylhydantoin. Archives of Neurology 1996; 15: 393 - 6.
    • (1996) Archives of Neurology , vol.15 , pp. 393-396
    • Cantu, R.C.1    Schwab, R.S.2
  • 7
    • 0020404375 scopus 로고
    • Zinc and copper metabolism in phenytoin therapy
    • Palm R., Hallmans G. Zinc and copper metabolism in phenytoin therapy. Epilepsia 1982; 23: 453 -61.
    • (1982) Epilepsia , vol.23 , pp. 453-461
    • Palm, R.1    Hallmans, G.2
  • 9
    • 0021854227 scopus 로고
    • The effects of phenytoin on serum and organ concentration of zinc and copper in cat
    • Palm R., Hanstom L., Hallmans G., Winblad B. The effects of phenytoin on serum and organ concentration of zinc and copper in cat. Epilepsia 1985; 26: 184 -8.
    • (1985) Epilepsia , vol.26 , pp. 184-188
    • Palm, R.1    Hanstom, L.2    Hallmans, G.3    Winblad, B.4
  • 11
    • 0020039616 scopus 로고
    • Serum copper concentration and hepatic enzyme induction during long-term therapy with anti-convulsants
    • Tutor JC, Fernandez MP, Paz JM Serum copper concentration and hepatic enzyme induction during long-term therapy with anti-convulsants. Clinical Chemistry 1982; 28: 1367-70.
    • (1982) Clinical Chemistry , vol.28 , pp. 1367-1370
    • Tutor, J.C.1    Fernandez, M.P.2    Paz, J.M.3
  • 12
    • 0023201142 scopus 로고
    • Lipid peroxidation in plasma as measured by liquid-chromatographic separation of malondialdehyde- thiobarbituric acid adduct
    • Wong SH, Night JA, Hopfer SM Lipid peroxidation in plasma as measured by liquid-chromatographic separation of malondialdehyde- thiobarbituric acid adduct. Clinical Chemistry 1987; 33: 214 - 20.
    • (1987) Clinical Chemistry , vol.33 , pp. 214-220
    • Wong, S.H.1    Night, J.A.2    Hopfer, S.M.3
  • 13
    • 0028022870 scopus 로고
    • Copper/zinc superoxide dismutase mRNA levels are increased in sporadic amyotrophic lateral sclerosis motorneurons
    • Bergeron C. et al. Copper/zinc superoxide dismutase mRNA levels are increased in sporadic amyotrophic lateral sclerosis motorneurons. Brain Research 1994; 659: 272 -6.
    • (1994) Brain Research , vol.659 , pp. 272-276
    • Bergeron, C.1
  • 14
    • 0026514680 scopus 로고
    • CuZn-superoxide dismutase mRNA and enzyme activity, and susceptibility to lipid peroxidation, increases with aging in murine brains
    • Haan JB, Newman JD, Kola I. CuZn-superoxide dismutase mRNA and enzyme activity, and susceptibility to lipid peroxidation, increases with aging in murine brains. Molecular Brain Research 1992; 13: 179-87.
    • (1992) Molecular Brain Research , vol.13 , pp. 179-187
    • Haan, J.B.1    Newman, J.D.2    Kola, I.3
  • 16
    • 0025699758 scopus 로고
    • Brain membrane fluidity and lipid peroxidation in the Alzheimer disease
    • Hajimohammadreza I., Brammer M. Brain membrane fluidity and lipid peroxidation in the Alzheimer disease. Neuroscience Letter 1990; 112: 333-7.
    • (1990) Neuroscience Letter , vol.112 , pp. 333-337
    • Hajimohammadreza, I.1    Brammer, M.2
  • 17
    • 0024823301 scopus 로고
    • Lipid abnormality in the brain in adult Down syndrome and Alzheimer disease
    • Brooksbank Bwl, Martinez M. Lipid abnormality in the brain in adult Down syndrome and Alzheimer disease. Molecular Chemistry and Neuropathology 1989; 11: 157 -85.
    • (1989) Molecular Chemistry and Neuropathology , vol.11 , pp. 157-185
    • Brooksbank, B.1    Martinez, M.2
  • 18
    • 0025736954 scopus 로고
    • Neuronal-specific expression of human copper-zinc superoxide dismutase gene in transgenic mice: animal model of gene dosage effects in Downs syndrome
    • Ceballos-Picot I. et al. Neuronal-specific expression of human copper-zinc superoxide dismutase gene in transgenic mice: animal model of gene dosage effects in Downs syndrome. Brain Research 1991; 552: 198 -214.
    • (1991) Brain Research , vol.552 , pp. 198-214
    • Ceballos-Picot, I.1
  • 19
    • 0020084230 scopus 로고
    • A comparative study of superoxide dismutase, catalase and lipid peroxidation in red blood cells from muscular dystrophy patients and normal controls
    • Matkovicx B., Laszlo A., Szabo L. A comparative study of superoxide dismutase, catalase and lipid peroxidation in red blood cells from muscular dystrophy patients and normal controls. Clinica Chimica Acta 1982; 118: 289 -92.
