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Volumn 85, Issue 15, 2007, Pages 3471-3479

Stimulation of H2O2 generation by calcium in brain mitochondria respiring on α-glycerophosphate

Author keywords

glycerophosphate dehydrogenase; Membrane potential; NAD(P)H; Reverse electron transport; ROS; Succinate

Indexed keywords

CALCIUM; GLYCEROPHOSPHATE; HYDROGEN PEROXIDE; PROTEIN RET; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; ROTENONE; SUCCINIC SEMIALDEHYDE;

EID: 35848959911     PISSN: 03604012     EISSN: 10974547     Source Type: Journal    
DOI: 10.1002/jnr.21405     Document Type: Conference Paper
Times cited : (38)

References (65)
  • 1
    • 24144464489 scopus 로고    scopus 로고
    • Production of reactive oxygen species in brain mitochondria: Contribution by electron transport chain and non-electron transport chain Sources
    • Adam-Vizi V. 2005. Production of reactive oxygen species in brain mitochondria: contribution by electron transport chain and non-electron transport chain Sources. Antioxid Redox Signal 7:1140-1149.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 1140-1149
    • Adam-Vizi, V.1
  • 2
    • 33751072935 scopus 로고    scopus 로고
    • Bioenergetics and the formation of mitochondrial reactive oxygen species
    • Adam-Vizi V, Chinopoulos C. 2006. Bioenergetics and the formation of mitochondrial reactive oxygen species. Trends Pharmacol Sci 27:639-645.
    • (2006) Trends Pharmacol Sci , vol.27 , pp. 639-645
    • Adam-Vizi, V.1    Chinopoulos, C.2
  • 3
    • 0017201717 scopus 로고
    • Safranine as a probe of the mitochondrial membrane potential
    • Akerman KE, Wikstrom MK. 1976. Safranine as a probe of the mitochondrial membrane potential. FEBS Lett 68:191-197.
    • (1976) FEBS Lett , vol.68 , pp. 191-197
    • Akerman, K.E.1    Wikstrom, M.K.2
  • 4
    • 0032777013 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and hydrogen peroxide production in brain mitochondria after haloperidol treatment
    • Arnaiz SL, Coronel MF, Boveris A. 1999. Nitric oxide, superoxide, and hydrogen peroxide production in brain mitochondria after haloperidol treatment. Nitric Oxide 3:235-243.
    • (1999) Nitric Oxide , vol.3 , pp. 235-243
    • Arnaiz, S.L.1    Coronel, M.F.2    Boveris, A.3
  • 6
    • 0033042778 scopus 로고    scopus 로고
    • Glutamate neurotoxicity in rat cerebellar granule cells involves cytochrome c release from mitochondria and mitochondrial shuttle impairment
    • Atlante A, Gagliardi S, Marra E, Calissano P, Passarella S. 1999. Glutamate neurotoxicity in rat cerebellar granule cells involves cytochrome c release from mitochondria and mitochondrial shuttle impairment. J Neurochem 73:237-246.
    • (1999) J Neurochem , vol.73 , pp. 237-246
    • Atlante, A.1    Gagliardi, S.2    Marra, E.3    Calissano, P.4    Passarella, S.5
  • 7
    • 35848954596 scopus 로고
    • Succinate-linked acetoacetate reduction. I. Endergonic reduction of acetoacetate by succinate in liver mitochondria
    • Azzone GF, Ernster L, Weinbach EC. 1963. Succinate-linked acetoacetate reduction. I. Endergonic reduction of acetoacetate by succinate in liver mitochondria. J Biol Chem 238:1825-1833.
    • (1963) J Biol Chem , vol.238 , pp. 1825-1833
    • Azzone, G.F.1    Ernster, L.2    Weinbach, E.C.3
  • 8
    • 0031721246 scopus 로고    scopus 로고
    • Localization at complex I and mechanism of the higher free radical production of brain nonsynaptic mitochondria in the short-lived rat than in the longevous pigeon
    • Barja G, Herrero A. 1998. Localization at complex I and mechanism of the higher free radical production of brain nonsynaptic mitochondria in the short-lived rat than in the longevous pigeon. J Bioenerg Biomembr 30:235-243.
