메뉴 건너뛰기




Volumn 1, Issue 1, 1998, Pages 53-66

A mechanism proposed to explain the rise in oxidative stress during aging

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIA; VERTEBRATA;

EID: 0002386563     PISSN: 10945458     EISSN: None     Source Type: Journal    
DOI: 10.1089/rej.1.1998.1.53     Document Type: Article
Times cited : (39)

References (73)
  • 1
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • Harman D: Aging: A theory based on free radical and radiation chemistry. J Gerontol 1956;11:298-300.
    • (1956) J Gerontol , vol.11 , pp. 298-300
    • Harman, D.1
  • 2
    • 0015319592 scopus 로고
    • The biologic clock: The mitochondria?
    • Harman D: The biologic clock: The mitochondria? J Am Geriatr Soc 1972;20:145-147.
    • (1972) J Am Geriatr Soc , vol.20 , pp. 145-147
    • Harman, D.1
  • 3
    • 0028349236 scopus 로고
    • Decline with age of the respiratory chain activity in human skeletal muscle
    • Boffoli D, Scacco SC, Vergar R et al.: Decline with age of the respiratory chain activity in human skeletal muscle. Biochim Biophys Acta 1994;1226:73-82.
    • (1994) Biochim Biophys Acta , vol.1226 , pp. 73-82
    • Boffoli, D.1    Scacco, S.C.2    Vergar, R.3
  • 4
    • 0027182560 scopus 로고
    • Changes in skeletal muscle, heart and liver mitochondrial electron transport activities in rats and dogs of various ages
    • Sugiyama S, Takasawa M, Hayakawa M et al.: Changes in skeletal muscle, heart and liver mitochondrial electron transport activities in rats and dogs of various ages. Biochem Mol Biol Int 1993;30:937-944.
    • (1993) Biochem Mol Biol Int , vol.30 , pp. 937-944
    • Sugiyama, S.1    Takasawa, M.2    Hayakawa, M.3
  • 5
    • 0006861095 scopus 로고
    • Changes in speed of contraction and ATPase activity in striated muscle during old age
    • Syrovy I, and Gutmann E: Changes in speed of contraction and ATPase activity in striated muscle during old age. Exp Gerontol 1977;12:31-35.
    • (1977) Exp Gerontol , vol.12 , pp. 31-35
    • Syrovy, I.1    Gutmann, E.2
  • 6
    • 0025674177 scopus 로고
    • Detection of a specific mitochondrial DNA deletion in tissues of older humans
    • Cortopassi GA, and Arnheim N: Detection of a specific mitochondrial DNA deletion in tissues of older humans. Nucleic Acids Res 1990;18:6927-6933.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6927-6933
    • Cortopassi, G.A.1    Arnheim, N.2
  • 7
    • 0026782895 scopus 로고
    • Deleterious mitochondrial DNA mutations accumulate in aging human tissues
    • Arnheim N, and Cortopassi G: Deleterious mitochondrial DNA mutations accumulate in aging human tissues. Mutat Res 1992;275:157-167.
    • (1992) Mutat Res , vol.275 , pp. 157-167
    • Arnheim, N.1    Cortopassi, G.2
  • 8
    • 0029101232 scopus 로고
    • Human aging is associated with stochastic somatic mutations of mitochondrial DNA
    • Kadenbach B, Muenscher C, Frank V et al.: Human aging is associated with stochastic somatic mutations of mitochondrial DNA. Mutat Res 1995;338:161-172.
    • (1995) Mutat Res , vol.338 , pp. 161-172
    • Kadenbach, B.1    Muenscher, C.2    Frank, V.3
  • 9
    • 0029741431 scopus 로고    scopus 로고
    • Evidence that specific mtDNA point mutations may not accumulate in skeletal muscle during normal human aging
    • Pallotti F, Chen X, Bonilla E et al: Evidence that specific mtDNA point mutations may not accumulate in skeletal muscle during normal human aging. Am J Hum Genet 1996;59:591-602.
