메뉴 건너뛰기




Volumn 35, Issue 1, 1999, Pages 11-17

Increased expression of glyceraldehyde-3-phosphate dehydrogenase in cultured astrocytes following exposure to manganese

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM; CYTOCHROME C OXIDASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LACTIC ACID; MAGNESIUM; MANGANESE; ZINC;

EID: 0032973293     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0197-0186(99)00024-8     Document Type: Article
Times cited : (39)

References (55)
  • 1
    • 0023261328 scopus 로고
    • Manganese poisoning and the attack of trivalent manganese upon catecholamines
    • Archibald F.S., Tyree C. Manganese poisoning and the attack of trivalent manganese upon catecholamines. Arch. Biochem. Biophys. 256:1987;638-650.
    • (1987) Arch. Biochem. Biophys. , vol.256 , pp. 638-650
    • Archibald, F.S.1    Tyree, C.2
  • 2
    • 0026536560 scopus 로고
    • Manganese uptake and efflux in cultured rat astrocytes
    • Aschner M., Gannon M., Kimelberg H.K. Manganese uptake and efflux in cultured rat astrocytes. J. Neurochem. 58:1992;730-735.
    • (1992) J. Neurochem. , vol.58 , pp. 730-735
    • Aschner, M.1    Gannon, M.2    Kimelberg, H.K.3
  • 3
    • 0021220995 scopus 로고
    • Manganese and extrapyramidal disorders
    • Barbeau A. Manganese and extrapyramidal disorders. Neurotoxicology. 5:1984;13-36.
    • (1984) Neurotoxicology , vol.5 , pp. 13-36
    • Barbeau, A.1
  • 4
    • 0017067402 scopus 로고
    • Interaction of anions and manganese with PEP carboxykinase
    • Bentle L.A., Lardy H.A. Interaction of anions and manganese with PEP carboxykinase. J. Biol. Chem. 251:1976;2916-2921.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2916-2921
    • Bentle, L.A.1    Lardy, H.A.2
  • 5
    • 0029587417 scopus 로고
    • Stimulation of glyceraldehyde-3-phosphate dehydrogenase mRNA levels by endogenous nitric oxide in cytokine-activated endothelium
    • Bereta J., Bereta M. Stimulation of glyceraldehyde-3-phosphate dehydrogenase mRNA levels by endogenous nitric oxide in cytokine-activated endothelium. Biochem. Biophys. Res. Comm. 217:1995;363-369.
    • (1995) Biochem. Biophys. Res. Comm. , vol.217 , pp. 363-369
    • Bereta, J.1    Bereta, M.2
  • 6
    • 0028125811 scopus 로고
    • Comparison of glyceraldehyde-3-phosphate dehydrogenase and 28 S-ribosomal RNA gene expression as RNA loading controls for northern blot analysis of cell lines of varying malignant potential
    • Bhatia P., Taylor W.R., Greenberg A.H., Wright J.A. Comparison of glyceraldehyde-3-phosphate dehydrogenase and 28 S-ribosomal RNA gene expression as RNA loading controls for northern blot analysis of cell lines of varying malignant potential. Anal. Biochem. 216:1994;223-226.
    • (1994) Anal. Biochem. , vol.216 , pp. 223-226
    • Bhatia, P.1    Taylor, W.R.2    Greenberg, A.H.3    Wright, J.A.4
  • 7
    • 0015447985 scopus 로고
    • Growth and cultivation of dissociated neurons and glial cells from embryonic chick, rat, and human brain in flask cultures
    • Booher J., Sensenbrenner M. Growth and cultivation of dissociated neurons and glial cells from embryonic chick, rat, and human brain in flask cultures. Neurobiol. 2:1972;97-105.
    • (1972) Neurobiol. , vol.2 , pp. 97-105
    • Booher, J.1    Sensenbrenner, M.2
  • 8
    • 0027447043 scopus 로고
    • Manganese injection into rat striatum produces excitotoxic lesions by impairing energy metabolism
    • Brouillet E.P., Shinobu I., McGarvey U., Hochberg F., Beal M.F. Manganese injection into rat striatum produces excitotoxic lesions by impairing energy metabolism. Exp. Neurol. 120:1993;89-94.
    • (1993) Exp. Neurol. , vol.120 , pp. 89-94
    • Brouillet, E.P.1    Shinobu, I.2    McGarvey, U.3    Hochberg, F.4    Beal, M.F.5
  • 9
    • 0028948660 scopus 로고
    • Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases
    • Chagnon P., Bétard C., Robitaille Y., Cholette A., Gauvreau D. Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases. NeuroReport. 6:1995;711-715.