    • (1998) J Bioenerg Biomembr , vol.30 , pp. 235-243
    • Barja, G.1    Herrero, A.2
  • 9
    • 0037379314 scopus 로고    scopus 로고
    • Bioenergetic approaches for neuroprotection in Parkinson's disease
    • Beal MF. 2003. Bioenergetic approaches for neuroprotection in Parkinson's disease. Ann Neurol 53(Suppl):S39-S47.
    • (2003) Ann Neurol , vol.53 , Issue.SUPPL.
    • Beal, M.F.1
  • 10
    • 25444474703 scopus 로고    scopus 로고
    • Mitochondria take center stage in aging and neurodegeneration
    • Beal MF. 2005. Mitochondria take center stage in aging and neurodegeneration. Ann Neurol 58:495-505.
    • (2005) Ann Neurol , vol.58 , pp. 495-505
    • Beal, M.F.1
  • 11
    • 0023818906 scopus 로고
    • Ca2+ and Mg2+ as modulators of mitochondrial L-glycerol-3-phosphate dehydrogenase
    • Beleznai Z, Szalay L, Jancsik V. 1988. Ca2+ and Mg2+ as modulators of mitochondrial L-glycerol-3-phosphate dehydrogenase. Eur J Biochem 170:631-636.
    • (1988) Eur J Biochem , vol.170 , pp. 631-636
    • Beleznai, Z.1    Szalay, L.2    Jancsik, V.3
  • 12
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • Boveris A, Chance B. 1973. The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen. Biochem J 134:707-716.
    • (1973) Biochem J , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 14
    • 0016367481 scopus 로고
    • Control of sn-glycerol 3-phosphate oxidation in brown adipose tissue mitochondria by calcium and acyl-CoA
    • Bukowiecki LJ, Lindberg O. 1974. Control of sn-glycerol 3-phosphate oxidation in brown adipose tissue mitochondria by calcium and acyl-CoA. Biochim Biophys Acta 348:115-125.
    • (1974) Biochim Biophys Acta , vol.348 , pp. 115-125
    • Bukowiecki, L.J.1    Lindberg, O.2
  • 15
    • 0020046475 scopus 로고
    • Glycerol phosphate dehydrogenase, glucose-6-phosphate dehydrogenase, and lactate dehydrogenase: Activities in oligodendrocytes, neurons, astrocytes, and myelin isolated from developing rat brains
    • Cammer W, Snyder DS, Zimmerman TR Jr, Farooq M, Norton WT. 1982. Glycerol phosphate dehydrogenase, glucose-6-phosphate dehydrogenase, and lactate dehydrogenase: activities in oligodendrocytes, neurons, astrocytes, and myelin isolated from developing rat brains. J Neurochem 38:360-367.
    • (1982) J Neurochem , vol.38 , pp. 360-367
    • Cammer, W.1    Snyder, D.S.2    Zimmerman Jr, T.R.3    Farooq, M.4    Norton, W.T.5
  • 16
    • 21344442593 scopus 로고    scopus 로고
    • High activity of mitochondrial glycerophosphate dehydrogenase and glycerophosphate-dependent ROS production in prostate cancer cell lines
    • Chowdhury SK, Gemin A, Singh G. 2005. High activity of mitochondrial glycerophosphate dehydrogenase and glycerophosphate-dependent ROS production in prostate cancer cell lines. Biochem Biophys Res Commun 333:1139-1145.
    • (2005) Biochem Biophys Res Commun , vol.333 , pp. 1139-1145
    • Chowdhury, S.K.1    Gemin, A.2    Singh, G.3
  • 17
    • 33645290262 scopus 로고    scopus 로고
    • Mitochondria: A target for neuroprotective interventions in cerebral ischemia-reperfusion
    • Christophe M, Nicolas S. 2006. Mitochondria: a target for neuroprotective interventions in cerebral ischemia-reperfusion. Curr Pharm Des 12:739-757.
    • (2006) Curr Pharm Des , vol.12 , pp. 739-757
    • Christophe, M.1    Nicolas, S.2
  • 18
    • 17944386749 scopus 로고
    • Localization of the L-glycerol 1-phosphate-flavoprotein oxidoreductase on the outer surface of the inner membrane of insect flight-muscle mitochondria
    • 31P
    • Donnellan JF, Barker MD, Beechey RB. 1970. Localization of the L-glycerol 1-phosphate-flavoprotein oxidoreductase on the outer surface of the inner membrane of insect flight-muscle mitochondria. Biochem J 116:31P.