    • (1996) Am J Hum Genet , vol.59 , pp. 591-602
    • Pallotti, F.1    Chen, X.2    Bonilla, E.3
  • 10
    • 0027017232 scopus 로고
    • Mitochondrial DNA deletions in human brain: Regional variability and increase with advanced age
    • Corral-Debrinski M, Horton T, Lott MT et al.: Mitochondrial DNA deletions in human brain: Regional variability and increase with advanced age. Nat Genet 1992;2:324-329.
    • (1992) Nat Genet , vol.2 , pp. 324-329
    • Corral-Debrinski, M.1    Horton, T.2    Lott, M.T.3
  • 11
    • 0026732706 scopus 로고
    • A pattern of accumulation of a somatic deletion of mitochondrial DNA in aging human tissues
    • Cortopassi GA, Shibata D, Soong NW et al.: A pattern of accumulation of a somatic deletion of mitochondrial DNA in aging human tissues. Proc Natl Acad Sci USA 1992;89:7370-7374.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7370-7374
    • Cortopassi, G.A.1    Shibata, D.2    Soong, N.W.3
  • 13
    • 0024541068 scopus 로고
    • Mitochondrial DNA mutations and neuromuscular disease
    • Wallace DC: Mitochondrial DNA mutations and neuromuscular disease. Trends Genet 1989;5:9-13.
    • (1989) Trends Genet , vol.5 , pp. 9-13
    • Wallace, D.C.1
  • 14
    • 0002827532 scopus 로고
    • Group report: The role of bioenergetics and mitochondrial DNA mutations in aging and age-related diseases
    • Esser K, Martin GM: Chichester, UK: Wiley
    • Wallace DC, Bohr VA, Cortopassi G et al.: Group report: The role of bioenergetics and mitochondrial DNA mutations in aging and age-related diseases, in Esser K, Martin GM: Molecular aspects of aging. Chichester, UK: Wiley, 1995:199-225.
    • (1995) Molecular Aspects of Aging , pp. 199-225
    • Wallace, D.C.1    Bohr, V.A.2    Cortopassi, G.3
  • 15
    • 0024366601 scopus 로고
    • Cytochrome c oxidase deficient cardiomyocytes in the human heart - An age-related phenomenon. A histochemical ultracytochemical study
    • Mueller-Hoecker J: Cytochrome c oxidase deficient cardiomyocytes in the human heart - An age-related phenomenon. A histochemical ultracytochemical study. Am J Pathol 1989;134:1167-1173.
    • (1989) Am J Pathol , vol.134 , pp. 1167-1173
    • Mueller-Hoecker, J.1
  • 16
    • 0027525966 scopus 로고
    • Different in situ hybridization patterns of mitochondrial DNA in cytochrome c oxidase-deficient extraocular muscle fibres in the elderly
    • Mueller-Hoecker J, Seibel P, Schneiderbanger K et al.: Different in situ hybridization patterns of mitochondrial DNA in cytochrome c oxidase-deficient extraocular muscle fibres in the elderly. Virchows Arch (A) 1993;422:7-15.
    • (1993) Virchows Arch (A) , vol.422 , pp. 7-15
    • Mueller-Hoecker, J.1    Seibel, P.2    Schneiderbanger, K.3
  • 17
    • 0026762675 scopus 로고
    • Mitochondrial DNA deletions and cytochrome c oxidase deficiency in muscle fibres
    • Oldfors A, Larsson NG, Holme E et al.: Mitochondrial DNA deletions and cytochrome c oxidase deficiency in muscle fibres. J Neurol Sci 1992;110:169-177.
    • (1992) J Neurol Sci , vol.110 , pp. 169-177
    • Oldfors, A.1    Larsson, N.G.2    Holme, E.3
  • 18
    • 0029890212 scopus 로고    scopus 로고
    • Defects of the respiratory chain in oxyphil and chief cells of the normal parathyroid and in hyperfunction
    • Mueller-Hoecker J, Aust D, Napiwotzky J et al.: Defects of the respiratory chain in oxyphil and chief cells of the normal parathyroid and in hyperfunction. Hum Pathol 1996;27:532-541.
