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Volumn 26, Issue 11-12, 1999, Pages 1418-1426

Neuroprotective effects of α-lipoic acid and its positively charged amide analogue

Author keywords

Antioxidants; Free radicals; Neurotoxicity; Redox; Thioctic acid

Indexed keywords

ANTIOXIDANT; FREE RADICAL; GLUTATHIONE; THIOCTIC ACID;

EID: 0032985492     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(99)00014-3     Document Type: Article
Times cited : (93)

References (32)
  • 1
    • 0031912854 scopus 로고    scopus 로고
    • Melatonin inhibits iron-induced epileptic discharges in rats by suppressing peroxidation
    • Kabuto H., Yokoi I., Ogawa N. Melatonin inhibits iron-induced epileptic discharges in rats by suppressing peroxidation. Epilepsia. 39:1998;237-243.
    • (1998) Epilepsia , vol.39 , pp. 237-243
    • Kabuto, H.1    Yokoi, I.2    Ogawa, N.3
  • 2
    • 0030794291 scopus 로고    scopus 로고
    • Decreased total antioxidant capacity and elevated lipid hydroperoxide concentrations in sera of epileptic patients receiving phenytoin
    • Mahle C., Dasgupta A. Decreased total antioxidant capacity and elevated lipid hydroperoxide concentrations in sera of epileptic patients receiving phenytoin. Life Sci. 61:1997;437-443.
    • (1997) Life Sci. , vol.61 , pp. 437-443
    • Mahle, C.1    Dasgupta, A.2
  • 3
    • 0029933628 scopus 로고    scopus 로고
    • Cerebroprotective effect of stable nitroxide radicals in closed head injury in the rat
    • Beit-Yannai E., Zhang R., Trembovler V., Samuni A., Shohami E. Cerebroprotective effect of stable nitroxide radicals in closed head injury in the rat. Brain Res. 717:1996;22-28.
    • (1996) Brain Res. , vol.717 , pp. 22-28
    • Beit-Yannai, E.1    Zhang, R.2    Trembovler, V.3    Samuni, A.4    Shohami, E.5
  • 4
    • 0031953601 scopus 로고    scopus 로고
    • Calcium in ischemic cell death
    • Kristian T., Siesjo B.K. Calcium in ischemic cell death. Stroke. 29:1998;705-718.
    • (1998) Stroke , vol.29 , pp. 705-718
    • Kristian, T.1    Siesjo, B.K.2
  • 5
    • 17344371804 scopus 로고    scopus 로고
    • Mitochondrial manganese superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury: Suppression of peroxynitrite production, lipid peroxidation, and mitochondrial dysfunction
    • Keller J.N., Kindy M.S., Holtsberg F.W., St Clair D.K., Yen H.C., Germeyer A., Steiner S.M., Bruce-Keller A.J., Hutchins J.B., Mattson M.P. Mitochondrial manganese superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury suppression of peroxynitrite production, lipid peroxidation, and mitochondrial dysfunction . J. Neurosci. 18:1998;687-697.
    • (1998) J. Neurosci. , vol.18 , pp. 687-697
    • Keller, J.N.1    Kindy, M.S.2    Holtsberg, F.W.3    St Clair, D.K.4    Yen, H.C.5    Germeyer, A.6    Steiner, S.M.7    Bruce-Keller, A.J.8    Hutchins, J.B.9    Mattson, M.P.10
  • 6
    • 0031974368 scopus 로고    scopus 로고
    • Mitochondrial susceptibility to oxidative stress exacerbates cerebral infarction that follows permanent focal cerebral ischemia in mutant mice with manganese superoxide dismutase deficiency
    • Murakami K., Kondo T., Kawase M., Li Y., Sato S., Chen S.F., Chan P.H. Mitochondrial susceptibility to oxidative stress exacerbates cerebral infarction that follows permanent focal cerebral ischemia in mutant mice with manganese superoxide dismutase deficiency. J. Neurosci. 18:1998;205-213.
    • (1998) J. Neurosci. , vol.18 , pp. 205-213
    • Murakami, K.1    Kondo, T.2    Kawase, M.3    Li, Y.4    Sato, S.5    Chen, S.F.6    Chan, P.H.7
  • 8
    • 0031776586 scopus 로고    scopus 로고
    • Cytochemical demonstration of oxidative damage in alzheimer disease by immunochemical enhancement of the carbonyl reaction with 2, 4- dinitrophenylhydrazine [In Process Citation]
    • Smith M.A., Sayre L.M., Anderson V.E., Harris P.L., Beal M.F., Kowall N., Perry G. Cytochemical demonstration of oxidative damage in alzheimer disease by immunochemical enhancement of the carbonyl reaction with 2, 4- dinitrophenylhydrazine [In Process Citation]. J. Histochem. Cytochem. 46:1998;731-736.
    • (1998) J. Histochem. Cytochem. , vol.46 , pp. 731-736
