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Volumn 1, Issue 2, 2001, Pages 151-159

Reactive oxygen species generated by the mitochondrial respiratory chain affect the complex III activity via cardiolipin peroxidation in beef-heart submitochondrial particles

Author keywords

Beef heart submitochondrial particles; Cardiolipin; CL, cardiolipin; Complex III; NAO, 10 N nonyl acridine orange; PC, phosphatidylcholine; Reactive oxygen species; ROS, reactive oxygen species; SMP, submitochondrial particles; SOD, superoxide dismutase

Indexed keywords

BOVINAE;

EID: 0008724863     PISSN: 15677249     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1567-7249(01)00011-3     Document Type: Article
Times cited : (109)

References (42)
  • 1
    • 0025147117 scopus 로고
    • Activation of beef-heart cytochrome c oxidase by cardiolipin and analogues of cardiolipin
    • Abramovitch D.A., Marsh D., Powell G.L. Activation of beef-heart cytochrome c oxidase by cardiolipin and analogues of cardiolipin. Biochim. Biophys. Acta. 1020:1990;34-42.
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 34-42
    • Abramovitch, D.A.1    Marsh, D.2    Powell, G.L.3
  • 3
    • 0027234615 scopus 로고
    • Hepatic mitochondrial energy production in rats with chronic iron overload
    • Bacon B.R., O'Neill R., Britton R.S. Hepatic mitochondrial energy production in rats with chronic iron overload. Gastroenterology. 105:1993;1134-1140.
    • (1993) Gastroenterology , vol.105 , pp. 1134-1140
    • Bacon, B.R.1    O'Neill, R.2    Britton, R.S.3
  • 4
    • 0032847556 scopus 로고    scopus 로고
    • Ethanol stimulates the production of reactive oxygen species at mitochondrial complexes I and III
    • Bailey S.M., Pietsch E.C., Cunningham C.C. Ethanol stimulates the production of reactive oxygen species at mitochondrial complexes I and III. Free Radic. Biol. Med. 27:1999;891-900.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 891-900
    • Bailey, S.M.1    Pietsch, E.C.2    Cunningham, C.C.3
  • 5
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh E.G., Dyer W.J. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37:1959;911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 6
    • 0021288856 scopus 로고
    • Determination of the production of superoxide radicals and hydrogen peroxide in mitochondria
    • Boveris A. Determination of the production of superoxide radicals and hydrogen peroxide in mitochondria. Methods Enzymol. 105:1984;429-435.
    • (1984) Methods Enzymol. , vol.105 , pp. 429-435
    • Boveris, A.1
  • 7
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • Boveris A., Chance B. The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen. Biochem. J. 134:1973;707-716.
    • (1973) Biochem. J. , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 8
    • 0017406503 scopus 로고
    • Production of superoxide radicals and hydrogen peroxide by NADH-lubiquinone reductase and ubiquinl-cytochrome c reductase from beef-heart mitochondria
    • Cadenas E., Boveris A., Ragan C.I., Stoppani A.O.M. Production of superoxide radicals and hydrogen peroxide by NADH-lubiquinone reductase and ubiquinl-cytochrome c reductase from beef-heart mitochondria. Arch. Biochem. Biophys. 180:1977;248-257.
    • (1977) Arch. Biochem. Biophys. , vol.180 , pp. 248-257
    • Cadenas, E.1    Boveris, A.2    Ragan, C.I.3    Stoppani, A.O.M.4
  • 9
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B., Sies H., Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59:1979;527-605.
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 10
    • 0019333130 scopus 로고
    • The localization of tightly bound cardiolipin in cytochrome oxidase
    • Fry M., Blondin G.A., Green D.E. The localization of tightly bound cardiolipin in cytochrome oxidase. J. Biol. Chem. 255:1980;9967-9970.
    • (1980) J. Biol. Chem. , vol.255 , pp. 9967-9970
    • Fry, M.1    Blondin, G.A.2    Green, D.E.3
  • 11
    • 0344019484 scopus 로고    scopus 로고