    • (1996) Hum Pathol , vol.27 , pp. 532-541
    • Mueller-Hoecker, J.1    Aust, D.2    Napiwotzky, J.3
  • 19
    • 0030800847 scopus 로고    scopus 로고
    • Defects of the respiratory chain in the normal human liver and in cirrhosis during aging
    • Mueller-Hoecker J, Aust D, Rohrbach H et al.: Defects of the respiratory chain in the normal human liver and in cirrhosis during aging. Hepatology 1997;26: 709-719.
    • (1997) Hepatology , vol.26 , pp. 709-719
    • Mueller-Hoecker, J.1    Aust, D.2    Rohrbach, H.3
  • 20
    • 0030982145 scopus 로고    scopus 로고
    • Caloric restriction reduces fiber loss and mitochondrial abnormalities in aged rat muscle
    • Aspnes LE, Lee CM, Weindruch R et al.: Caloric restriction reduces fiber loss and mitochondrial abnormalities in aged rat muscle. FASEB J 1997;11:573-581.
    • (1997) FASEB J , vol.11 , pp. 573-581
    • Aspnes, L.E.1    Lee, C.M.2    Weindruch, R.3
  • 22
    • 0031081410 scopus 로고    scopus 로고
    • A proposed refinement of the mitochondrial free radical theory of aging
    • de Grey ADNJ: A proposed refinement of the mitochondrial free radical theory of aging. BioEssays 1997;19:161-166.
    • (1997) BioEssays , vol.19 , pp. 161-166
    • De Grey, A.D.N.J.1
  • 23
    • 0030583123 scopus 로고    scopus 로고
    • Comparison of different quantitative PCR procedures in the analysis of the 4977-bp deletion in human mitochondrial DNA
    • Zhang C, Peters LE, Linnane AW et al.: Comparison of different quantitative PCR procedures in the analysis of the 4977-bp deletion in human mitochondrial DNA. Biochem Biophys Res Commun 1996;223: 450-455.
    • (1996) Biochem Biophys Res Commun , vol.223 , pp. 450-455
    • Zhang, C.1    Peters, L.E.2    Linnane, A.W.3
  • 24
    • 0019423856 scopus 로고
    • Sequence and organization of the human mitochondrial genome
    • Anderson S, Bankier AT, Barrell BG et al.: Sequence and organization of the human mitochondrial genome. Nature 1981;290:457-465.
    • (1981) Nature , vol.290 , pp. 457-465
    • Anderson, S.1    Bankier, A.T.2    Barrell, B.G.3
  • 25
    • 0030931198 scopus 로고    scopus 로고
    • Quantitative allele-specific PCR: Demonstration of age-associated accumulation in human tissues of the A → G mutation at nucleotide 3243 in mitochondrial DNA
    • Liu VW, Zhang C, Linnane AW et al.: Quantitative allele-specific PCR: Demonstration of age-associated accumulation in human tissues of the A → G mutation at nucleotide 3243 in mitochondrial DNA. Hum Mutat 1997;9:265-271.
    • (1997) Hum Mutat , vol.9 , pp. 265-271
    • Liu, V.W.1    Zhang, C.2    Linnane, A.W.3
  • 26
    • 0030743628 scopus 로고    scopus 로고
    • Multiplex fluorescence-based primer extension method for quantitative mutation analysis of mitochondrial DNA and its diagnostic application for Alzheimer's disease
    • Fahy E, Nazarbaghi R, Zomorrodi M et al.: Multiplex fluorescence-based primer extension method for quantitative mutation analysis of mitochondrial DNA and its diagnostic application for Alzheimer's disease. Nucleic Acids Res 1997;25:3102-3109.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3102-3109
    • Fahy, E.1    Nazarbaghi, R.2    Zomorrodi, M.3
  • 27
    • 0042873918 scopus 로고    scopus 로고
    • Correspondence arising from BioEssays 19:161-166
    • Gershon D, and de Grey ADNJ: Correspondence arising from BioEssays 19:161-166. BioEssays 1997;19: 533-534.
