메뉴 건너뛰기




Volumn 1147, Issue , 2008, Pages 37-52

The role of mitochondria in reactive oxygen species metabolism and signaling

Author keywords

Hypoxia induced ROS increase; Malate; Nutraceutics; ROS sink; ROS sources; ROS targets; Succinate

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; CYTOCHROME C OXIDASE; ELECTRON TRANSFERRING FLAVOPROTEIN; GLUTAREDOXIN; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; MALIC ACID; MANGANESE SUPEROXIDE DISMUTASE; NUTRACEUTICAL; PEROXIREDOXIN; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SIGNAL PEPTIDE; SUCCINATE DEHYDROGENASE; SUCCINIC ACID; THIOREDOXIN 2; THIOREDOXIN REDUCTASE; UBIQUINONE;

EID: 57649233079     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1196/annals.1427.015     Document Type: Conference Paper
Times cited : (670)

References (88)
  • 1
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • &
    • Lin, M.T. & M.F. Beal. 2006. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443 : 787 795.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 2
    • 34548451974 scopus 로고    scopus 로고
    • Reactive oxygen species in mitochondria-mediated cell death
    • Orrenius, S. 2007. Reactive oxygen species in mitochondria-mediated cell death. Drug. Metab. Rev. 39 : 443 455.
    • (2007) Drug. Metab. Rev. , vol.39 , pp. 443-455
    • Orrenius, S.1
  • 3
    • 34249104544 scopus 로고    scopus 로고
    • Oxidative stress and aberrant signaling in aging and cognitive decline
    • &
    • Droge, W. & H.M. Schipper. 2007. Oxidative stress and aberrant signaling in aging and cognitive decline. Aging Cell 6 : 361 370.
    • (2007) Aging Cell , vol.6 , pp. 361-370
    • Droge, W.1    Schipper, H.M.2
  • 4
    • 34547830983 scopus 로고    scopus 로고
    • Diabetes associated cell stress and dysfunction: Role of mitochondrial and non-mitochondrial ROS production and activity
    • Newsholme, P. et al. 2007. Diabetes associated cell stress and dysfunction: role of mitochondrial and non-mitochondrial ROS production and activity. J. Physiol. 583 : 9 24.
    • (2007) J. Physiol. , vol.583 , pp. 9-24
    • Newsholme, P.1
  • 5
    • 33750616552 scopus 로고    scopus 로고
    • Mitochondrial dysfunction, persistently elevated levels of reactive oxygen species and radiation-induced genomic instability: A review
    • &
    • Kim, G.J., K. Chandrasekaran & W.F. Morgan. 2006. Mitochondrial dysfunction, persistently elevated levels of reactive oxygen species and radiation-induced genomic instability: a review. Mutagenesis 21 : 361 367.
    • (2006) Mutagenesis , vol.21 , pp. 361-367
    • Kim, G.J.1    Chandrasekaran, K.2    Morgan, W.F.3
  • 6
    • 33846522832 scopus 로고    scopus 로고
    • Oxidative stress as the leading cause of acute myocardial infarction in diabetics
    • Di Filippo, C. et al. 2006. Oxidative stress as the leading cause of acute myocardial infarction in diabetics. Cardiovasc. Drug. Rev. 24 : 77 87.
    • (2006) Cardiovasc. Drug. Rev. , vol.24 , pp. 77-87
    • Di Filippo, C.1
  • 7
    • 22944436150 scopus 로고    scopus 로고
    • Oxidative stress in allergic and inflammatory skin diseases
    • Okayama, Y. 2005. Oxidative stress in allergic and inflammatory skin diseases. Curr. Drug. Targets Inflamm. Allergy 4 : 517 519.
    • (2005) Curr. Drug. Targets Inflamm. Allergy , vol.4 , pp. 517-519
    • Okayama, Y.1
  • 8
    • 17244367828 scopus 로고    scopus 로고
    • Reactive oxygen species in tumor progression
    • Storz, P. 2005. Reactive oxygen species in tumor progression. Front. Biosci. 10 : 1881 1896.