    • (1970) Biochem J , vol.116
    • Donnellan, J.F.1    Barker, M.D.2    Beechey, R.B.3
  • 19
    • 0036244950 scopus 로고    scopus 로고
    • Glycerophosphate-dependent hydrogen peroxide production by brown adipose tissue mitochondria and its activation by ferricyanide
    • Drahota Z, Chowdhury SK, Floryk D, Mracek T, Wilhelm J, Rauchova H, Lenaz G, Houstek J. 2002. Glycerophosphate-dependent hydrogen peroxide production by brown adipose tissue mitochondria and its activation by ferricyanide. J Bioenerg Biomembr 34:105-113.
    • (2002) J Bioenerg Biomembr , vol.34 , pp. 105-113
    • Drahota, Z.1    Chowdhury, S.K.2    Floryk, D.3    Mracek, T.4    Wilhelm, J.5    Rauchova, H.6    Lenaz, G.7    Houstek, J.8
  • 20
    • 0000274924 scopus 로고
    • alpha-Glycerophosphate oxidase of flight muscle mitochondria
    • Estabrook RW, Sacktor B. 1958. alpha-Glycerophosphate oxidase of flight muscle mitochondria. J Biol Chem 233:1014-1019.
    • (1958) J Biol Chem , vol.233 , pp. 1014-1019
    • Estabrook, R.W.1    Sacktor, B.2
  • 21
    • 0015937214 scopus 로고
    • Respiration of rat lung mitochondria and the influence of Ca 2+ on substrate utilization
    • Fisher AB, Scarpa A, LaNoue KF, Bassett D, Williamson JR. 1973. Respiration of rat lung mitochondria and the influence of Ca 2+ on substrate utilization. Biochemistry 12:1438-1445.
    • (1973) Biochemistry , vol.12 , pp. 1438-1445
    • Fisher, A.B.1    Scarpa, A.2    LaNoue, K.F.3    Bassett, D.4    Williamson, J.R.5
  • 22
    • 0035890197 scopus 로고    scopus 로고
    • Dynamics of intracellular calcium and free radical production during ischemia in pyramidal neurons
    • Frantseva MV, Carlen PL, Perez Velazquez JL. 2001. Dynamics of intracellular calcium and free radical production during ischemia in pyramidal neurons. Free Radic Biol Med 31:1216-1227.
    • (2001) Free Radic Biol Med , vol.31 , pp. 1216-1227
    • Frantseva, M.V.1    Carlen, P.L.2    Perez Velazquez, J.L.3
  • 23
    • 24944525045 scopus 로고    scopus 로고
    • Molecular pathogenesis of Parkinson's disease
    • Gandhi S, Wood NW. 2005. Molecular pathogenesis of Parkinson's disease. Hum Mol Genet 14 Spec No. 2:2749-2755.
    • (2005) Hum Mol Genet , vol.14 , Issue.SPEC 2 , pp. 2749-2755
    • Gandhi, S.1    Wood, N.W.2
  • 24
    • 0021895138 scopus 로고
    • A new generation of Ca2+ indicators with greatly improved fluorescence properties
    • Grynkiewicz G, Poenie M, Tsien RY. 1985. A new generation of Ca2+ indicators with greatly improved fluorescence properties. J Biol Chem 260:3440-3450.
    • (1985) J Biol Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 25
    • 3142777700 scopus 로고    scopus 로고
    • Shift in the localization of sites of hydrogen peroxide production in brain mitochondria by mitochondrial stress
    • Gyulkhandanyan AV, Pennefather PS. 2004. Shift in the localization of sites of hydrogen peroxide production in brain mitochondria by mitochondrial stress. J Neurochem 90:405-421.
    • (2004) J Neurochem , vol.90 , pp. 405-421
    • Gyulkhandanyan, A.V.1    Pennefather, P.S.2
  • 26
    • 0014214696 scopus 로고
    • The effect of Ca2+ on the oxidation of glycerol phosphate by blowfly flight-muscle mitochondria
    • Hansford RG, Chappell JB. 1967. The effect of Ca2+ on the oxidation of glycerol phosphate by blowfly flight-muscle mitochondria. Biochem Biophys Res Commun 27:686-692.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 686-692
    • Hansford, R.G.1    Chappell, J.B.2
  • 27
    • 0030615104 scopus 로고    scopus 로고
    • Dependence of H2O2 formation by rat heart mitochondria on substrate availability and donor age
    • Hansford RG, Hogue BA, Mildaziene V. 1997. Dependence of H2O2 formation by rat heart mitochondria on substrate availability and donor age. J Bioenerg Biomembr 29:89-95.