    • Quantitative determination of cardiolipin in mitochondrial electron transferring complexes by silicic acid high-performance liquid chromatography
    • Gomez B. Jr., Robinson N.C. Quantitative determination of cardiolipin in mitochondrial electron transferring complexes by silicic acid high-performance liquid chromatography. Anal. Biochem. 267:1999a;212-216.
    • (1999) Anal. Biochem. , vol.267 , pp. 212-216
    • Gomez B., Jr.1    Robinson, N.C.2
  • 13
    • 0030856714 scopus 로고    scopus 로고
    • Direct inhibition of mitochondrial repiratory chain complex III by cell-permeable ceramide
    • Gudz T.I., Tserng K.Y., Hoppel C.L. Direct inhibition of mitochondrial repiratory chain complex III by cell-permeable ceramide. J. Biol. Chem. 272:1997;24154-24158.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24154-24158
    • Gudz, T.I.1    Tserng, K.Y.2    Hoppel, C.L.3
  • 15
    • 0030012354 scopus 로고    scopus 로고
    • Regulation of cardiolipin biosynthesis in the heart
    • Hatch G.M. Regulation of cardiolipin biosynthesis in the heart. Mol. Cell Biochem. 159:1996;139-148.
    • (1996) Mol. Cell Biochem. , vol.159 , pp. 139-148
    • Hatch, G.M.1
  • 16
    • 0026603840 scopus 로고
    • Cardiolipins and biomembrane function
    • Hoch F.L. Cardiolipins and biomembrane function. Biochim. Biophys. Acta. 1113:1992;71-133.
    • (1992) Biochim. Biophys. Acta , vol.1113 , pp. 71-133
    • Hoch, F.L.1
  • 18
    • 29644435163 scopus 로고
    • Energy-coupling in nonphosphorylating submitochondrial particles
    • Lee C., Ernster L. Energy-coupling in nonphosphorylating submitochondrial particles. Methods Enzymol. 10:1967;543-548.
    • (1967) Methods Enzymol. , vol.10 , pp. 543-548
    • Lee, C.1    Ernster, L.2
  • 19
    • 50549169010 scopus 로고
    • Succinate-linked diphosphopyridine nucleotide reduction in submitochondrial particles
    • Löw H., Vallin I. Succinate-linked diphosphopyridine nucleotide reduction in submitochondrial particles. Biochim. Biophys. Acta. 69:1963;361-374.
    • (1963) Biochim. Biophys. Acta , vol.69 , pp. 361-374
    • Löw, H.1    Vallin, I.2
  • 20
    • 0023831219 scopus 로고
    • Free radicals and myocardial ischemia: Overview and outlook
    • McCord J.M. Free radicals and myocardial ischemia: overview and outlook. Free Radic. Biol. Med. 4:1988;9-14.
    • (1988) Free Radic. Biol. Med. , vol.4 , pp. 9-14
    • McCord, J.M.1
  • 21
    • 0027291723 scopus 로고
    • Age-dependent decrease in the cytochrome c oxidase activity and changes in phospholipid in rat-heart mitochondria
    • Paradies G., Ruggiero F.M., Petrosillo G., Quagliariello E. Age-dependent decrease in the cytochrome c oxidase activity and changes in phospholipid in rat-heart mitochondria. Arch. Gerontol. Geriatr. 16:1993a;263-272.
    • (1993) Arch. Gerontol. Geriatr. , vol.16 , pp. 263-272
    • Paradies, G.1    Ruggiero, F.M.2    Petrosillo, G.3    Quagliariello, E.4
  • 22
    • 0027489678 scopus 로고
    • Decreased cytochrome oxidase activity and changes in phospholipids in heart mitochondria from hypothyroid rats
    • Paradies G., Ruggiero F.M., Dinoi P., Petrosillo G., Quagliariello E. Decreased cytochrome oxidase activity and changes in phospholipids in heart mitochondria from hypothyroid rats. Arch. Biochem. Biophys. 307:1993b;91-95.
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 91-95
    • Paradies, G.1    Ruggiero, F.M.2    Dinoi, P.3    Petrosillo, G.4    Quagliariello, E.5
  • 23
    • 0028025440 scopus 로고
    • Effect of aging and acetyl-L-carnitine on the activity of cytochrome oxidase and adenine nucleotide
    • Paradies G., Ruggiero F.M., Petrosillo G., Gadaleta M.N., Quagliariello E. Effect of aging and acetyl-L-carnitine on the activity of cytochrome oxidase and adenine nucleotide. FEBS Lett. 350:1994a;213-215.
    • (1994) FEBS Lett. , vol.350 , pp. 213-215
    • Paradies, G.1    Ruggiero, F.M.2    Petrosillo, G.3    Gadaleta, M.N.4    Quagliariello, E.5
  • 24
    • 0027979906 scopus 로고
    • Enhanced cytochrome oxidase activity and modification of lipids in heart mitochondria from hyperthyroid rats