    • (2005) Front. Biosci. , vol.10 , pp. 1881-1896
    • Storz, P.1
  • 9
    • 33749986298 scopus 로고    scopus 로고
    • Free radicals and antioxidants in normal physiological functions and human disease
    • Valko, M. et al. 2007. Free radicals and antioxidants in normal physiological functions and human disease. Int. J. Biochem. Cell Biol. 39 : 44 84.
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 44-84
    • Valko, M.1
  • 10
    • 14644442283 scopus 로고    scopus 로고
    • Oxygen, oxidative stress, hypoxia, and heart failure
    • Giordano, F.J. 2005. Oxygen, oxidative stress, hypoxia, and heart failure. J. Clin. Invest. 115 : 500 508.
    • (2005) J. Clin. Invest. , vol.115 , pp. 500-508
    • Giordano, F.J.1
  • 11
    • 2442440907 scopus 로고    scopus 로고
    • Role of reactive oxygen species in skin carcinogenesis
    • &
    • Nishigori, C., Y. Hattori & S. Toyokuni. 2004. Role of reactive oxygen species in skin carcinogenesis. Antioxid. Redox. Signal 6 : 561 570.
    • (2004) Antioxid. Redox. Signal , vol.6 , pp. 561-570
    • Nishigori, C.1    Hattori, Y.2    Toyokuni, S.3
  • 12
    • 0141761418 scopus 로고    scopus 로고
    • Contribution of reactive oxygen species to cartilage degradation in rheumatic diseases: Molecular pathways, diagnosis and potential therapeutic strategies
    • Schiller, J. et al. 2003. Contribution of reactive oxygen species to cartilage degradation in rheumatic diseases: molecular pathways, diagnosis and potential therapeutic strategies. Curr. Med. Chem. 10 : 2123 2145.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 2123-2145
    • Schiller, J.1
  • 13
    • 0037382663 scopus 로고    scopus 로고
    • Role of reactive oxygen species in the pathophysiology of human reproduction
    • &
    • Agarwal, A., R.A. Saleh & M.A. Bedaiwy. 2003. Role of reactive oxygen species in the pathophysiology of human reproduction. Fertil. Steril. 79 : 829 843.
    • (2003) Fertil. Steril. , vol.79 , pp. 829-843
    • Agarwal, A.1    Saleh, R.A.2    Bedaiwy, M.A.3
  • 14
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge, W. 2002. Free radicals in the physiological control of cell function. Physiol. Rev. 82 : 47 95.
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 15
    • 34548148201 scopus 로고    scopus 로고
    • Hydrogen peroxide: A metabolic by-product or a common mediator of ageing signals?
    • Giorgio, M. et al. 2007. Hydrogen peroxide: a metabolic by-product or a common mediator of ageing signals? Nat. Rev. Mol. Cell Biol. 8 : 722 728.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 722-728
    • Giorgio, M.1
  • 16
    • 35848932278 scopus 로고    scopus 로고
    • Signaling functions of free radicals superoxide & nitric oxide under physiological & pathological conditions
    • Afanas'ev, I.B. 2007. Signaling functions of free radicals superoxide & nitric oxide under physiological & pathological conditions. Mol. Biotechnol. 37 : 2 4.
    • (2007) Mol. Biotechnol. , vol.37 , pp. 2-4
    • Afanas'Ev, I.B.1
  • 17
    • 33749999563 scopus 로고    scopus 로고
    • Protein-mediated energy-dissipating pathways in mitochondria
    • Starkov, A.A. 2006. Protein-mediated energy-dissipating pathways in mitochondria. Chem. Biol. Interact. 163 : 133 144.
    • (2006) Chem. Biol. Interact. , vol.163 , pp. 133-144
    • Starkov, A.A.1
  • 19
    • 0032716145 scopus 로고    scopus 로고
    • The regeneration of reduced glutathione in rat forebrain mitochondria identifies metabolic pathways providing the NADPH required
    • Vogel, R. et al. 1999. The regeneration of reduced glutathione in rat forebrain mitochondria identifies metabolic pathways providing the NADPH required. Neurosci. Lett. 275 : 97 100.