    • (1995) NeuroReport , vol.6 , pp. 711-715
    • Chagnon, P.1    Bétard, C.2    Robitaille, Y.3    Cholette, A.4    Gauvreau, D.5
  • 10
    • 0014267876 scopus 로고
    • Chronic manganese poisoning: Clearance of tissue manganese concentrations with persistence of the neurological picture
    • Cotzias G.C., Horiuchi M.S., Fuenzalida S., Mena I. Chronic manganese poisoning: clearance of tissue manganese concentrations with persistence of the neurological picture. Neurology. 18:1968;376-382.
    • (1968) Neurology , vol.18 , pp. 376-382
    • Cotzias, G.C.1    Horiuchi, M.S.2    Fuenzalida, S.3    Mena, I.4
  • 13
    • 0023589234 scopus 로고
    • The physiopathologic significance of manganese in brain: Its relation to schizophrenia and neurodegenerative disorders
    • Donaldson J. The physiopathologic significance of manganese in brain: its relation to schizophrenia and neurodegenerative disorders. Neurotoxicology. 8:1987;451-462.
    • (1987) Neurotoxicology , vol.8 , pp. 451-462
    • Donaldson, J.1
  • 15
    • 0028973338 scopus 로고
    • Vulnerability of mitochondrial complex I in PC12 cells exposed to manganese
    • Galvani P., Fumagalli P., Santagostino A. Vulnerability of mitochondrial complex I in PC12 cells exposed to manganese. Eur. J. Pharmacol. 293:1995;377-383.
    • (1995) Eur. J. Pharmacol. , vol.293 , pp. 377-383
    • Galvani, P.1    Fumagalli, P.2    Santagostino, A.3
  • 17
    • 0021196047 scopus 로고
    • Catecholamine toxicity: A proposal for the molecular pathogenesis of manganese neurotoxicity and Parkinson's disease
    • Graham D.G. Catecholamine toxicity: a proposal for the molecular pathogenesis of manganese neurotoxicity and Parkinson's disease. Neurotoxicology. 5:1984;83-96.
    • (1984) Neurotoxicology , vol.5 , pp. 83-96
    • Graham, D.G.1
  • 18
    • 0031912776 scopus 로고    scopus 로고
    • Hypoxic regulation of endothelial glyceraldehyde-3-phosphate dehydrogenase
    • Graven K.K., McDonald R.J., Farber H.W. Hypoxic regulation of endothelial glyceraldehyde-3-phosphate dehydrogenase. Amer. J. Physiol. 274:1998;C347-355.
    • (1998) Amer. J. Physiol. , vol.274 , pp. 347-355
    • Graven, K.K.1    McDonald, R.J.2    Farber, H.W.3
  • 19
    • 0021207254 scopus 로고
    • Manganese ions, oxidation reactions and the superoxide radical
    • Halliwell B. Manganese ions, oxidation reactions and the superoxide radical. Neurotoxicology. 5:1984;113-117.
    • (1984) Neurotoxicology , vol.5 , pp. 113-117
    • Halliwell, B.1
  • 20
    • 0030831158 scopus 로고    scopus 로고
    • Manganese decreases glutamate uptake in cultured astrocytes
    • Hazell A.S., Norenberg M.D. Manganese decreases glutamate uptake in cultured astrocytes. Neurochem. Res. 22:1997;1443-1447.
    • (1997) Neurochem. Res. , vol.22 , pp. 1443-1447
    • Hazell, A.S.1    Norenberg, M.D.2
  • 21
    • 0031976604 scopus 로고    scopus 로고
    • Ammonia and manganese increase arginine uptake in cultured astrocytes
    • Hazell A.S., Norenberg M.D. Ammonia and manganese increase arginine uptake in cultured astrocytes. Neurochem. Res. 23:1998;869-873.
    • (1998) Neurochem. Res. , vol.23 , pp. 869-873
    • Hazell, A.S.1    Norenberg, M.D.2
  • 23
    • 0022359757 scopus 로고
    • Bundling of microtubules by glyceraldehyde-3-phosphate dehydrogenase and its modulation by ATP
    • Huitorel P., Pantaloni D. Bundling of microtubules by glyceraldehyde-3-phosphate dehydrogenase and its modulation by ATP. Eur. J. Biochem. 150:1985;265-269.