    • Smith, M.A.1    Sayre, L.M.2    Anderson, V.E.3    Harris, P.L.4    Beal, M.F.5    Kowall, N.6    Perry, G.7
  • 9
    • 0031929586 scopus 로고    scopus 로고
    • Role of oxidative stress and the glutathione system in loss of dopamine neurons due to impairment of energy metabolism
    • Zeevalk G.D., Bernard L.P., Nicklas W.J. Role of oxidative stress and the glutathione system in loss of dopamine neurons due to impairment of energy metabolism. J. Neurochem. 70:1998;1421-1430.
    • (1998) J. Neurochem. , vol.70 , pp. 1421-1430
    • Zeevalk, G.D.1    Bernard, L.P.2    Nicklas, W.J.3
  • 10
    • 0031899172 scopus 로고    scopus 로고
    • Oxidative mechanisms in nigral cell death in Parkinson's disease [In Process Citation]
    • Jenner P. Oxidative mechanisms in nigral cell death in Parkinson's disease [In Process Citation]. Mov. Disord. 13:(Suppl. 1):1998;24-34.
    • (1998) Mov. Disord. , vol.13 , Issue.SUPPL. 1 , pp. 24-34
    • Jenner, P.1
  • 12
    • 0031200869 scopus 로고    scopus 로고
    • Free radicals and the pathobiology of brain dopamine systems
    • Cadet J.L., Brannock C. Free radicals and the pathobiology of brain dopamine systems. Neurochem. Int. 32:1998;117-131.
    • (1998) Neurochem. Int. , vol.32 , pp. 117-131
    • Cadet, J.L.1    Brannock, C.2
  • 13
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate, and neurodegenerative disorders
    • Coyle J.T., Puttfarcken P. Oxidative stress, glutamate, and neurodegenerative disorders. Science. 262:1993;689-695.
    • (1993) Science , vol.262 , pp. 689-695
    • Coyle, J.T.1    Puttfarcken, P.2
  • 14
    • 0025438029 scopus 로고
    • Methods for antagonizing glutamate neurotoxicity
    • Choi D.W. Methods for antagonizing glutamate neurotoxicity. Cerebrovasc. Brain Metab. Rev. 2:1990;105-147.
    • (1990) Cerebrovasc. Brain Metab. Rev. , vol.2 , pp. 105-147
    • Choi, D.W.1
  • 15
    • 0032526940 scopus 로고    scopus 로고
    • The regulation of reactive oxygen species production during programmed cell death
    • Tan S., Sagara Y., Liu Y., Maher P., Schubert D. The regulation of reactive oxygen species production during programmed cell death. J. Cell Biol. 141:1998;1423-1432.
    • (1998) J. Cell Biol. , vol.141 , pp. 1423-1432
    • Tan, S.1    Sagara, Y.2    Liu, Y.3    Maher, P.4    Schubert, D.5
  • 16
    • 0025355933 scopus 로고
    • Immature cortical neurons are uniquely sensitive to glutamate toxicity by inhibition of cystine uptake
    • Murphy T.H., Schnaar R.L., Coyle J.T. Immature cortical neurons are uniquely sensitive to glutamate toxicity by inhibition of cystine uptake. FASEB J. 4:1990;1624-1633.
    • (1990) FASEB J. , vol.4 , pp. 1624-1633
    • Murphy, T.H.1    Schnaar, R.L.2    Coyle, J.T.3
  • 17
    • 0030707678 scopus 로고    scopus 로고
    • Protection against glutamate-induced cytotoxicity in C6 glial cells by thiol antioxidants
    • Han D., Sen C.K., Roy S., Kobayashi M.S., Tritschler H.J., Packer L. Protection against glutamate-induced cytotoxicity in C6 glial cells by thiol antioxidants. Am. J. Physiol. 273:1997;R1771-R1778.
    • (1997) Am. J. Physiol. , vol.273
    • Han, D.1    Sen, C.K.2    Roy, S.3    Kobayashi, M.S.4    Tritschler, H.J.5    Packer, L.6
  • 18
    • 0026637624 scopus 로고
    • A mechanism for glutamate toxicity in the C6 glioma cells involving inhibition of cystine uptake leading to glutathione depletion
    • Kato S., Negishi K., Mawatari K., Kuo C.H. A mechanism for glutamate toxicity in the C6 glioma cells involving inhibition of cystine uptake leading to glutathione depletion. Neuroscience. 48:1992;903-914.
    • (1992) Neuroscience , vol.48 , pp. 903-914
    • Kato, S.1    Negishi, K.2    Mawatari, K.3    Kuo, C.H.4
  • 19
    • 0030927533 scopus 로고    scopus 로고
    • Role of glutathione metabolism in the glutamate-induced programmed cell death of neuronal-like PC12 cells
    • Froissard P., Monrocq H., Duval D. Role of glutathione metabolism in the glutamate-induced programmed cell death of neuronal-like PC12 cells. Eur. J. Pharmacol. 326:1997;93-99.
    • (1997) Eur. J. Pharmacol. , vol.326 , pp. 93-99