    • (1999) Neurosci. Lett. , vol.275 , pp. 97-100
    • Vogel, R.1
  • 20
    • 0017332157 scopus 로고
    • Effect of ammonia on mitochondrial and cytosolic NADH and NADPH systems in isolated rat liver cells
    • &
    • Tischler, M.E., P. Hecht & J.R. Williamson. 1977. Effect of ammonia on mitochondrial and cytosolic NADH and NADPH systems in isolated rat liver cells. FEBS Lett. 76 : 99 104.
    • (1977) FEBS Lett. , vol.76 , pp. 99-104
    • Tischler, M.E.1    Hecht, P.2    Williamson, J.R.3
  • 21
    • 0018337607 scopus 로고
    • Assay of citric acid cycle intermediates and related compounds-update with tissue metabolite levels and intracellular distribution
    • &
    • Williamson, J.R. & B.E. Corkey. 1979. Assay of citric acid cycle intermediates and related compounds-update with tissue metabolite levels and intracellular distribution. Methods Enzymol. 55 : 200 222.
    • (1979) Methods Enzymol. , vol.55 , pp. 200-222
    • Williamson, J.R.1    Corkey, B.E.2
  • 22
    • 0018320433 scopus 로고
    • Hepatic mitochondrial and cytosolic glutathione content and the subcellular distribution of GSH-S-transferases
    • Wahllander, A. et al. 1979. Hepatic mitochondrial and cytosolic glutathione content and the subcellular distribution of GSH-S-transferases. FEBS Lett. 97 : 138 140.
    • (1979) FEBS Lett. , vol.97 , pp. 138-140
    • Wahllander, A.1
  • 23
    • 0001547757 scopus 로고
    • Origin and turnover of mitochondrial glutathione
    • &
    • Griffith, O.W. & A. Meister. 1985. Origin and turnover of mitochondrial glutathione. Proc. Natl. Acad. Sci. USA 82 : 4668 4672.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4668-4672
    • Griffith, O.W.1    Meister, A.2
  • 24
    • 0041326831 scopus 로고    scopus 로고
    • Effects of age and caloric restriction on glutathione redox state in mice
    • &
    • Rebrin, I., S. Kamzalov & R.S. Sohal. 2003. Effects of age and caloric restriction on glutathione redox state in mice. Free. Radic. Biol. Med. 35 : 626 635.
    • (2003) Free. Radic. Biol. Med. , vol.35 , pp. 626-635
    • Rebrin, I.1    Kamzalov, S.2    Sohal, R.S.3
  • 25
    • 6944220226 scopus 로고    scopus 로고
    • Comparison of thiol redox state of mitochondria and homogenates of various tissues between two strains of mice with different longevities
    • &
    • Rebrin, I. & R.S. Sohal. 2004. Comparison of thiol redox state of mitochondria and homogenates of various tissues between two strains of mice with different longevities. Exp. Gerontol. 39 : 1513 1519.
    • (2004) Exp. Gerontol. , vol.39 , pp. 1513-1519
    • Rebrin, I.1    Sohal, R.S.2
  • 26
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • Gardner, P.R. et al. 1995. Superoxide radical and iron modulate aconitase activity in mammalian cells. J. Biol. Chem. 270 : 13399 13405.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13399-13405
    • Gardner, P.R.1
  • 27
    • 0033000269 scopus 로고    scopus 로고
    • Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals: Inhibition of alpha-ketoglutarate dehydrogenase
    • &
    • Chinopoulos, C., L. Tretter & V. Adam-Vizi. 1999. Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals: inhibition of alpha-ketoglutarate dehydrogenase. J. Neurochem. 73 : 220 228.
    • (1999) J. Neurochem. , vol.73 , pp. 220-228
    • Chinopoulos, C.1    Tretter, L.2    Adam-Vizi, V.3
  • 28
    • 0142028110 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress and mitochondrial DNA
    • &
    • Kang, D. & N. Hamasaki. 2003. Mitochondrial oxidative stress and mitochondrial DNA. Clin. Chem. Lab. Med. 41 : 1281 1288.