    • (1985) Eur. J. Biochem. , vol.150 , pp. 265-269
    • Huitorel, P.1    Pantaloni, D.2
  • 24
    • 0030045251 scopus 로고    scopus 로고
    • Evidence that glyceraldehyde-3-phosphate dehydrogenase is involved in age-induced apoptosis in mature cerebellar neurons in culture
    • Ishitani R., Sunaga K., Hirano A., Saunders P., Katsube N., Chuang D.-M. Evidence that glyceraldehyde-3-phosphate dehydrogenase is involved in age-induced apoptosis in mature cerebellar neurons in culture. J. Neurochem. 66:1996;928-935.
    • (1996) J. Neurochem. , vol.66 , pp. 928-935
    • Ishitani, R.1    Sunaga, K.2    Hirano, A.3    Saunders, P.4    Katsube, N.5    Chuang, D.-M.6
  • 25
    • 0030022523 scopus 로고    scopus 로고
    • Oxidative stress increases glyceraldehyde-3-phosphate dehydrogenase mRNA levels in isolated rabbit aorta
    • Ito Y., Pagano P.J., Tornheim K., Brecher P., Cohen R.A. Oxidative stress increases glyceraldehyde-3-phosphate dehydrogenase mRNA levels in isolated rabbit aorta. Am. J. Physiol. 270:1996;H81-H87.
    • (1996) Am. J. Physiol. , vol.270
    • Ito, Y.1    Pagano, P.J.2    Tornheim, K.3    Brecher, P.4    Cohen, R.A.5
  • 26
    • 0022799313 scopus 로고
    • Manganese-deoxyribonucleic acid binding modes. Nuclear magnetic relaxation dispersion results
    • Kennedy S.D., Bryant R.G. Manganese-deoxyribonucleic acid binding modes. Nuclear magnetic relaxation dispersion results. Biophys. J. 50:1986;669-676.
    • (1986) Biophys. J. , vol.50 , pp. 669-676
    • Kennedy, S.D.1    Bryant, R.G.2
  • 27
    • 0030789808 scopus 로고    scopus 로고
    • Decreased glutamate transporter (GLT-1) expression in frontal cortex of rats with acute liver failure
    • Knecht K., Michalak A., Rose C., Rothstein J.D., Butterworth R.F. Decreased glutamate transporter (GLT-1) expression in frontal cortex of rats with acute liver failure. Neurosci. Lett. 229:1997;201-203.
    • (1997) Neurosci. Lett. , vol.229 , pp. 201-203
    • Knecht, K.1    Michalak, A.2    Rose, C.3    Rothstein, J.D.4    Butterworth, R.F.5
  • 28
    • 18144453930 scopus 로고    scopus 로고
    • Inhibition of glyceraldehyde-3-phosphate dehydrogenase in post-ischaemic myocardium
    • Knight R.J., Kofoed K.F., Schelbert H.R., Buxton D.B. Inhibition of glyceraldehyde-3-phosphate dehydrogenase in post-ischaemic myocardium. Cardiovasc. Res. 32:1996;1016-1023.
    • (1996) Cardiovasc. Res. , vol.32 , pp. 1016-1023
    • Knight, R.J.1    Kofoed, K.F.2    Schelbert, H.R.3    Buxton, D.B.4
  • 31
    • 0024788703 scopus 로고
    • Antigenic probes locate binding sites for the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase on the actin monomer in microfilaments
    • Méjean C., Pons F., Benyamin Y., Roustan C. Antigenic probes locate binding sites for the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase on the actin monomer in microfilaments. Biochem. J. 264:1989;671-677.
    • (1989) Biochem. J. , vol.264 , pp. 671-677
    • Méjean, C.1    Pons, F.2    Benyamin, Y.3    Roustan, C.4
  • 32
    • 0014051573 scopus 로고
    • Chronic manganese poisoning - clinical picture and manganese turnover
    • Mena I., Mario O., Fuenzalida S., Cotzias G.C. Chronic manganese poisoning - clinical picture and manganese turnover. Neurology. 17:1967;128-136.
    • (1967) Neurology , vol.17 , pp. 128-136
    • Mena, I.1    Mario, O.2    Fuenzalida, S.3    Cotzias, G.C.4
  • 34
    • 0022535636 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is a nonhistone protein and a possible activator of transcription in neurons
    • Morgenegg G., Winkler G.C., Hübscher U., Heizmann C.W., Mous J., Kuenzle C.C. Glyceraldehyde-3-phosphate dehydrogenase is a nonhistone protein and a possible activator of transcription in neurons. J. Neurochem. 47:1986;54-62.