    • (1982) Clinica Chimica Acta , vol.118 , pp. 289-292
    • Matkovicx, B.1    Laszlo, A.2    Szabo, L.3
  • 20
    • 0021131198 scopus 로고
    • Superoxide dismutase, catalase, and glutathione peroxidase in red blood cells from patients with malignant disease
    • Gonzales R. et al. Superoxide dismutase, catalase, and glutathione peroxidase in red blood cells from patients with malignant disease. Cancer Research 1984; 44: 4137 -9.
    • (1984) Cancer Research , vol.44 , pp. 4137-4139
    • Gonzales, R.1
  • 21
    • 0024439958 scopus 로고
    • Elevated superoxide dismutase in Bloom syndrome: A genetic condition of oxidative stress
    • Nicotera TM et al. Elevated superoxide dismutase in Bloom syndrome: A genetic condition of oxidative stress. Cancer Research 1989; 49: 5239-43.
    • (1989) Cancer Research , vol.49 , pp. 5239-5243
    • Nicotera, T.M.1
  • 22
    • 0026593966 scopus 로고
    • Blood superoxide dismutase and plasma malondialdehyde among workers exposed to asbestos
    • Kamal A. et al. Blood superoxide dismutase and plasma malondialdehyde among workers exposed to asbestos. American Journal of Industrial Medicine 1992; 21: 353-61.
    • (1992) American Journal of Industrial Medicine , vol.21 , pp. 353-361
    • Kamal, A.1
  • 23
    • 0026064149 scopus 로고
    • Regulation of Cu, Zn superoxide dismutase with copper
    • Percival SS, Harris ED Regulation of Cu, Zn superoxide dismutase with copper. Biochemical Journal 1991; 274: 153-8.
    • (1991) Biochemical Journal , vol.274 , pp. 153-158
    • Percival, S.S.1    Harris, E.D.2
  • 24
    • 0025957551 scopus 로고
    • Evidence for co-regulation of Cu, Zu superoxide dismutase and metallothionein gene expression in yeast through transcriptional control by copper via the ACE 1 factor
    • Carri MT, Galiazzo F., Ciriolo MR, Rotilio G. Evidence for co-regulation of Cu, Zu superoxide dismutase and metallothionein gene expression in yeast through transcriptional control by copper via the ACE 1 factor. FEBS Letters 1991; 278: 263-6.
    • (1991) FEBS Letters , vol.278 , pp. 263-266
    • Carri, M.T.1    Galiazzo, F.2    Ciriolo, M.R.3    Rotilio, G.4
  • 25
    • 0028798434 scopus 로고
    • Oxidative mechanisms in the toxicity of metal ions
    • Stohs SJ, Bagchi D. Oxidative mechanisms in the toxicity of metal ions. Free Radical Biology & Medicine 1995; 18: 321- 36.
    • (1995) Free Radical Biology & Medicine , vol.18 , pp. 321-336
    • Stohs, S.J.1    Bagchi, D.2
  • 26
    • 0020972417 scopus 로고
    • Glutathione. Annual Reviews of
    • Meister A., Anderson ME Glutathione. Annual Reviews of Biochemistry 1983; 52: 711 - 60.
    • (1983) Biochemistry , vol.52 , pp. 711-760
    • Meister, A.1    Anderson, M.E.2
  • 27
    • 0028354625 scopus 로고
    • Evidence for embryonic peroxidase-catalyzed bioactivation and glutathione-dependent cytoprotection in phenytoin teratogenicity: modulation by eicosatetricnoic acid and buthionine sulfoximine in murine embryo culture
    • Miranda AF, Wiley MJ, Wells PG Evidence for embryonic peroxidase-catalyzed bioactivation and glutathione-dependent cytoprotection in phenytoin teratogenicity: modulation by eicosatetricnoic acid and buthionine sulfoximine in murine embryo culture. Toxicology and Applied Pharmacology 1994; 124: 230-41.
    • (1994) Toxicology and Applied Pharmacology , vol.124 , pp. 230-241
    • Miranda, A.F.1    Wiley, M.J.2    Wells, P.G.3
  • 28
    • 0024458721 scopus 로고
    • Enhancement of murine phenytoin teratogenicity by gammaglutamylcysteine synthetase inhibitor L-buthionine-(S,R)-sulfoximine and by the glutathione depletor diethyl mallet
    • Wong M., Helston LM, Wells PG Enhancement of murine phenytoin teratogenicity by gammaglutamylcysteine synthetase inhibitor L-buthionine-(S,R)-sulfoximine and by the glutathione depletor diethyl mallet. Teratology 1989; 40: 127-41.
    • (1989) Teratology , vol.40 , pp. 127-141
    • Wong, M.1    Helston, L.M.2    Wells, P.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.