    • (2003) Clin. Chem. Lab. Med. , vol.41 , pp. 1281-1288
    • Kang, D.1    Hamasaki, N.2
  • 29
    • 34247127167 scopus 로고    scopus 로고
    • Mitochondrial DNA repair: A critical player in the response of cells of the CNS to genotoxic insults
    • LeDoux, S.P. et al. 2007. Mitochondrial DNA repair: a critical player in the response of cells of the CNS to genotoxic insults. Neuroscience 145 : 1249 1259.
    • (2007) Neuroscience , vol.145 , pp. 1249-1259
    • Ledoux, S.P.1
  • 30
    • 30344432706 scopus 로고    scopus 로고
    • Role of mitochondrial DNA in toxic responses to oxidative stress
    • &
    • Van Houten, B., V. Woshner & J.H. Santos. 2006. Role of mitochondrial DNA in toxic responses to oxidative stress. DNA Repair (Amst) 5 : 145 152.
    • (2006) DNA Repair (Amst) , vol.5 , pp. 145-152
    • Van Houten, B.1    Woshner, V.2    Santos, J.H.3
  • 32
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens, J.F. 2003. Mitochondrial formation of reactive oxygen species. J. Physiol. 552 : 335 344.
    • (2003) J. Physiol. , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 33
    • 33751072935 scopus 로고    scopus 로고
    • Bioenergetics and the formation of mitochondrial reactive oxygen species
    • &
    • Adam-Vizi, V. & C. Chinopoulos. 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
  • 34
    • 0024616270 scopus 로고
    • Dihydrolipoamide dehydrogenase: Functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases
    • &
    • Carothers, D.J., G. Pons & M.S. Patel. 1989. Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases. Arch. Biochem. Biophys. 268 : 409 425.
    • (1989) Arch. Biochem. Biophys. , vol.268 , pp. 409-425
    • Carothers, D.J.1    Pons, G.2    Patel, M.S.3
  • 35
    • 4544226082 scopus 로고    scopus 로고
    • Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase
    • &
    • Tretter, L. & V. Adam-Vizi. 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
  • 36
    • 4544359913 scopus 로고    scopus 로고
    • Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species
    • Starkov, A.A. et al. 2004. Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species. J. Neurosci. 24 : 7779 7788.
    • (2004) J. Neurosci. , vol.24 , pp. 7779-7788
    • Starkov, A.A.1
  • 37
    • 0017638174 scopus 로고
    • The effective proton conductance of the inner membrane of mitochondria from brown adipose tissue. Dependency on proton electrochemical potential gradient
    • Nicholls, D.G. 1977. The effective proton conductance of the inner membrane of mitochondria from brown adipose tissue. Dependency on proton electrochemical potential gradient. Eur. J. Biochem. 77 : 349 356.
    • (1977) Eur. J. Biochem. , vol.77 , pp. 349-356
    • Nicholls, D.G.1
  • 38
    • 4544264062 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and aging
    • Nicholls, D.G. 2004. Mitochondrial membrane potential and aging. Aging Cell 3 : 35 40.
    • (2004) Aging Cell , vol.3 , pp. 35-40
    • Nicholls, D.G.1
  • 39
    • 0023718383 scopus 로고
    • Pathways of succinate formation and their contribution to improvement of cardiac function in the hypoxic rat heart
    • &
    • Wiesner, R.J., P. Rosen & M.K. Grieshaber. 1988. Pathways of succinate formation and their contribution to improvement of cardiac function in the hypoxic rat heart. Biochem. Med. Metab. Biol. 40 : 19 34.
    • (1988) Biochem. Med. Metab. Biol. , vol.40 , pp. 19-34
    • Wiesner, R.J.1    Rosen, P.2    Grieshaber, M.K.3
  • 40
    • 0028403340 scopus 로고
    • Myocardial metabolic markers of total ischemia in vitro
    • Kakinuma, Y. et al. 1994. Myocardial metabolic markers of total ischemia in vitro. Nagoya. J. Med. Sci. 57 : 35 42.
