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Volumn 26, Issue 11-12, 1999, Pages 1369-1374

Blocking NMDA receptors prevents the oxidative stress induced by acute ammonia intoxication

Author keywords

Ammonia toxicity; Free radicals; Glutamate receptors; Glutathione; Hepatic encephalopathy; Hyperammonemia; Neurotoxicity; Nitric oxide; NMDA receptor

Indexed keywords

AMMONIA; DIZOCILPINE; FREE RADICAL; GLUTAMATE RECEPTOR; GLUTATHIONE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR BLOCKING AGENT; SUPEROXIDE;

EID: 0032967196     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(98)00339-6     Document Type: Article
Times cited : (147)

References (39)
  • 3
    • 0015787774 scopus 로고
    • The acute action of ammonia on rat brain metabolism in vivo
    • Hawkins R.A., Miller A.L., Nielsen R.C., Veech R.L. The acute action of ammonia on rat brain metabolism in vivo. Biochem. J. 134:1973;1001-1008.
    • (1973) Biochem. J. , vol.134 , pp. 1001-1008
    • Hawkins, R.A.1    Miller, A.L.2    Nielsen, R.C.3    Veech, R.L.4
  • 4
    • 0017362424 scopus 로고
    • Effect of acute ammonia intoxication on cerebral metabolism in rats with portacaval shunts
    • Hindfelt B., Plum F., Duffy T.E. Effect of acute ammonia intoxication on cerebral metabolism in rats with portacaval shunts. J. Clin. Invest. 59:1977;386-396.
    • (1977) J. Clin. Invest. , vol.59 , pp. 386-396
    • Hindfelt, B.1    Plum, F.2    Duffy, T.E.3
  • 5
    • 0027500453 scopus 로고
    • Chronic hyperammonemia prevents changes in brain energy and ammonia metabolites induced by acute ammonia intoxication
    • Kosenko E., Kaminsky Y., Felipo V., Miñana M.D., Grisolía S. Chronic hyperammonemia prevents changes in brain energy and ammonia metabolites induced by acute ammonia intoxication. Biochim. Biophys. Acta. 1180:1993;321-326.
    • (1993) Biochim. Biophys. Acta , vol.1180 , pp. 321-326
    • Kosenko, E.1    Kaminsky, Y.2    Felipo, V.3    Miñana, M.D.4    Grisolía, S.5
  • 10
    • 0023137252 scopus 로고
    • Ionic dependence of glutamate neurotoxicity
    • Choi D.W. Ionic dependence of glutamate neurotoxicity. J. Neurosci. 7:1987;369-379.
    • (1987) J. Neurosci. , vol.7 , pp. 369-379
    • Choi, D.W.1
  • 11
    • 0023895734 scopus 로고
    • Glutamate becomes neurotoxic via the N-methyl-D-aspartate receptor when intracellular energy levels are reduced
    • Novelli A., Reilly J.A., Lysko P.G., Henneberry R.C. Glutamate becomes neurotoxic via the N-methyl-D-aspartate receptor when intracellular energy levels are reduced. Brain Res. 451:1988;205-212.
    • (1988) Brain Res. , vol.451 , pp. 205-212
    • Novelli, A.1    Reilly, J.A.2    Lysko, P.G.3    Henneberry, R.C.4
  • 12
    • 0030434484 scopus 로고    scopus 로고
    • Carnitine and choline derivatives containing a trimethylamine group prevent ammonia toxicity in mice and glutamate toxicity in primary cultures of neurons
    • Miñana M.D., Hermenegildo C., Llansola M., Montoliu C., Grisolía S., Felipo V. Carnitine and choline derivatives containing a trimethylamine group prevent ammonia toxicity in mice and glutamate toxicity in primary cultures of neurons. J. Pharmacol. Exp. Ther. 279:1996;194-199.
    • (1996) J. Pharmacol. Exp. Ther. , vol.279 , pp. 194-199
    • Miñana, M.D.1    Hermenegildo, C.2    Llansola, M.3    Montoliu, C.4    Grisolía, S.5    Felipo, V.6
  • 13
    • 0028894969 scopus 로고
    • Lack of correlation between glutamate-induced depletion of ATP and neuronal death in primary cultures of cerebellum
    • Marcaida G., Miñana M.D., Grisolía S., Felipo V. Lack of correlation between glutamate-induced depletion of ATP and neuronal death in primary cultures of cerebellum. Brain Res. 695:1995;146-150.
    • (1995) Brain Res. , vol.695 , pp. 146-150
    • Marcaida, G.1    Miñana, M.D.2    Grisolía, S.3    Felipo, V.4
  • 15
    • 0030901009 scopus 로고    scopus 로고
    • Effects of acute hyperammonemia in vivo on oxidative metabolism in nonsynaptic rat brain mitochondria
    • Kosenko E., Felipo V., Miñana M.D., Grisolia S., Kaminsky Y. Effects of acute hyperammonemia in vivo on oxidative metabolism in nonsynaptic rat brain mitochondria. Metab. Brain Dis. 12:1997;69-82.