    • (1997) J Bioenerg Biomembr , vol.29 , pp. 89-95
    • Hansford, R.G.1    Hogue, B.A.2    Mildaziene, V.3
  • 28
    • 0014217470 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome beta region of the respiratory chain of beef heart submitochondrial particles
    • Hinkle PC, Butow RA, Racker E, Chance B. 1967. Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome beta region of the respiratory chain of beef heart submitochondrial particles. J Biol Chem 242:5169-5173.
    • (1967) J Biol Chem , vol.242 , pp. 5169-5173
    • Hinkle, P.C.1    Butow, R.A.2    Racker, E.3    Chance, B.4
  • 29
    • 0014764841 scopus 로고
    • Localization of the glycerol-phosphate dehydrogenase in the outer phase of the mitochondrial inner membrane
    • Klingenberg M. 1970. Localization of the glycerol-phosphate dehydrogenase in the outer phase of the mitochondrial inner membrane. Eur J Biochem 13:247-252.
    • (1970) Eur J Biochem , vol.13 , pp. 247-252
    • Klingenberg, M.1
  • 30
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov SS, Skulachev VP, Starkov AA. 1997. High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett 416:15-18.
    • (1997) FEBS Lett , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 31
    • 0033774468 scopus 로고    scopus 로고
    • Bcl-2 prevents mitochondrial permeability transition and cytochrome c release via maintenance of reduced pyridine nucleotides
    • Kowaltowski AJ, Vercesi AE, Fiskum G. 2000. Bcl-2 prevents mitochondrial permeability transition and cytochrome c release via maintenance of reduced pyridine nucleotides. Cell Death Differ 7:903-910.
    • (2000) Cell Death Differ , vol.7 , pp. 903-910
    • Kowaltowski, A.J.1    Vercesi, A.E.2    Fiskum, G.3
  • 32
    • 0031853099 scopus 로고    scopus 로고
    • Substrate and site specificity of hydrogen peroxide generation in mouse mitochondria
    • Kwong LK, Sohal RS. 1998. Substrate and site specificity of hydrogen peroxide generation in mouse mitochondria. Arch Biochem Biophys 350:118-126.
    • (1998) Arch Biochem Biophys , vol.350 , pp. 118-126
    • Kwong, L.K.1    Sohal, R.S.2
  • 33
    • 0036319021 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the mitochondrial electron transport chain
    • Liu Y, Fiskum G, Schubert D. 2002. Generation of reactive oxygen species by the mitochondrial electron transport chain. J Neurochem 80:780-787.
    • (2002) J Neurochem , vol.80 , pp. 780-787
    • Liu, Y.1    Fiskum, G.2    Schubert, D.3
  • 34
    • 0030926003 scopus 로고    scopus 로고
    • Mitochondrial activation directly triggers the exocytosis of insulin in permeabilized pancreatic beta-cells
    • Maechler P, Kennedy ED, Pozzan T, Wollheim CB. 1997. Mitochondrial activation directly triggers the exocytosis of insulin in permeabilized pancreatic beta-cells. EMBO J 16:3833-3841.
    • (1997) EMBO J , vol.16 , pp. 3833-3841
    • Maechler, P.1    Kennedy, E.D.2    Pozzan, T.3    Wollheim, C.B.4
  • 35
    • 0025879155 scopus 로고
    • Hexose metabolism in pancreatic islets. Regulation of aerobic glycolysis and pyruvate decarboxylation
    • Malaisse WJ, Rasschaert J, Conget I, Sener A. 1991. Hexose metabolism in pancreatic islets. Regulation of aerobic glycolysis and pyruvate decarboxylation. Int J Biochem 23:955-959.
    • (1991) Int J Biochem , vol.23 , pp. 955-959
    • Malaisse, W.J.1    Rasschaert, J.2    Conget, I.3    Sener, A.4
  • 36
    • 0028108347 scopus 로고
    • Activation of molecular oxygen by flavins and flavoproteins
    • Massey V. 1994. Activation of molecular oxygen by flavins and flavoproteins. J Biol Chem 269:22459-22462.