    • (1994) Nagoya. J. Med. Sci. , vol.57 , pp. 35-42
    • Kakinuma, Y.1
  • 41
    • 0020062174 scopus 로고
    • Relationships between gamma-aminobutyrate and succinate cycles during and after cerebral ischemia
    • &
    • Benzi, G., O. Pastoris & M. Dossena. 1982. Relationships between gamma-aminobutyrate and succinate cycles during and after cerebral ischemia. J. Neurosci. Res. 7 : 193 201.
    • (1982) J. Neurosci. Res. , vol.7 , pp. 193-201
    • Benzi, G.1    Pastoris, O.2    Dossena, M.3
  • 42
    • 0029008947 scopus 로고
    • Insulin, ketone bodies, and mitochondrial energy transduction
    • Sato, K. et al. 1995. Insulin, ketone bodies, and mitochondrial energy transduction. FASEB J. 9 : 651 658.
    • (1995) FASEB J. , vol.9 , pp. 651-658
    • Sato, K.1
  • 45
    • 34547850680 scopus 로고    scopus 로고
    • 2 release at NADH:ubiquinone oxidoreductase (Complex I) in brain mitochondria
    • 2 release at NADH:ubiquinone oxidoreductase (Complex I) in brain mitochondria. Biochem. J. 406 : 125 129.
    • (2007) Biochem. J. , vol.406 , pp. 125-129
    • Zoccarato, F.1
  • 47
    • 38749087624 scopus 로고    scopus 로고
    • High rates of superoxide production in skeletal muscle mitochondria respiring on both Complex I and Complex II linked substrates
    • Muller, F.L. et al. 2008. High rates of superoxide production in skeletal muscle mitochondria respiring on both Complex I and Complex II linked substrates. Biochem. J. 409 : 491 499.
    • (2008) Biochem. J. , vol.409 , pp. 491-499
    • Muller, F.L.1
  • 48
    • 0014199579 scopus 로고
    • The inhibition of succinate dehydrogenase by oxaloacetate
    • &
    • Zeyelmaker, W.P. & E.C. Slater. 1967. The inhibition of succinate dehydrogenase by oxaloacetate. Biochim. Biophys. Acta 132 : 210 212.
    • (1967) Biochim. Biophys. Acta , vol.132 , pp. 210-212
    • Zeyelmaker, W.P.1    Slater, E.C.2
  • 49
    • 0014696173 scopus 로고
    • The inhibition of succinate dehydrogenase by oxalacetate
    • &
    • Wojtczak, L., A.B. Wojtczak & L. Ernster. 1969. The inhibition of succinate dehydrogenase by oxalacetate. Biochim. Biophys. Acta 191 : 10 21.
    • (1969) Biochim. Biophys. Acta , vol.191 , pp. 10-21
    • Wojtczak, L.1    Wojtczak, A.B.2    Ernster, L.3
  • 50
    • 21844441151 scopus 로고    scopus 로고
    • Reducing mitochondrial decay with mitochondrial nutrients to delay and treat cognitive dysfunction, Alzheimer's disease, and Parkinson's disease
    • &
    • Liu, J. & B.N. Ames. 2005. Reducing mitochondrial decay with mitochondrial nutrients to delay and treat cognitive dysfunction, Alzheimer's disease, and Parkinson's disease. Nutr. Neurosci. 8 : 67 89.
    • (2005) Nutr. Neurosci. , vol.8 , pp. 67-89
    • Liu, J.1    Ames, B.N.2
  • 51
    • 25444474703 scopus 로고    scopus 로고
    • Mitochondria take center stage in aging and neurodegeneration
    • Beal, M.F. 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
  • 52
    • 10244246626 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative damage in Alzheimer's and Parkinson's diseases and coenzyme Q10 as a potential treatment
    • Beal, M.F. 2004. Mitochondrial dysfunction and oxidative damage in Alzheimer's and Parkinson's diseases and coenzyme Q10 as a potential treatment. J. Bioenerg. Biomembr. 36 : 381 386.