    • (1986) J. Neurochem. , vol.47 , pp. 54-62
    • Morgenegg, G.1    Winkler, G.C.2    Hübscher, U.3    Heizmann, C.W.4    Mous, J.5    Kuenzle, C.C.6
  • 35
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase activity is reduced in Alzheimer's disease
    • Mutisya E.M., Bowling A.C., Beal M.F. Cortical cytochrome oxidase activity is reduced in Alzheimer's disease. J. Neurochem. 63:1994;2179-2184.
    • (1994) J. Neurochem. , vol.63 , pp. 2179-2184
    • Mutisya, E.M.1    Bowling, A.C.2    Beal, M.F.3
  • 36
    • 0028816615 scopus 로고
    • +-binding region (Rossman Fold)
    • +-binding region (Rossman Fold). J. Biol. Chem. 270:1995;2755-2763.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2755-2763
    • Nagy, E.1    Rigby, W.F.C.2
  • 37
    • 0000977706 scopus 로고
    • The astrocyte in liver disease
    • Norenberg M.D. The astrocyte in liver disease. Adv. Cell. Neurobiol. 2:1981;303-352.
    • (1981) Adv. Cell. Neurobiol. , vol.2 , pp. 303-352
    • Norenberg, M.D.1
  • 39
    • 0001501720 scopus 로고
    • Experimental manganese encephalopathy in monkeys. A preliminary report
    • Pentschew A., Ebner F.F., Kovatch R.M. Experimental manganese encephalopathy in monkeys. A preliminary report. J. Neuropathol. Exp. Neurol. 22:1963;488-499.
    • (1963) J. Neuropathol. Exp. Neurol. , vol.22 , pp. 488-499
    • Pentschew, A.1    Ebner, F.F.2    Kovatch, R.M.3
  • 40
    • 0027369531 scopus 로고
    • Glutamate uptake by astrocytes is inhibited by reactive oxygen intermediates but not by other macrophage-derived molecules including cytokines, leukotrienes or platelet-activating factor
    • Piani D., Frei K., Pfister H-W., Fontana A. Glutamate uptake by astrocytes is inhibited by reactive oxygen intermediates but not by other macrophage-derived molecules including cytokines, leukotrienes or platelet-activating factor. J. Neuroimmunol. 48:1993;99-104.
    • (1993) J. Neuroimmunol. , vol.48 , pp. 99-104
    • Piani, D.1    Frei, K.2    Pfister, H.-W.3    Fontana, A.4
  • 41
    • 0028927312 scopus 로고
    • Increased manganese concentrations in pallidum of cirrhotic patients
    • Pomier Layrargues G., Spahr L., Butterworth R.F. Increased manganese concentrations in pallidum of cirrhotic patients. Lancet. 345:1995;735.
    • (1995) Lancet , vol.345 , pp. 735
    • Pomier Layrargues, G.1    Spahr, L.2    Butterworth, R.F.3
  • 42
    • 0030809974 scopus 로고    scopus 로고
    • Subcellular distribution of glyceraldehyde-3-phosphate dehydrogenase in cerebellar granule cells undergoing cytosine arabinoside-induced apoptosis
    • Saunders P.A., Chalecka-Franaszek E., Chuang D-M. Subcellular distribution of glyceraldehyde-3-phosphate dehydrogenase in cerebellar granule cells undergoing cytosine arabinoside-induced apoptosis. J. Neurochem. 69:1997;1820-1828.
    • (1997) J. Neurochem. , vol.69 , pp. 1820-1828
    • Saunders, P.A.1    Chalecka-Franaszek, E.2    Chuang, D.-M.3
  • 43
    • 0031936125 scopus 로고    scopus 로고
    • Manganese augments nitric oxide synthesis in murine astrocytes: A new pathogenetic mechanism in manganism?
    • Spranger M., Schwab S., Desiderato S., Bonmann E., Krieger D., Fandrey J. Manganese augments nitric oxide synthesis in murine astrocytes: a new pathogenetic mechanism in manganism? Exp. Neurol. 149:1998;277-283.
    • (1998) Exp. Neurol. , vol.149 , pp. 277-283
    • Spranger, M.1    Schwab, S.2    Desiderato, S.3    Bonmann, E.4    Krieger, D.5    Fandrey, J.6
  • 45
    • 0027235477 scopus 로고
    • Free radical and lipid peroxidation in manganese-induced neuronal cell injury
    • Sun A.Y., Yang W.L., Kim H.D. Free radical and lipid peroxidation in manganese-induced neuronal cell injury. Ann. N. Y. Acad. Sci. 679:1993;358-363.