    • (1994) J Biol Chem , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 37
    • 0027727915 scopus 로고
    • Regulation of energy metabolism in synaptic terminals and cultured rat brain astrocytes: Differences revealed using aminooxyacetate
    • McKenna MC, Tildon JT, Stevenson JH, Boatright R, Huang S. 1993. Regulation of energy metabolism in synaptic terminals and cultured rat brain astrocytes: differences revealed using aminooxyacetate. Dev Neurosci 15:320-329.
    • (1993) Dev Neurosci , vol.15 , pp. 320-329
    • McKenna, M.C.1    Tildon, J.T.2    Stevenson, J.H.3    Boatright, R.4    Huang, S.5
  • 38
    • 30444437034 scopus 로고    scopus 로고
    • Neuronal and astrocytic shuttle mechanisms for cytosolic-mitochondrial transfer of reducing equivalents: Current evidence and pharmacological tools
    • McKenna MC, Waagepetersen HS, Schousboe A, Sonnewald U. 2006. Neuronal and astrocytic shuttle mechanisms for cytosolic-mitochondrial transfer of reducing equivalents: current evidence and pharmacological tools. Biochem Pharmacol 71:399-407.
    • (2006) Biochem Pharmacol , vol.71 , pp. 399-407
    • McKenna, M.C.1    Waagepetersen, H.S.2    Schousboe, A.3    Sonnewald, U.4
  • 39
    • 24344508510 scopus 로고    scopus 로고
    • The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophila mitochondria
    • Miwa S, Brand MD. 2005. The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophila mitochondria. Biochim Biophys Acta 1709:214-219.
    • (2005) Biochim Biophys Acta , vol.1709 , pp. 214-219
    • Miwa, S.1    Brand, M.D.2
  • 40
    • 0141526414 scopus 로고    scopus 로고
    • Superoxide and hydrogen peroxide production by Drosophila mitochondria
    • Miwa S, St Pierre J, Partridge L, Brand MD. 2003. Superoxide and hydrogen peroxide production by Drosophila mitochondria. Free Radic Biol Med 35:938-948.
    • (2003) Free Radic Biol Med , vol.35 , pp. 938-948
    • Miwa, S.1    St Pierre, J.2    Partridge, L.3    Brand, M.D.4
  • 41
    • 0031588923 scopus 로고    scopus 로고
    • A highly sensitive fluorescent micro-assay of H2O2 release from activated human leukocytes using a dihydroxyphenoxazine derivative
    • Mohanty JG, Jaffe JS, Schulman ES, Raible DG. 1997. A highly sensitive fluorescent micro-assay of H2O2 release from activated human leukocytes using a dihydroxyphenoxazine derivative. J Immunol Methods 202:133-141.
    • (1997) J Immunol Methods , vol.202 , pp. 133-141
    • Mohanty, J.G.1    Jaffe, J.S.2    Schulman, E.S.3    Raible, D.G.4
  • 42
    • 0018269944 scopus 로고
    • The regulation of extramitochondrial free calcium ion concentration by rat liver mitochondria
    • Nicholls DG. 1978. The regulation of extramitochondrial free calcium ion concentration by rat liver mitochondria. Biochem J 176:463-474.
    • (1978) Biochem J , vol.176 , pp. 463-474
    • Nicholls, D.G.1
  • 43
    • 0032504708 scopus 로고    scopus 로고
    • Mitochondria and neuronal glutamate excitotoxicity
    • Nicholls DG, Budd SL. 1998. Mitochondria and neuronal glutamate excitotoxicity. Biochim Biophys Acta 1366:97-112.
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 97-112
    • Nicholls, D.G.1    Budd, S.L.2
  • 44
    • 0031584809 scopus 로고    scopus 로고
    • Mutation in the calcium-binding domain of the mitochondrial glycerophosphate dehydrogenase gene in a family of diabetic subjects
    • Novials A, Vidal J, Franco C, Ribera F, Sener A, Malaisse WJ, Gomis R. 1997. Mutation in the calcium-binding domain of the mitochondrial glycerophosphate dehydrogenase gene in a family of diabetic subjects. Biochem Biophys Res Commun 231:570-572.