    • (2004) J. Bioenerg. Biomembr. , vol.36 , pp. 381-386
    • Beal, M.F.1
  • 53
    • 27544484846 scopus 로고    scopus 로고
    • Are mitochondria critical in the pathogenesis of Alzheimer's disease?
    • &
    • Reddy, P.H. & M.F. Beal. 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
  • 54
    • 23244435445 scopus 로고    scopus 로고
    • The alpha-ketoglutarate-dehydrogenase complex: A mediator between mitochondria and oxidative stress in neurodegeneration
    • Gibson, G.E. et al. 2005. The alpha-ketoglutarate-dehydrogenase complex: a mediator between mitochondria and oxidative stress in neurodegeneration. Mol. Neurobiol. 31 : 43 63.
    • (2005) Mol. Neurobiol. , vol.31 , pp. 43-63
    • Gibson, G.E.1
  • 55
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • &
    • Turrens, J.F. & A. Boveris. 1980. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 191 : 421 427.
    • (1980) Biochem. J. , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 56
    • 0018393931 scopus 로고
    • NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH-ubiquinone reductase preparation
    • &
    • Takeshige, K. & S. Minakami. 1979. NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH-ubiquinone reductase preparation. Biochem. J. 180 : 129 135.
    • (1979) Biochem. J. , vol.180 , pp. 129-135
    • Takeshige, K.1    Minakami, S.2
  • 57
    • 4043090717 scopus 로고    scopus 로고
    • Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane
    • &
    • Lambert, A.J. & M.D. Brand. 2004. Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane. Biochem. J. 384 : 511 517.
    • (2004) Biochem. J. , vol.384 , pp. 511-517
    • Lambert, A.J.1    Brand, M.D.2
  • 58
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • &
    • Boveris, A. & B. Chance. 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
  • 60
    • 0029398106 scopus 로고
    • Nonphosphorylating respiration as the mechanism preventing the formation of active forms of oxygen
    • Skulachev, V.P. 1995. Nonphosphorylating respiration as the mechanism preventing the formation of active forms of oxygen. Mol. Biol. (Mosk) 29 : 1199 1209.
    • (1995) Mol. Biol. (Mosk) , vol.29 , pp. 1199-1209
    • Skulachev, V.P.1
  • 61
    • 0029765443 scopus 로고    scopus 로고
    • Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants
    • Skulachev, V.P. 1996. Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants. Q. Rev. Biophys. 29 : 169 202.
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 169-202
    • Skulachev, V.P.1
  • 62
    • 33846225260 scopus 로고    scopus 로고
    • Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: Implications for hypoxic cell signaling
    • &
    • Hoffman, D.L., J.D. Salter & P.S. Brookes. 2007. Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: implications for hypoxic cell signaling. Am. J. Physiol. Heart. Circ. Physiol. 292 : H101 H108.
    • (2007) Am. J. Physiol. Heart. Circ. Physiol. , vol.292
    • Hoffman, D.L.1    Salter, J.D.2    Brookes, P.S.3
  • 63
    • 34548126843 scopus 로고    scopus 로고
    • Fluorescent and luminescent probes for measurement of oxidative and nitrosative species in cells and tissues: Progress, pitfalls, and prospects
    • Wardman, P. 2007. Fluorescent and luminescent probes for measurement of oxidative and nitrosative species in cells and tissues: progress, pitfalls, and prospects. Free. Radic. Biol. Med. 43 : 995 1022.
    • (2007) Free. Radic. Biol. Med. , vol.43 , pp. 995-1022
    • Wardman, P.1
  • 64
    • 0034816698 scopus 로고    scopus 로고
    • Cytochrome C is a potent catalyst of dichlorofluorescin oxidation: Implications for the role of reactive oxygen species in apoptosis
    • &
    • Burkitt, M.J. & P. Wardman. 2001. Cytochrome C is a potent catalyst of dichlorofluorescin oxidation: implications for the role of reactive oxygen species in apoptosis. Biochem. Biophys. Res. Commun. 282 : 329 333.