    • (1993) Ann. N. Y. Acad. Sci. , vol.679 , pp. 358-363
    • Sun, A.Y.1    Yang, W.L.2    Kim, H.D.3
  • 47
    • 0022423245 scopus 로고
    • Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: Genomic complexity and molecular evolution of the gene
    • Tso J.Y., Sun X-H., Kao T-H., Reece K.S., Wu R. Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene. Nucleic Acids Res. 13:1985;2485-2502.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 2485-2502
    • Tso, J.Y.1    Sun, X.-H.2    Kao, T.-H.3    Reece, K.S.4    Wu, R.5
  • 48
    • 0019379368 scopus 로고
    • Trace metals in human and animal health
    • Underwood E.J. Trace metals in human and animal health. J. Human Nutr. 35:1981;37-48.
    • (1981) J. Human Nutr. , vol.35 , pp. 37-48
    • Underwood, E.J.1
  • 49
    • 0028208495 scopus 로고
    • Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes
    • Volterra A., Trotti D., Tromba C., Floridi S., Racagni G. Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes. J. Neurosci. 14:1994;2924-2932.
    • (1994) J. Neurosci. , vol.14 , pp. 2924-2932
    • Volterra, A.1    Trotti, D.2    Tromba, C.3    Floridi, S.4    Racagni, G.5
  • 50
    • 0028945971 scopus 로고
    • Determination of the number and location of the manganese binding sites of DNA quadruplexes in solution by EPR and NMR
    • Wang K.Y., Gerena L., Swaminathan S., Bolton P.H. Determination of the number and location of the manganese binding sites of DNA quadruplexes in solution by EPR and NMR. Nucleic Acids. Res. 23:1995;844-848.
    • (1995) Nucleic Acids. Res. , vol.23 , pp. 844-848
    • Wang, K.Y.1    Gerena, L.2    Swaminathan, S.3    Bolton, P.H.4
  • 51
    • 0002527564 scopus 로고
    • Interactions of Mn(II) with mammalian glutamine synthetase
    • V.L. Schramm, & F.C. Wedler. New York: Academic Press
    • Wedler F.C., Toms R. Interactions of Mn(II) with mammalian glutamine synthetase. Schramm V.L., Wedler F.C. Manganese in Metabolism and Enzyme Function. 1986;221-238 Academic Press, New York.
    • (1986) Manganese in Metabolism and Enzyme Function , pp. 221-238
    • Wedler, F.C.1    Toms, R.2
  • 52
    • 0024785884 scopus 로고
    • Manganese(II) dynamics and distribution in glial cells cultured from chick cerebral cortex
    • Wedler F.C., Ley B.W., Grippo A.A. Manganese(II) dynamics and distribution in glial cells cultured from chick cerebral cortex. Neurochem. Res. 14:1989;1129-1135.
    • (1989) Neurochem. Res. , vol.14 , pp. 1129-1135
    • Wedler, F.C.1    Ley, B.W.2    Grippo, A.A.3
  • 54
    • 0022450141 scopus 로고
    • Chronic manganese poisoning: A neuropathological study with determination of manganese distribution in the brain
    • Yamada M., Ohno S., Okayasu I., Hatakeyama S., Watanabe H., Ushio K., Tsukagoshi H. Chronic manganese poisoning: A neuropathological study with determination of manganese distribution in the brain. Acta Neuropathol. 70:1986;273-278.
    • (1986) Acta Neuropathol. , vol.70 , pp. 273-278
    • Yamada, M.1    Ohno, S.2    Okayasu, I.3    Hatakeyama, S.4    Watanabe, H.5    Ushio, K.6    Tsukagoshi, H.7
  • 55
    • 0023944212 scopus 로고
    • A role for divalent cations in specifying the start site for transcription from chromatin templates in vitro
    • Zhang-Keck Z.Y., Eckstein F., Washington L.D., Stallcup M.R. A role for divalent cations in specifying the start site for transcription from chromatin templates in vitro. J. Biol.Chem. 263:1988;9550-9556.
    • (1988) J. Biol.Chem. , vol.263 , pp. 9550-9556
    • Zhang-Keck, Z.Y.1    Eckstein, F.2    Washington, L.D.3    Stallcup, M.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.