    • (1997) BioEssays , vol.19 , pp. 533-534
    • Gershon, D.1    De Grey, A.D.N.J.2
  • 28
    • 2542509453 scopus 로고    scopus 로고
    • Defects of the respiratory chain in various tissues of old monkeys: A cytochemical-immunocytochemical study
    • Mueller-Hoecker J, Schaefer S, Link TA et al.: Defects of the respiratory chain in various tissues of old monkeys: A cytochemical-immunocytochemical study. Mech. Ageing Dev 1996;86:197-213.
    • (1996) Mech. Ageing Dev , vol.86 , pp. 197-213
    • Mueller-Hoecker, J.1    Schaefer, S.2    Link, T.A.3
  • 29
    • 0024448458 scopus 로고
    • Human cells lacking mtDNA: Repopulation with exogenous mitochondria by complementation
    • King MP, and Attardi G: Human cells lacking mtDNA: Repopulation with exogenous mitochondria by complementation. Science 1989;246:500-503.
    • (1989) Science , vol.246 , pp. 500-503
    • King, M.P.1    Attardi, G.2
  • 30
    • 0027788187 scopus 로고
    • 0 human Namalwa cells lacking oxidative phosphorylation can be sustained by redox compounds potassium ferricyanide or coenzyme Q10 putatively acting through the plasma membrane oxidase
    • 0 human Namalwa cells lacking oxidative phosphorylation can be sustained by redox compounds potassium ferricyanide or coenzyme Q10 putatively acting through the plasma membrane oxidase. Biochem Mol Biol Int 1993;31:997-1005.
    • (1993) Biochem Mol Biol Int , vol.31 , pp. 997-1005
    • Martinus, R.D.1    Linnane, A.W.2    Nagley, P.3
  • 31
    • 0017147261 scopus 로고
    • NADH oxidation in liver and fat cell plasma membranes
    • Crane FL, and Loew H: NADH oxidation in liver and fat cell plasma membranes. FEBS Lett 1976;68: 153-156.
    • (1976) FEBS Lett , vol.68 , pp. 153-156
    • Crane, F.L.1    Loew, H.2
  • 32
    • 0021971399 scopus 로고
    • Transplasma-membrane redox systems in growth and development
    • Crane FL, Sun IL, Clark MG et al.: Transplasma-membrane redox systems in growth and development. Biochim Biophys Acta 1985;811:233-264.
    • (1985) Biochim Biophys Acta , vol.811 , pp. 233-264
    • Crane, F.L.1    Sun, I.L.2    Clark, M.G.3
  • 34
    • 0019882289 scopus 로고
    • Evidence for the extracellular reduction of ferricyanide by rat liver. A trans-plasma membrane redox system
    • Clark MG, Partick EJ, Patten GS et al.: Evidence for the extracellular reduction of ferricyanide by rat liver. A trans-plasma membrane redox system. Biochem J 1981;200:565-572.
    • (1981) Biochem J , vol.200 , pp. 565-572
    • Clark, M.G.1    Partick, E.J.2    Patten, G.S.3
  • 35
    • 0029966791 scopus 로고    scopus 로고
    • Effectors of the mammalian plasma membrane NADH-oxidoreductase system. Short-chain ubiquinone analogues as potent stimulators
    • Vaillant F, Larm JA, McMullen GL et al.: Effectors of the mammalian plasma membrane NADH-oxidoreductase system. Short-chain ubiquinone analogues as potent stimulators. J Bioenerg Biomembr 1996;28: 531-540.
    • (1996) J Bioenerg Biomembr , vol.28 , pp. 531-540
    • Vaillant, F.1    Larm, J.A.2    McMullen, G.L.3
  • 36
    • 0028805056 scopus 로고
    • The interstitium of the human arterial wall contains very large amounts of extracellular superoxide dismutase
    • Stralin P, Karlsson K, Johansson BO et al.: The interstitium of the human arterial wall contains very large amounts of extracellular superoxide dismutase. Arterioscler Thromb Vasc Biol 1995;15:2032-2036.