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 329-333
    • Burkitt, M.J.1    Wardman, P.2
  • 65
    • 0037196379 scopus 로고    scopus 로고
    • Rapid oxidation of dichlorodihydrofluorescin with heme and hemoproteins: Formation of the fluorescein is independent of the generation of reactive oxygen species
    • Ohashi, T. et al. 2002. Rapid oxidation of dichlorodihydrofluorescin with heme and hemoproteins: formation of the fluorescein is independent of the generation of reactive oxygen species. FEBS Lett. 511 : 21 27.
    • (2002) FEBS Lett. , vol.511 , pp. 21-27
    • Ohashi, T.1
  • 66
    • 16244384516 scopus 로고    scopus 로고
    • 2: Relevance to redox signalling in apoptosis
    • 2: relevance to redox signalling in apoptosis. Biochem. Soc. Symp. 71 : 97 106.
    • (2004) Biochem. Soc. Symp. , vol.71 , pp. 97-106
    • Burkitt, M.1
  • 67
    • 0024439390 scopus 로고
    • Cytochrome P-450, reductive metabolism, and cell injury
    • &
    • De Groot, H. & H. Sies. 1989. Cytochrome P-450, reductive metabolism, and cell injury. Drug. Metab. Rev. 20 : 275 284.
    • (1989) Drug. Metab. Rev. , vol.20 , pp. 275-284
    • De Groot, H.1    Sies, H.2
  • 68
    • 33847084336 scopus 로고    scopus 로고
    • Tissue heterogeneity of the mammalian mitochondrial proteome
    • Johnson, D.T. et al. 2007. Tissue heterogeneity of the mammalian mitochondrial proteome. Am. J. Physiol. Cell Physiol. 292 : C689 C697.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Johnson, D.T.1
  • 69
    • 33847083940 scopus 로고    scopus 로고
    • Functional consequences of mitochondrial proteome heterogeneity
    • Johnson, D.T. et al. 2007. Functional consequences of mitochondrial proteome heterogeneity. Am. J. Physiol. Cell Physiol. 292 : C698 C707.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Johnson, D.T.1
  • 70
    • 0031847248 scopus 로고    scopus 로고
    • The role of manganese superoxide dismutase in health and disease
    • Robinson, B.H. 1998. The role of manganese superoxide dismutase in health and disease. J. Inherit. Metab. Dis. 21 : 598 603.
    • (1998) J. Inherit. Metab. Dis. , vol.21 , pp. 598-603
    • Robinson, B.H.1
  • 71
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria
    • &
    • Okado-Matsumoto, A. & I. Fridovich. 2001. Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria. J. Biol. Chem. 276 : 38388 38393.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 72
    • 17144427680 scopus 로고    scopus 로고
    • Redox activation of mitochondrial intermembrane space Cu,Zn-superoxide dismutase
    • Inarrea, P. et al. 2005. Redox activation of mitochondrial intermembrane space Cu,Zn-superoxide dismutase. Biochem. J. 387 : 203 209.
    • (2005) Biochem. J. , vol.387 , pp. 203-209
    • Inarrea, P.1
  • 73
    • 33646241740 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and amyotrophic lateral sclerosis
    • &
    • Hervias, I., M.F. Beal & G. Manfredi. 2006. Mitochondrial dysfunction and amyotrophic lateral sclerosis. Muscle. Nerve. 33 : 598 608.
    • (2006) Muscle. Nerve. , vol.33 , pp. 598-608
    • Hervias, I.1    Beal, M.F.2    Manfredi, G.3
  • 74
    • 0032712539 scopus 로고    scopus 로고
    • The antioxidant functions of cytochrome c
    • Korshunov, S.S. et al. 1999. The antioxidant functions of cytochrome c. FEBS Lett. 462 : 192 198.
    • (1999) FEBS Lett. , vol.462 , pp. 192-198
    • Korshunov, S.S.1
  • 75
    • 0025003089 scopus 로고
    • Superoxide radical as electron donor for oxidative phosphorylation of ADP
    • Mailer, K. 1990. Superoxide radical as electron donor for oxidative phosphorylation of ADP. Biochem. Biophys. Res. Commun. 170 : 59 64.