    • Paradies G., Ruggiero F.M., Petrosillo G., Quagliariello E. Enhanced cytochrome oxidase activity and modification of lipids in heart mitochondria from hyperthyroid rats. Biochim. Biophys. Acta. 1225:1994b;165-170.
    • (1994) Biochim. Biophys. Acta , vol.1225 , pp. 165-170
    • Paradies, G.1    Ruggiero, F.M.2    Petrosillo, G.3    Quagliariello, E.4
  • 25
    • 0030992498 scopus 로고    scopus 로고
    • Age-dependent decline in the cytochrome c oxidase activity in rat heart mitochondria: Role of cardiolipin
    • Paradies G., Ruggiero F.M., Petrosillo G., Quagliariello E. Age-dependent decline in the cytochrome c oxidase activity in rat heart mitochondria: role of cardiolipin. FEBS Lett. 406:1997a;136-138.
    • (1997) FEBS Lett. , vol.406 , pp. 136-138
    • Paradies, G.1    Ruggiero, F.M.2    Petrosillo, G.3    Quagliariello, E.4
  • 26
    • 0030929650 scopus 로고    scopus 로고
    • Cardiolipin-dependent decrease of cytochrome c oxidase activity in heart mitochondria from hypothyroid rats
    • Paradies G., Petrosillo G., Ruggiero F.M. Cardiolipin-dependent decrease of cytochrome c oxidase activity in heart mitochondria from hypothyroid rats. Biochim. Biophys. Acta. 1319:1997b;5-8.
    • (1997) Biochim. Biophys. Acta , vol.1319 , pp. 5-8
    • Paradies, G.1    Petrosillo, G.2    Ruggiero, F.M.3
  • 27
    • 0032513135 scopus 로고    scopus 로고
    • Peroxidative damage to cardiac mitochondria: Cytochrome oxidase and cardiolipin alterations
    • Paradies G., Ruggiero F.M., Petrosillo G., Quagliariello E. Peroxidative damage to cardiac mitochondria: cytochrome oxidase and cardiolipin alterations. FEBS Lett. 424:1998;155-158.
    • (1998) FEBS Lett. , vol.424 , pp. 155-158
    • Paradies, G.1    Ruggiero, F.M.2    Petrosillo, G.3    Quagliariello, E.4
  • 28
    • 0032775546 scopus 로고    scopus 로고
    • Lipid peroxidation and alterations to oxidative metabolism in mitochondria isolated from rat heart subjected to ischemia and reperfusion
    • Paradies G., Petrosillo G., Pistolese M., Di Venosa N., Serena D., Ruggiero F.M. Lipid peroxidation and alterations to oxidative metabolism in mitochondria isolated from rat heart subjected to ischemia and reperfusion. Free Radic. Biol. Med. 27:1999;42-50.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 42-50
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Di Venosa, N.4    Serena, D.5    Ruggiero, F.M.6
  • 29
    • 0033984710 scopus 로고    scopus 로고
    • The effect of reactive oxygen species generated from mitochondrial electron transport chain on the cytochrome c oxidase activity and on the cardiolipin content in bovine heart submitochondrial particles
    • Paradies G., Petrosillo G., Pistolese M., Ruggiero F.M. The effect of reactive oxygen species generated from mitochondrial electron transport chain on the cytochrome c oxidase activity and on the cardiolipin content in bovine heart submitochondrial particles. FEBS Lett. 466:2000;323-326.
    • (2000) FEBS Lett. , vol.466 , pp. 323-326
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 30
    • 0026742850 scopus 로고
    • 10-N-nonyl acridine orange interacts with cardiolipin and allows the quantification of this phospholipid in isolated mitochondria
    • Petit J.M., Maftah A., Ratinaud M.H., Julien R. 10-N-nonyl acridine orange interacts with cardiolipin and allows the quantification of this phospholipid in isolated mitochondria. Eur. J. Biochem. 209:1992;267-273.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 267-273
    • Petit, J.M.1    Maftah, A.2    Ratinaud, M.H.3    Julien, R.4
  • 31
    • 0023567929 scopus 로고
    • Spin-label studies on the specificity of interaction of cardiolipin with beef heart cytochrome oxidase
    • Powell G.L., Knowles P.F., Marsh D. Spin-label studies on the specificity of interaction of cardiolipin with beef heart cytochrome oxidase. Biochemistry. 26:1987;8138-8145.
    • (1987) Biochemistry , vol.26 , pp. 8138-8145
    • Powell, G.L.1    Knowles, P.F.2    Marsh, D.3