    • (1995) Arterioscler Thromb Vasc Biol , vol.15 , pp. 2032-2036
    • Stralin, P.1    Karlsson, K.2    Johansson, B.O.3
  • 37
    • 0001557130 scopus 로고
    • Lipid peroxidation: Mechanisms, analysis, enzymology and biological relevance
    • Sies H: New York: Academic Press
    • Kappus H: Lipid peroxidation: Mechanisms, analysis, enzymology and biological relevance, in Sies H: Oxidative stress. New York: Academic Press, 1985:152-195.
    • (1985) Oxidative Stress , pp. 152-195
    • Kappus, H.1
  • 38
    • 0023144940 scopus 로고
    • Superoxide-dependent and ascorbate-dependent formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Are lactoferrin and transferrin promoters of hydroxyl-radical generation?
    • Aruoma OI, and Halliwell B: Superoxide-dependent and ascorbate-dependent formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Are lactoferrin and transferrin promoters of hydroxyl-radical generation? Biochem J 1987;241:273-278.
    • (1987) Biochem J , vol.241 , pp. 273-278
    • Aruoma, O.I.1    Halliwell, B.2
  • 39
    • 0023423859 scopus 로고
    • Involvement of transferrin in the reduction of iron by the transplasma membrane electron transport system
    • Loew H, Grebing C, Lindgren A et al.: Involvement of transferrin in the reduction of iron by the transplasma membrane electron transport system. J Bioenerg Biomembr 1987;19:535-549.
    • (1987) J Bioenerg Biomembr , vol.19 , pp. 535-549
    • Loew, H.1    Grebing, C.2    Lindgren, A.3
  • 40
    • 0024576159 scopus 로고
    • Inhibition of superoxide and ferritin-dependent lipid peroxidation by ceruloplasmin
    • Samokyszyn VM, Miller DM, Reif DW et al.: Inhibition of superoxide and ferritin-dependent lipid peroxidation by ceruloplasmin. J Biol Chem 1989;264: 21-26.
    • (1989) J Biol Chem , vol.264 , pp. 21-26
    • Samokyszyn, V.M.1    Miller, D.M.2    Reif, D.W.3
  • 41
    • 0028800858 scopus 로고
    • The involvement of low-density lipoprotein in hemin transport potentiates peroxidative damage
    • Miller YI, Felikman Y, and Shaklai N: The involvement of low-density lipoprotein in hemin transport potentiates peroxidative damage. Biochim Biophys Acta 1995;1272:119-127.
    • (1995) Biochim Biophys Acta , vol.1272 , pp. 119-127
    • Miller, Y.I.1    Felikman, Y.2    Shaklai, N.3
  • 42
    • 0017158738 scopus 로고
    • Transfer of heme from heme-albumin to hemopexin
    • Morgan WT, Liem HH, Sutor RP et al.: Transfer of heme from heme-albumin to hemopexin. Biochim Biophys Acta 1976;444:435-445.
    • (1976) Biochim Biophys Acta , vol.444 , pp. 435-445
    • Morgan, W.T.1    Liem, H.H.2    Sutor, R.P.3
  • 43
    • 0029802271 scopus 로고    scopus 로고
    • Role of hemopexin in protection of low-density lipoprotein against hemoglobin-induced oxidation
    • Miller YI, Smith A, Morgan WT et al.: Role of hemopexin in protection of low-density lipoprotein against hemoglobin-induced oxidation. Biochemistry 1996; 35:13112-13117.
    • (1996) Biochemistry , vol.35 , pp. 13112-13117
    • Miller, Y.I.1    Smith, A.2    Morgan, W.T.3
  • 44
    • 0030034871 scopus 로고    scopus 로고
    • Low-density lipoprotein is the major carrier of lipid hydroperoxides in plasma. Relevance to determination of total plasma lipid hydroperoxide concentrations
    • Nourooz-Zadeh J, Tajaddini-Sarmadi J, Ling KL et al.: Low-density lipoprotein is the major carrier of lipid hydroperoxides in plasma. Relevance to determination of total plasma lipid hydroperoxide concentrations. Biochem J 1996;313:781-786.