    • (1997) Biochem Biophys Res Commun , vol.231 , pp. 570-572
    • Novials, A.1    Vidal, J.2    Franco, C.3    Ribera, F.4    Sener, A.5    Malaisse, W.J.6    Gomis, R.7
  • 46
    • 27544484846 scopus 로고    scopus 로고
    • Are mitochondria critical in the pathogenesis of Alzheimer's disease?
    • Reddy PH, Beal MF. 2005. Are mitochondria critical in the pathogenesis of Alzheimer's disease? Brain Res Brain Res Rev 49:618-632.
    • (2005) Brain Res Brain Res Rev , vol.49 , pp. 618-632
    • Reddy, P.H.1    Beal, M.F.2
  • 47
    • 0026635622 scopus 로고
    • CHELATOR: An improved method for computing metal ion concentrations in physiological solutions
    • Schoenmakers TJ, Visser GJ, Flik G, Theuvenet AP. 1992. CHELATOR: an improved method for computing metal ion concentrations in physiological solutions. Biotechniques 12:870-879.
    • (1992) Biotechniques , vol.12 , pp. 870-879
    • Schoenmakers, T.J.1    Visser, G.J.2    Flik, G.3    Theuvenet, A.P.4
  • 49
    • 0025471534 scopus 로고
    • Rapid isolation of metabolically active mitochondria from rat-brain and subregions using Percoll density gradient centrifugation
    • Sims NR. 1990. Rapid isolation of metabolically active mitochondria from rat-brain and subregions using Percoll density gradient centrifugation. J Neurochem 55:698-707.
    • (1990) J Neurochem , vol.55 , pp. 698-707
    • Sims, N.R.1
  • 50
    • 33646085779 scopus 로고    scopus 로고
    • Protein-mediated energy-dissipating pathways in mitochondria
    • Starkov AA. 2006. Protein-mediated energy-dissipating pathways in mitochondria. Chem Biol Interact 161:57-68.
    • (2006) Chem Biol Interact , vol.161 , pp. 57-68
    • Starkov, A.A.1
  • 51
    • 3342910554 scopus 로고    scopus 로고
    • Mitochondrial calcium and oxidative stress as mediators of ischemic brain injury
    • Starkov AA, Chinopoulos C, Fiskum G. 2004a. Mitochondrial calcium and oxidative stress as mediators of ischemic brain injury. Cell Calcium 36:257-264.
    • (2004) Cell Calcium , vol.36 , pp. 257-264
    • Starkov, A.A.1    Chinopoulos, C.2    Fiskum, G.3
  • 52
    • 0034811384 scopus 로고    scopus 로고
    • Myxothiazol induces H(2)O(2) production from mitochondrial respiratory chain
    • Starkov AA, Fiskum G. 2001. Myxothiazol induces H(2)O(2) production from mitochondrial respiratory chain. Biochem Biophys Res Commun 281:645-650.
    • (2001) Biochem Biophys Res Commun , vol.281 , pp. 645-650
    • Starkov, A.A.1    Fiskum, G.2
  • 54
    • 0036788941 scopus 로고    scopus 로고
    • Regulation of hydrogen peroxide production by brain mitochondria by calcium and Bax 2
    • Starkov AA, Polster BM, Fiskum G. 2002. Regulation of hydrogen peroxide production by brain mitochondria by calcium and Bax 2. J Neurochem 83:220-228.
    • (2002) J Neurochem , vol.83 , pp. 220-228
    • Starkov, A.A.1    Polster, B.M.2    Fiskum, G.3
  • 56
    • 4544226082 scopus 로고    scopus 로고
    • Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase
    • Tretter L, Adam-Vizi V. 2004. Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase. J Neurosci 24:7771-7778.
    • (2004) J Neurosci , vol.24 , pp. 7771-7778
    • Tretter, L.1    Adam-Vizi, V.2
  • 57
    • 33745252231 scopus 로고    scopus 로고
    • Alpha-ketoglutarate dehydrogenase: A target and generator of oxidative stress
    • Tretter L, Adam-Vizi V. 2005. Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress. Philos Trans R Soc Lond B Biol Sci 360:2335-2345.
    • (2005) Philos Trans R Soc Lond B Biol Sci , vol.360 , pp. 2335-2345
    • Tretter, L.1    Adam-Vizi, V.2
  • 58
    • 33947592809 scopus 로고    scopus 로고
    • Moderate dependence of ROS formation on DeltaPsim in isolated brain mitochondria supported by NADH-linked substrates
    • Tretter L, Adam-Vizi V. 2006. Moderate dependence of ROS formation on DeltaPsim in isolated brain mitochondria supported by NADH-linked substrates. Neurochem Res 32:569-575.