  • 32
    • 0027252494 scopus 로고
    • Functional binding of cardiolipin to cytochrome c oxidase
    • Robinson N.C. Functional binding of cardiolipin to cytochrome c oxidase. J. Bioenerg. Biomembr. 25:1993;153-163.
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 153-163
    • Robinson, N.C.1
  • 33
    • 0019317502 scopus 로고
    • Investigation of the essential boundary layer phospholipids of cytochrome c oxidase using Triton X-100 delipidation
    • Robinson N.C., Strey F., Talbert L. Investigation of the essential boundary layer phospholipids of cytochrome c oxidase using Triton X-100 delipidation. Biochemistry. 19:1980;3656-3661.
    • (1980) Biochemistry , vol.19 , pp. 3656-3661
    • Robinson, N.C.1    Strey, F.2    Talbert, L.3
  • 34
    • 0021346839 scopus 로고
    • Lipid composition of liver mitochondria and microsomes in hyperthyroid rats
    • Ruggiero F.M., Landriscina C., Gnoni G.V., Quagliariello E. Lipid composition of liver mitochondria and microsomes in hyperthyroid rats. Lipids. 19:1984;171-178.
    • (1984) Lipids , vol.19 , pp. 171-178
    • Ruggiero, F.M.1    Landriscina, C.2    Gnoni, G.V.3    Quagliariello, E.4
  • 35
    • 0031552931 scopus 로고    scopus 로고
    • Cardiolipin synthase from mammalian mitochondria
    • Schlame M., Hostetler K.Y. Cardiolipin synthase from mammalian mitochondria. Biochim. Biophys. Acta. 1348:1997;207-213.
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 207-213
    • Schlame, M.1    Hostetler, K.Y.2
  • 36
    • 0021763962 scopus 로고
    • Free-radical mechanism in tissue injury
    • Slater T. Free-radical mechanism in tissue injury. Biochem. J. 222:1984;1-15.
    • (1984) Biochem. J. , vol.222 , pp. 1-15
    • Slater, T.1
  • 37
    • 0027177530 scopus 로고
    • Abnormal hepatic mitochondrial respiration and cytochrome C oxidase activity in rats with long-term copper overload
    • Sokol R.J., Devereaux M.W., O'Brien K., Khandwala R.A., Loehr J.P. Abnormal hepatic mitochondrial respiration and cytochrome C oxidase activity in rats with long-term copper overload. Gastroeneterology. 105:1993;178-187.
    • (1993) Gastroeneterology , vol.105 , pp. 178-187
    • Sokol, R.J.1    Devereaux, M.W.2    O'Brien, K.3    Khandwala, R.A.4    Loehr, J.P.5
  • 38
    • 0030969868 scopus 로고    scopus 로고
    • Superoxide production by the mitochondrial respiratory chain
    • Turrens J. Superoxide production by the mitochondrial respiratory chain. Biosci. Rep. 17:1997;3-8.
    • (1997) Biosci. Rep. , vol.17 , pp. 3-8
    • Turrens, J.1
  • 39
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens J.F., Boveris A. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 191:1980;421-427.
    • (1980) Biochem. J. , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 40
    • 0019546059 scopus 로고
    • Diphosphatidylglycerol is required for optimal activity of beef heart cytochrome c oxidase
    • Vik S.B., Georgevich G., Capaldi R.A. Diphosphatidylglycerol is required for optimal activity of beef heart cytochrome c oxidase. Proc. Natl Acad. Sci. USA. 78:1981;1456-1460.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 1456-1460
    • Vik, S.B.1    Georgevich, G.2    Capaldi, R.A.3
  • 41
    • 0026587335 scopus 로고
    • Mitochondrial genetics: A paradigm for aging and degenerative diseases?
    • Wallace D.C. Mitochondrial genetics: a paradigm for aging and degenerative diseases? Science. 256:1992;628-632.
    • (1992) Science , vol.256 , pp. 628-632
    • Wallace, D.C.1
  • 42
    • 0024996681 scopus 로고
    • The oxidative inactivation of mitochondrial electron transport chain components and ATPase
    • Zhang Y., Marcillat O., Giulivi C., Ernster L., Davies K.J.A. The oxidative inactivation of mitochondrial electron transport chain components and ATPase. J. Biol. Chem. 265:1990;16330-16336.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16330-16336
    • Zhang, Y.1    Marcillat, O.2    Giulivi, C.3    Ernster, L.4    Davies, K.J.A.5


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