    • (1996) Biochem J , vol.313 , pp. 781-786
    • Nourooz-Zadeh, J.1    Tajaddini-Sarmadi, J.2    Ling, K.L.3
  • 45
    • 0030799043 scopus 로고    scopus 로고
    • Low density lipoprotein oxidation and its pathobiological significance
    • Steinberg D: Low density lipoprotein oxidation and its pathobiological significance. J Biol Chem 1997;272: 20963-20966.
    • (1997) J Biol Chem , vol.272 , pp. 20963-20966
    • Steinberg, D.1
  • 46
    • 0025281588 scopus 로고
    • Minimally modified low density lipoprotein induces monocyte chemotactic protein 1 in human endothelial cells and smooth muscle cells
    • Cushing SD, Berliner JA, Valente AJ et al.: Minimally modified low density lipoprotein induces monocyte chemotactic protein 1 in human endothelial cells and smooth muscle cells. Proc Natl Acad Sci USA 1990;87:5134-5138.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5134-5138
    • Cushing, S.D.1    Berliner, J.A.2    Valente, A.J.3
  • 47
    • 0025177343 scopus 로고
    • Type I macrophage scavenger receptor contains alpha-helical and collagen-like coiled coils
    • Kodama T, Freeman M, Rohrer L et al.: Type I macrophage scavenger receptor contains alpha-helical and collagen-like coiled coils. Nature 1990;343: 531-535.
    • (1990) Nature , vol.343 , pp. 531-535
    • Kodama, T.1    Freeman, M.2    Rohrer, L.3
  • 48
    • 0025886155 scopus 로고
    • Different fate in vivo of oxidatively modified low density lipoprotein and acetylated low density lipoprotein in rats. Recognition by various scavenger receptors on Kupffer and endothelial liver cells
    • van Berkel TJ, de Rijke YB, and Kruijt JK: Different fate in vivo of oxidatively modified low density lipoprotein and acetylated low density lipoprotein in rats. Recognition by various scavenger receptors on Kupffer and endothelial liver cells. J Biol Chem 1991;266:2282-2289.
    • (1991) J Biol Chem , vol.266 , pp. 2282-2289
    • Berkel, T.J.1    De Rijke, Y.B.2    Kruijt, J.K.3
  • 49
    • 0028874432 scopus 로고
    • Contents of D-lactate and its related metabolites as well as enzyme activities in the liver, muscle and blood plasma of aging rats
    • Kawase M, Kondoh C, Matsumoto S et al.: Contents of D-lactate and its related metabolites as well as enzyme activities in the liver, muscle and blood plasma of aging rats. Mech Ageing Dev 1995;84:55-63.
    • (1995) Mech Ageing Dev , vol.84 , pp. 55-63
    • Kawase, M.1    Kondoh, C.2    Matsumoto, S.3
  • 50
    • 0028890715 scopus 로고
    • Protein hydroperoxides can give rise to reactive free radicals
    • Davies MJ, Fu S, and Dean RT: Protein hydroperoxides can give rise to reactive free radicals. Biochem J 1995;305:643-649.
    • (1995) Biochem J , vol.305 , pp. 643-649
    • Davies, M.J.1    Fu, S.2    Dean, R.T.3
  • 51
    • 0028989694 scopus 로고
    • A direct role for serum albumin in the cellular uptake of long-chain fatty acids
    • Trigatti BL, and Gerber GE: A direct role for serum albumin in the cellular uptake of long-chain fatty acids. Biochem J 1995;308:155-159.
    • (1995) Biochem J , vol.308 , pp. 155-159
    • Trigatti, B.L.1    Gerber, G.E.2
  • 52
    • 0027436058 scopus 로고
    • Reactivity of plasma glutathione peroxidase with hydroperoxide substrates and glutathione
    • Esworthy RS, Chu FF, Geiger P et al.: Reactivity of plasma glutathione peroxidase with hydroperoxide substrates and glutathione. Arch Biochem Biophys 1993;307:29-34.