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 59-64
    • Mailer, K.1
  • 76
    • 0029082812 scopus 로고
    • Mitochondrial respiration scavenges extramitochondrial superoxide anion via a nonenzymatic mechanism
    • Guidot, D.M. et al. 1995. Mitochondrial respiration scavenges extramitochondrial superoxide anion via a nonenzymatic mechanism. J. Clin. Invest. 96 : 1131 1136.
    • (1995) J. Clin. Invest. , vol.96 , pp. 1131-1136
    • Guidot, D.M.1
  • 77
    • 0022790702 scopus 로고
    • The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport
    • &
    • Hackenbrock, C.R., B. Chazotte & S.S. Gupte. 1986. The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport. J. Bioenerg. Biomembr. 18 : 331 368.
    • (1986) J. Bioenerg. Biomembr. , vol.18 , pp. 331-368
    • Hackenbrock, C.R.1    Chazotte, B.2    Gupte, S.S.3
  • 78
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • &
    • McCord, J.M. & I. Fridovich. 1969. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244 : 6049 6055.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 80
  • 81
    • 0023161822 scopus 로고
    • 2 production by brain in vivo
    • 2 production by brain in vivo. J. Appl. Physiol. 63 : 353 358.
    • (1987) J. Appl. Physiol. , vol.63 , pp. 353-358
    • Yusa, T.1
  • 82
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • &
    • Chance, B., H. Sies & A. Boveris. 1979. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59 : 527 605.
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 83
    • 0002889135 scopus 로고    scopus 로고
    • Cellular sources and steady-state levels of reactive oxygen species
    • In: L.B. Clerch. & D.J. Massaro, Eds.: Marcel Dekker. New York.
    • Boveris, A., Cadenas, E. 1997. Cellular sources and steady-state levels of reactive oxygen species. In : Oxygen, Gene Expression and Cellular Function. L.B. Clerch & D.J. Massaro, Eds. : 1 25. Marcel Dekker. New York.
    • (1997) Oxygen, Gene Expression and Cellular Function. , pp. 1-25
    • Boveris, A.1    Cadenas, E.2
  • 84
    • 0030816391 scopus 로고    scopus 로고
    • Cellular glutathione peroxidase knockout mice express normal levels of selenium-dependent plasma and phospholipid hydroperoxide glutathione peroxidases in various tissues
    • Cheng, W.H. et al. 1997. Cellular glutathione peroxidase knockout mice express normal levels of selenium-dependent plasma and phospholipid hydroperoxide glutathione peroxidases in various tissues. J. Nutr. 127 : 1445 1450.
    • (1997) J. Nutr. , vol.127 , pp. 1445-1450
    • Cheng, W.H.1
  • 85
    • 0030971057 scopus 로고    scopus 로고
    • Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia
    • Ho, Y.S. et al. 1997. Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia. J. Biol. Chem. 272 : 16644 16651.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16644-16651
    • Ho, Y.S.1
  • 86
    • 0032834347 scopus 로고    scopus 로고
    • H(2)O(2) detection from intact mitochondria as a measure for one-electron reduction of dioxygen requires a non-invasive assay system
    • &
    • Staniek, K. & H. Nohl. 1999. H(2)O(2) detection from intact mitochondria as a measure for one-electron reduction of dioxygen requires a non-invasive assay system. Biochim. Biophys. Acta 1413 : 70 80.
    • (1999) Biochim. Biophys. Acta , vol.1413 , pp. 70-80
    • Staniek, K.1    Nohl, H.2
  • 87
    • 34248159898 scopus 로고    scopus 로고
    • Mitochondrial targeting of quinones: Therapeutic implications
    • Cocheme, H.M. et al. 2007. Mitochondrial targeting of quinones: therapeutic implications. Mitochondrion 7 (Suppl S94 S102.
    • (2007) Mitochondrion , vol.7
    • Cocheme, H.M.1
  • 88
    • 0034811384 scopus 로고    scopus 로고
    • Myxothiazol induces H(2)O(2) production from mitochondrial respiratory chain
    • &
    • Starkov, A.A. & G. Fiskum. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.