    • (1997) Metab. Brain Dis. , vol.12 , pp. 69-82
    • Kosenko, E.1    Felipo, V.2    Miñana, M.D.3    Grisolia, S.4    Kaminsky, Y.5
  • 16
    • 0030065474 scopus 로고    scopus 로고
    • Free radicals and neuronal cell death
    • Dawson V.L., Dawson T.M. Free radicals and neuronal cell death. Cell Death Differ. 3:1996;71-78.
    • (1996) Cell Death Differ. , vol.3 , pp. 71-78
    • Dawson, V.L.1    Dawson, T.M.2
  • 18
    • 0027221998 scopus 로고
    • NMDA-dependent superoxide production and neurotoxicity
    • Lafon-Cazal M., Pietri S., Culcasi M., Bockaert J. NMDA-dependent superoxide production and neurotoxicity. Nature. 364:1993;535-537.
    • (1993) Nature , vol.364 , pp. 535-537
    • Lafon-Cazal, M.1    Pietri, S.2    Culcasi, M.3    Bockaert, J.4
  • 19
    • 0030008052 scopus 로고    scopus 로고
    • Superoxide production in rat hippocampal neurons: Selective imaging with hydroethidine
    • Bindokas V.P., Jordán J., Lee C.C., Miller R.J. Superoxide production in rat hippocampal neurons selective imaging with hydroethidine . J. Neurosci. 15:1996;1324-1336.
    • (1996) J. Neurosci. , vol.15 , pp. 1324-1336
    • Bindokas, V.P.1    Jordán, J.2    Lee, C.C.3    Miller, R.J.4
  • 21
    • 0001528839 scopus 로고
    • Glutathione reductase
    • Bergmeyer H.U. New York: Wiley
    • Golderg D.M., Spooner R.J. Glutathione reductase. Bergmeyer H.U. Methods of enzymatic analysis. Vol. 3:1984;259-265 Wiley, New York.
    • (1984) Methods of Enzymatic Analysis , vol.3 , pp. 259-265
    • Golderg, D.M.1    Spooner, R.J.2
  • 22
    • 0017067418 scopus 로고
    • Glutathione peroxidase activity in selenium-deficient rat liver
    • Lawrence R.A., Burk R.F. Glutathione peroxidase activity in selenium-deficient rat liver. Biochem. Biophys. Res. Commun. 71:1976;952-958.
    • (1976) Biochem. Biophys. Res. Commun. , vol.71 , pp. 952-958
    • Lawrence, R.A.1    Burk, R.F.2
  • 23
    • 0000024078 scopus 로고
    • Catalase
    • Bergmeyer H.U. New York: Wiley
    • Aebi H.E. Catalase. Bergmeyer H.U. Methods of enzymatic analysis. Vol. 3:1984;273-286 Wiley, New York.
    • (1984) Methods of Enzymatic Analysis , vol.3 , pp. 273-286
    • Aebi, H.E.1
  • 24
    • 0014756187 scopus 로고
    • Measurement of catalase activity in tissue extracts
    • Cohen G., Dembiec D., Marcus J. Measurement of catalase activity in tissue extracts. Anal. Biochem. 34:1970;30-38.
    • (1970) Anal. Biochem. , vol.34 , pp. 30-38
    • Cohen, G.1    Dembiec, D.2    Marcus, J.3
  • 25
    • 0015153416 scopus 로고
    • Improved assays and an assay applicable to acrylamide gels
    • Beauchamp C., Fridovich I. Improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44:1971;276-287.
    • (1971) Anal. Biochem. , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 26
    • 0001422064 scopus 로고
    • Glucose-6-phosphate dehydrogenase
    • Bergmeyer H.U. Weinheim: Verlag Chemie
    • Deutsch J. Glucose-6-phosphate dehydrogenase. Bergmeyer H.U. Methods of enzymatic analysis. Vol. 3:1983;190-196 Verlag Chemie, Weinheim.
    • (1983) Methods of Enzymatic Analysis , vol.3 , pp. 190-196
    • Deutsch, J.1
  • 27
    • 0017293045 scopus 로고
    • Dihidroorotate-dependent superoxide production in rat brain and liver. A function of the primary dehydrogenase
    • Forman H.J., Kennedy J. Dihidroorotate-dependent superoxide production in rat brain and liver. A function of the primary dehydrogenase. Arch. Biochem. Biophys. 173:1976;219-224.
    • (1976) Arch. Biochem. Biophys. , vol.173 , pp. 219-224
    • Forman, H.J.1    Kennedy, J.2
  • 28
    • 0018384650 scopus 로고
    • Assay of lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa H., Ohishi N., Yagi K. Assay of lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal. Biochem. 95:1979;351-358.
    • (1979) Anal. Biochem. , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 29
    • 0022272493 scopus 로고
    • Determination of glutathione and glutathione disulfide in biological samples