    • (1993) Arch Biochem Biophys , vol.307 , pp. 29-34
    • Esworthy, R.S.1    Chu, F.F.2    Geiger, P.3
  • 53
    • 0018786482 scopus 로고
    • NADH oxidoreductase of mouse liver plasma membranes
    • Goldenberg H, Crane LF, Moore DJ: NADH oxidoreductase of mouse liver plasma membranes. J. Biol. Chem. 1979;254:2491-2498.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2491-2498
    • Goldenberg, H.1    Crane, L.F.2    Moore, D.J.3
  • 54
    • 0023109883 scopus 로고
    • Heparin-induced release of extracellular superoxide dismutase to human blood plasma
    • Karlsson K, and Marklund SL: Heparin-induced release of extracellular superoxide dismutase to human blood plasma. Biochem J 1987;242:55-59.
    • (1987) Biochem J , vol.242 , pp. 55-59
    • Karlsson, K.1    Marklund, S.L.2
  • 55
    • 0000061171 scopus 로고
    • Modification of low density lipoprotein by endothelial cells involves lipid peroxidation and degradation of low density lipoprotein phospholipids
    • Steinbrecher UP, Parthasarathy S, Leake DS et al.: Modification of low density lipoprotein by endothelial cells involves lipid peroxidation and degradation of low density lipoprotein phospholipids. Proc Natl Acad Sci USA 1984;81:3883-3887.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3883-3887
    • Steinbrecher, U.P.1    Parthasarathy, S.2    Leake, D.S.3
  • 56
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • Boveris A, and Chance B: The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen. Biochem J 1973;134: 707-716.
    • (1973) Biochem J , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 57
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett BS, and Stadtman ER: Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 1997;272:20313-20316.
    • (1997) J Biol Chem , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 58
    • 0031038812 scopus 로고    scopus 로고
    • Selective inhibition of mutant human mitochondrial DNA replication in vitro by peptide nucleic acids
    • Taylor RW, Chinnery PF, Turnbull DM et al.: Selective inhibition of mutant human mitochondrial DNA replication in vitro by peptide nucleic acids. Nature Genet 1997;15:212-215.
    • (1997) Nature Genet , vol.15 , pp. 212-215
    • Taylor, R.W.1    Chinnery, P.F.2    Turnbull, D.M.3
  • 59
    • 0028804570 scopus 로고
    • Transfection of mitochondria: Strategy towards a gene therapy of mitochondrial DNA diseases
    • Seibel P, Trappe J, Villani G et al.: Transfection of mitochondria: Strategy towards a gene therapy of mitochondrial DNA diseases. Nucleic Acids Res 1995;23:10-17.
    • (1995) Nucleic Acids Res , vol.23 , pp. 10-17
    • Seibel, P.1    Trappe, J.2    Villani, G.3
  • 60
    • 0024121557 scopus 로고
    • Assembly of functional proton-translocating ATPase complex in yeast mitochondria with cytoplasmically synthesized subunit 8, a polypeptide normally encoded within the organelle
    • Nagley P, Farrell LB, Gearing DP et al.: Assembly of functional proton-translocating ATPase complex in yeast mitochondria with cytoplasmically synthesized subunit 8, a polypeptide normally encoded within the organelle. Proc Natl Acad Sci USA 1988;85:2091-2095.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2091-2095
    • Nagley, P.1    Farrell, L.B.2    Gearing, D.P.3
  • 61
    • 0025315698 scopus 로고
    • Mitochondrial diseases: Gene mapping and gene therapy
    • Lander ES, and Lodish H: Mitochondrial diseases: Gene mapping and gene therapy. Cell 1990;61:925-926.
    • (1990) Cell , vol.61 , pp. 925-926
    • Lander, E.S.1    Lodish, H.2
  • 62
    • 0027234431 scopus 로고
    • Possible reversal of ageing and other mitochondrial deficiencies through retroviral transfection of mitochondrially encoded proteins to the nucleus
    • Hoeben P: Possible reversal of ageing and other mitochondrial deficiencies through retroviral transfection of mitochondrially encoded proteins to the nucleus. Med Hypotheses 1993;41:131-133.