    • Froissard, P.1    Monrocq, H.2    Duval, D.3
  • 20
    • 0030757990 scopus 로고    scopus 로고
    • Glutamate toxicity on a PC12 cell line involves glutathione (GSH) depletion and oxidative stress
    • Pereira C.M., Oliveira C.R. Glutamate toxicity on a PC12 cell line involves glutathione (GSH) depletion and oxidative stress. Free Radic. Biol. Med. 23:1997;637-647.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 637-647
    • Pereira, C.M.1    Oliveira, C.R.2
  • 21
    • 0027468201 scopus 로고
    • Vulnerability of oligodendroglia to glutamate: Pharmacology, mechanisms, and prevention
    • Oka A., Belliveau M.J., Rosenberg P.A., Volpe J.J. Vulnerability of oligodendroglia to glutamate pharmacology, mechanisms, and prevention . J. Neurosci. 13:1993;1441-1453.
    • (1993) J. Neurosci. , vol.13 , pp. 1441-1453
    • Oka, A.1    Belliveau, M.J.2    Rosenberg, P.A.3    Volpe, J.J.4
  • 22
    • 0024446419 scopus 로고
    • Antioxidants protect against glutamate-induced cytotoxicity in a neuronal cell line
    • Miyamoto M., Murphy T.H., Schnaar R.L., Coyle J.T. Antioxidants protect against glutamate-induced cytotoxicity in a neuronal cell line. J. Pharmacol. Exp. Ther. 250:1989;1132-1140.
    • (1989) J. Pharmacol. Exp. Ther. , vol.250 , pp. 1132-1140
    • Miyamoto, M.1    Murphy, T.H.2    Schnaar, R.L.3    Coyle, J.T.4
  • 23
    • 0024678458 scopus 로고
    • Glutamate toxicity in a neuronal cell line involves inhibition of cystine transport leading to oxidative stress
    • Murphy T.H., Miyamoto M., Sastre A., Schnaar R.L., Coyle J.T. Glutamate toxicity in a neuronal cell line involves inhibition of cystine transport leading to oxidative stress. Neuron. 2:1989;1547-1558.
    • (1989) Neuron. , vol.2 , pp. 1547-1558
    • Murphy, T.H.1    Miyamoto, M.2    Sastre, A.3    Schnaar, R.L.4    Coyle, J.T.5
  • 24
    • 17444447322 scopus 로고    scopus 로고
    • A positively charged a-lipoic acid analogue with increased cellular uptake and more potent immunomodulatory activity
    • Sen C.K., Tirosh O., Roy S., Kobayashi M., Packer L. A positively charged a-lipoic acid analogue with increased cellular uptake and more potent immunomodulatory activity. Biochem. Biophys. Res. Commun. 247:1998;223-228.
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 223-228
    • Sen, C.K.1    Tirosh, O.2    Roy, S.3    Kobayashi, M.4    Packer, L.5
  • 25
    • 0025363372 scopus 로고
    • Excitatory amino acid uptake and N-methyl-D-aspartate-mediated secretion in a neural cell line
    • Morimoto B.H., Koshland D.E. Jr. Excitatory amino acid uptake and N-methyl-D-aspartate-mediated secretion in a neural cell line. Proc. Natl. Acad. Sci. USA. 87:1990;3518-3521.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3518-3521
    • Morimoto, B.H.1    Koshland D.E., Jr.2
  • 26
    • 0026644178 scopus 로고
    • Growth factors and vitamin E modify neuronal glutamate toxicity
    • Schubert D., Kimura H., Maher P. Growth factors and vitamin E modify neuronal glutamate toxicity. Proc. Natl. Acad. Sci. USA. 89:1992;8264-8267.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8264-8267
    • Schubert, D.1    Kimura, H.2    Maher, P.3
  • 27
    • 0031026392 scopus 로고    scopus 로고
    • Cytosolic and mitochondrial systems for NADH-and NADPH-dependent reduction of alpha-lipoic acid
    • Haramaki N., Han D., Handelman G.J., Tritschler H.J., Packer L. Cytosolic and mitochondrial systems for NADH-and NADPH-dependent reduction of alpha-lipoic acid. Free Radic. Biol. Med. 22:1997;535-542.
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 535-542
    • Haramaki, N.1    Han, D.2    Handelman, G.J.3    Tritschler, H.J.4    Packer, L.5
  • 30
    • 0030690287 scopus 로고    scopus 로고
    • Evidence for a functional relevance of the selenocysteine residue in mammalian thioredoxin reductase
    • Marcocci L., Flohe L., Packer L. Evidence for a functional relevance of the selenocysteine residue in mammalian thioredoxin reductase. Biofactors. 6:1997;351-358.
    • (1997) Biofactors , vol.6 , pp. 351-358
    • Marcocci, L.1    Flohe, L.2    Packer, L.3


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