    • Anderson M. Determination of glutathione and glutathione disulfide in biological samples. Methods Enzymol. 113:1985;548-552.
    • (1985) Methods Enzymol. , vol.113 , pp. 548-552
    • Anderson, M.1
  • 30
    • 0015848173 scopus 로고
    • Superoxide dismutase. Organelle specificity
    • Weisiger R.A., Fridovich I. Superoxide dismutase. Organelle specificity. J. Biol. Chem. 248:1973;3582-3592.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3582-3592
    • Weisiger, R.A.1    Fridovich, I.2
  • 31
    • 0032146210 scopus 로고    scopus 로고
    • Differential expression of superoxide dismutase isoforms in neuronal and glial compartments in the course of excitotoxicity mediated neurodegeneration: Relation to oxidative and nitrergic stress
    • Noack H., Lindenau J., Rothe F., Asayama K., Wolf G. Differential expression of superoxide dismutase isoforms in neuronal and glial compartments in the course of excitotoxicity mediated neurodegeneration relation to oxidative and nitrergic stress . Glia. 23:1998;285-297.
    • (1998) Glia , vol.23 , pp. 285-297
    • Noack, H.1    Lindenau, J.2    Rothe, F.3    Asayama, K.4    Wolf, G.5
  • 33
    • 0029918676 scopus 로고    scopus 로고
    • The chemistry and tumoricidal activity of nitric oxide/hydrogen peroxide and the implications to cell resistance/susceptibility
    • Farias-Eisner R., Chaudhuri G., Aeberhard E., Fukuto J.M. The chemistry and tumoricidal activity of nitric oxide/hydrogen peroxide and the implications to cell resistance/susceptibility. J. Biol. Chem. 271:1996;6144-6151.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6144-6151
    • Farias-Eisner, R.1    Chaudhuri, G.2    Aeberhard, E.3    Fukuto, J.M.4
  • 34
    • 0029132167 scopus 로고
    • Reversible binding and inhibition of catalase by nitric oxide
    • Brown G.C. Reversible binding and inhibition of catalase by nitric oxide. Eur. J. Biochem. 232:1995;188-191.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 188-191
    • Brown, G.C.1
  • 36
    • 0028145462 scopus 로고
    • Nitric oxide-mediated inhibition of the mitochondrial respiratory chain in cultured astrocytes
    • Bolaños J.P., Peuchen S., Heales S.J., Land J.M., Clark J.B. Nitric oxide-mediated inhibition of the mitochondrial respiratory chain in cultured astrocytes. J. Neurochem. 63:1994;910-916.
    • (1994) J. Neurochem. , vol.63 , pp. 910-916
    • Bolaños, J.P.1    Peuchen, S.2    Heales, S.J.3    Land, J.M.4    Clark, J.B.5
  • 37
    • 0029789043 scopus 로고    scopus 로고
    • NO-induced oxidative stress and glutathione metabolism in rodent and human cells
    • Luperchio S., Tamir S., Tannembaum S.R. NO-induced oxidative stress and glutathione metabolism in rodent and human cells. Free Radic. Biol. Med. 21:1996;513-519.
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 513-519
    • Luperchio, S.1    Tamir, S.2    Tannembaum, S.R.3
  • 38
    • 0031949404 scopus 로고    scopus 로고
    • Nitroarginine, an inhibitor of nitric oxide synthase, prevents changes in superoxide radical and antioxidant enzymes induced by ammonia intoxication
    • Kosenko E., Kaminsky Y., Lopata O., Muravyov N., Kaminsky A., Hermenegildo C., Felipo V. Nitroarginine, an inhibitor of nitric oxide synthase, prevents changes in superoxide radical and antioxidant enzymes induced by ammonia intoxication. Metab. Brain. Dis. 13:1998;29-41.
    • (1998) Metab. Brain. Dis. , vol.13 , pp. 29-41
    • Kosenko, E.1    Kaminsky, Y.2    Lopata, O.3    Muravyov, N.4    Kaminsky, A.5    Hermenegildo, C.6    Felipo, V.7
  • 39
    • 0029023214 scopus 로고
    • N-arginine, an inhibitor of nitric oxide synthase, attenuates ammonia toxicity and ammonia-induced alterations in brain metabolism
    • Kosenko, E.; Kaminsky, Y.; Grau, E.; Miñana, M. D.; Grisolía, S.; Felipo, V. N-arginine, an inhibitor of nitric oxide synthase, attenuates ammonia toxicity and ammonia-induced alterations in brain metabolism. Neurochem. Res. 20:451-456; 1995.
    • (1995) Neurochem. Res. , vol.20 , pp. 451-456
    • Kosenko, E.1    Kaminsky, Y.2    Grau, E.3    Miñana, M.D.4    Grisolía, S.5    Felipo, V.6


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