    • (1993) Med Hypotheses , vol.41 , pp. 131-133
    • Hoeben, P.1
  • 63
  • 65
    • 0030872907 scopus 로고    scopus 로고
    • Selective targeting of bioactive compounds to mitochondria
    • Murphy MP: Selective targeting of bioactive compounds to mitochondria. Trends Biotechnol 1997;15: 326-330.
    • (1997) Trends Biotechnol , vol.15 , pp. 326-330
    • Murphy, M.P.1
  • 66
    • 0025852051 scopus 로고
    • Duplication of leader sequence for protein targeting to mitochondria leads to increased import efficiency
    • Galanis M, Devenish RJ, and Nagley P: Duplication of leader sequence for protein targeting to mitochondria leads to increased import efficiency. FEBS Lett 1991;282:425-430.
    • (1991) FEBS Lett , vol.282 , pp. 425-430
    • Galanis, M.1    Devenish, R.J.2    Nagley, P.3
  • 67
    • 0028932673 scopus 로고    scopus 로고
    • Limitations to in vivo import of hydrophobic proteins into yeast mitochondria. The case of a cytoplasmically synthesised apocytochrome b
    • Claros MG, Perea J, Shu Y et al.: Limitations to in vivo import of hydrophobic proteins into yeast mitochondria. The case of a cytoplasmically synthesised apocytochrome b. Eur J Biochem 1996;228:762-771.
    • (1996) Eur J Biochem , vol.228 , pp. 762-771
    • Claros, M.G.1    Perea, J.2    Shu, Y.3
  • 68
    • 0030930366 scopus 로고    scopus 로고
    • A model for in vivo-induced apoptosis
    • Polyak K, Xia Y, Zweier JL et al.: A model for in vivo-induced apoptosis. Nature 1997;389:300-305.
    • (1997) Nature , vol.389 , pp. 300-305
    • Polyak, K.1    Xia, Y.2    Zweier, J.L.3
  • 69
    • 0031563164 scopus 로고    scopus 로고
    • p53 induces myocyte apoptosis via the activation of the reninangiotensin system
    • Pierzchalaski P, Reiss K, Cheng W et al.: p53 induces myocyte apoptosis via the activation of the reninangiotensin system. Exp Cell Res 1997;234:57-65.
    • (1997) Exp Cell Res , vol.234 , pp. 57-65
    • Pierzchalaski, P.1    Reiss, K.2    Cheng, W.3
  • 70
    • 0001218860 scopus 로고
    • Ascorbate is an outstanding antioxidant in human blood plasma
    • Frei B, England L, and Ames BN: Ascorbate is an outstanding antioxidant in human blood plasma. Proc Natl Acad Sci USA 1989;86:6377-6381.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6377-6381
    • Frei, B.1    England, L.2    Ames, B.N.3
  • 71
    • 0343086874 scopus 로고
    • Increase of plasma-membrane oxidoreductase activity is not correlated with the production of extracellular superoxide radicals in human Namalwa cells
    • Larm JA, Wolvetang EJ, Vaillant F et al.: Increase of plasma-membrane oxidoreductase activity is not correlated with the production of extracellular superoxide radicals in human Namalwa cells. Protoplasma 1995;184:173-180.
    • (1995) Protoplasma , vol.184 , pp. 173-180
    • Larm, J.A.1    Wolvetang, E.J.2    Vaillant, F.3
  • 72
    • 0027254622 scopus 로고
    • A new sensitive chemiluminescence probe, L-012, for measuring the production of superoxide anion by cells
    • Nishinaka Y, Aramaki Y, Yoshida H et al.: A new sensitive chemiluminescence probe, L-012, for measuring the production of superoxide anion by cells. Biochem Biophys Res Commun 1993;193:554-559.
    • (1993) Biochem Biophys Res Commun , vol.193 , pp. 554-559
    • Nishinaka, Y.1    Aramaki, Y.2    Yoshida, H.3
  • 73
    • 0028007581 scopus 로고
    • Hormone- and growth factor-stimulated NADH oxidase
    • Moore DJ: Hormone- and growth factor-stimulated NADH oxidase. J. Bioenerg. Biomembr. 1994;26:421-433.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 421-433
    • Moore, D.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.