    • (2006) Neurochem Res , vol.32 , pp. 569-575
    • Tretter, L.1    Adam-Vizi, V.2
  • 59
    • 33845451992 scopus 로고    scopus 로고
    • The effect of bovine serum albumin on the membrane potential and reactive oxygen species generation in succinate-supported isolated brain mitochondria 1
    • Tretter L, Mayer-Takacs D, Adam-Vizi V. 2007a. The effect of bovine serum albumin on the membrane potential and reactive oxygen species generation in succinate-supported isolated brain mitochondria 1. Neurochem Int 50:139-147.
    • (2007) Neurochem Int , vol.50 , pp. 139-147
    • Tretter, L.1    Mayer-Takacs, D.2    Adam-Vizi, V.3
  • 60
    • 0023097348 scopus 로고
    • Effect of succinate on mitochondrial lipid peroxidation. 2. The protective effect of succinate against functional and structural changes induced by lipid peroxidation
    • Tretter L, Szabados G, Ando A, Horvath I. 1987. Effect of succinate on mitochondrial lipid peroxidation. 2. The protective effect of succinate against functional and structural changes induced by lipid peroxidation. J Bioenerg Biomembr 19:31-44.
    • (1987) J Bioenerg Biomembr , vol.19 , pp. 31-44
    • Tretter, L.1    Szabados, G.2    Ando, A.3    Horvath, I.4
  • 61
    • 33846188870 scopus 로고    scopus 로고
    • Characteristics of alpha-glycerophosphate-evoked H(2)O(2) generation in brain mitochondria
    • Tretter L, Takacs K, Hegedus V, Adam-Vizi V. 2007b. Characteristics of alpha-glycerophosphate-evoked H(2)O(2) generation in brain mitochondria. J Neurochem 100:650-663.
    • (2007) J Neurochem , vol.100 , pp. 650-663
    • Tretter, L.1    Takacs, K.2    Hegedus, V.3    Adam-Vizi, V.4
  • 62
    • 0034740585 scopus 로고    scopus 로고
    • DeltaPsi(m)-Dependent and -independent production of reactive oxygen species by rat brain mitochondria
    • Votyakova TV, Reynolds IJ. 2001. DeltaPsi(m)-Dependent and -independent production of reactive oxygen species by rat brain mitochondria. J Neurochem 79:266-277.
    • (2001) J Neurochem , vol.79 , pp. 266-277
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 63
    • 0035577327 scopus 로고    scopus 로고
    • Elucidation of the quantitative significance of pyruvate carboxylation in cultured cerebellar neurons and astrocytes
    • Waagepetersen HS, Qu H, Schousboe A, Sonnewald U. 2001. Elucidation of the quantitative significance of pyruvate carboxylation in cultured cerebellar neurons and astrocytes. J Neurosci Res 66:763-770.
    • (2001) J Neurosci Res , vol.66 , pp. 763-770
    • Waagepetersen, H.S.1    Qu, H.2    Schousboe, A.3    Sonnewald, U.4
  • 64
    • 0019888718 scopus 로고
    • Ca2+ stimulation of rat liver mitochondrial glycerophosphate dehydrogenase
    • Wernette ME, Ochs RS, Lardy HA. 1981. Ca2+ stimulation of rat liver mitochondrial glycerophosphate dehydrogenase. J Biol Chem 256:12767-12771.
    • (1981) J Biol Chem , vol.256 , pp. 12767-12771
    • Wernette, M.E.1    Ochs, R.S.2    Lardy, H.A.3
  • 65
    • 0023811458 scopus 로고
    • Pathways of hydrogen peroxide generation in guinea pig cerebral cortex mitochondria 2
    • Zoccarato F, Cavallini L, Deana R, Alexandre A. 1988. Pathways of hydrogen peroxide generation in guinea pig cerebral cortex mitochondria 2. Biochem Biophys Res Commun 154:727-734.
    • (1988) Biochem Biophys Res Commun , vol.154 , pp. 727-734
    • Zoccarato, F.1    Cavallini, L.2    Deana, R.3    Alexandre, A.4


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