메뉴 건너뛰기




Volumn 66, Issue 4, 1996, Pages 1617-1624

Threshold effects and control of oxidative phosphorylation in nonsynaptic rat brain mitochondria

Author keywords

Aging; Alzheimer's disease; Brain mitochondria; Complex I; Complex III; Complex IV; Flux control coefficients; Huntington's disease; Oxidative phosphorylation; Parkinson's disease; Threshold effects

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYTOCHROME C OXIDASE; MITOCHONDRIAL DNA; MYXOTHIAZOL; POTASSIUM CYANIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); ROTENONE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 0029873904     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.66041617.x     Document Type: Article
Times cited : (187)

References (46)
  • 1
    • 0028793538 scopus 로고
    • Postnatal development of the complexes of the electron transport chain in synaptic mitochondria from rat brain
    • Almeida A., Brooks K. J., Sammut I., Keelan J., Davey G. P., Clark J. A., and Bates T. E. (1995) Postnatal development of the complexes of the electron transport chain in synaptic mitochondria from rat brain. Dev. Neurosci 17, 212-218.
    • (1995) Dev. Neurosci , vol.17 , pp. 212-218
    • Almeida, A.1    Brooks, K.J.2    Sammut, I.3    Keelan, J.4    Davey, G.P.5    Clark, J.A.6    Bates, T.E.7
  • 2
    • 0026584524 scopus 로고
    • Does impairment of energy metabolism result in excitotoxic neuronal death in neurodegenerative illnesses?
    • Beal M. F. (1992) Does impairment of energy metabolism result in excitotoxic neuronal death in neurodegenerative illnesses? Ann. Neurol. 31, 119-130.
    • (1992) Ann. Neurol. , vol.31 , pp. 119-130
    • Beal, M.F.1
  • 3
    • 0028952832 scopus 로고
    • Effect of peroxynitrite on the mitochondrial respiratory chain: Differential susceptibility of neurones and astrocytes in primary culture
    • Bolaños J. P., Heales S. J. R., Land J. M., and Clark J. B. (1995) Effect of peroxynitrite on the mitochondrial respiratory chain: differential susceptibility of neurones and astrocytes in primary culture. J. Neurochem. 64, 1965-1972.
    • (1995) J. Neurochem. , vol.64 , pp. 1965-1972
    • Bolaños, J.P.1    Heales, S.J.R.2    Land, J.M.3    Clark, J.B.4
  • 4
    • 0028936986 scopus 로고
    • Bioenergetic and oxidative stress in neurodegenerative diseases
    • Bowling A. C. and Beal M. F. (1995) Bioenergetic and oxidative stress in neurodegenerative diseases. Life Sci. 56, 1151-1171.
    • (1995) Life Sci. , vol.56 , pp. 1151-1171
    • Bowling, A.C.1    Beal, M.F.2
  • 6
    • 0023681888 scopus 로고
    • Control of respiration in non-phosphorylating mitochondria is shared between the proton leak and the respiratory chain
    • Brand M. D., Hafner R. P., and Brown G. C. (1988) Control of respiration in non-phosphorylating mitochondria is shared between the proton leak and the respiratory chain. Biochem. J. 255, 535-539.
    • (1988) Biochem. J. , vol.255 , pp. 535-539
    • Brand, M.D.1    Hafner, R.P.2    Brown, G.C.3
  • 7
    • 0021883670 scopus 로고
    • Regional mitochondrial respiratory activity in Huntington's disease brain
    • Brennan W. A. Jr., Bird E. D., and Aprille J. R. (1985) Regional mitochondrial respiratory activity in Huntington's disease brain. J. Neurochem. 44, 1948-1950.
    • (1985) J. Neurochem. , vol.44 , pp. 1948-1950
    • Brennan Jr., W.A.1    Bird, E.D.2    Aprille, J.R.3
  • 8
    • 0028134892 scopus 로고
    • Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • Brown G. C. and Cooper C. E. (1994) Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase. FEBS Lett. 356, 295-298.
    • (1994) FEBS Lett. , vol.356 , pp. 295-298
    • Brown, G.C.1    Cooper, C.E.2
  • 9
    • 0029033427 scopus 로고
    • Nitric oxide produced by activated astrocytes rapidly and reversibly inhibits cellular respiration
    • Brown G C., Bolaños J. P., Heales S. J. R., and Clark J. B. (1995) Nitric oxide produced by activated astrocytes rapidly and reversibly inhibits cellular respiration. Neurosci. Lett. 193, 201-204.
    • (1995) Neurosci. Lett. , vol.193 , pp. 201-204
    • Brown, G.C.1    Bolaños, J.P.2    Heales, S.J.R.3    Clark, J.B.4
  • 10
    • 0020604776 scopus 로고
    • Phosphate-activated glutaminase in relation to Huntington's disease and agonal state
    • Butterworth J., Yates C. M., and Simpson J. (1983) Phosphate-activated glutaminase in relation to Huntington's disease and agonal state. J. Neurochem. 41, 440-447.
    • (1983) J. Neurochem. , vol.41 , pp. 440-447
    • Butterworth, J.1    Yates, C.M.2    Simpson, J.3
  • 11
  • 12
    • 84911229134 scopus 로고
    • The metabolism of rat brain mitochondria
    • Clark J. B. and Nicklas W. J. (1970) The metabolism of rat brain mitochondria. J. Biol. Chem. 193, 265-275.
    • (1970) J. Biol. Chem. , vol.193 , pp. 265-275
    • Clark, J.B.1    Nicklas, W.J.2
  • 13
    • 0026598930 scopus 로고
    • Irreversible inhibition of mitochondrial complex I by 1-methyl-4-phenylpyridinium: Evidence for free radical involvement
    • Cleeter M. W. J., Cooper J. M., and Schapira A. H. V. (1992) Irreversible inhibition of mitochondrial complex I by 1-methyl-4-phenylpyridinium: evidence for free radical involvement. J. Neurochem. 58, 786-789.
    • (1992) J. Neurochem. , vol.58 , pp. 786-789
    • Cleeter, M.W.J.1    Cooper, J.M.2    Schapira, A.H.V.3
  • 14
    • 0026469073 scopus 로고
    • Analysis of mitochondrial respiration chain functions and mitochondrial-DNA deletions in human skeletal muscle - Effect of aging
    • Cooper J. M., Mann V. M., and Schapira A. H. V (1992) Analysis of mitochondrial respiration chain functions and mitochondrial-DNA deletions in human skeletal muscle - effect of aging. J. Neurol. Sci. 113, 91-98.
    • (1992) J. Neurol. Sci. , vol.113 , pp. 91-98
    • Cooper, J.M.1    Mann, V.M.2    Schapira, A.H.V.3
  • 15
    • 0027017232 scopus 로고
    • Mitochondrial-DNA deletions in human brain-regional variability and increase with advanced age
    • Corral-Debrinski M., Horton T., Lott M. T , Shoffner J. M., Beal M. F., and Wallace D. C. (1992) Mitochondrial-DNA deletions in human brain-regional variability and increase with advanced age. Nat. Genet 2, 324-329.
    • (1992) Nat. Genet , vol.2 , pp. 324-329
    • Corral-Debrinski, M.1    Horton, T.2    Lott, M.T.3    Shoffner, J.M.4    Beal, M.F.5    Wallace, D.C.6
  • 16
    • 0021106617 scopus 로고
    • Control of mitochondrial respiration: The contribution of adenine nucleotide translocator depends on the ATP- and ADP-consuming enzymes
    • Gellerich F. N., Bohnensack R., and Kunz W. (1983) Control of mitochondrial respiration: the contribution of adenine nucleotide translocator depends on the ATP- and ADP-consuming enzymes. Biochim. Biophys. Acta 722, 381-391.
    • (1983) Biochim. Biophys. Acta , vol.722 , pp. 381-391
    • Gellerich, F.N.1    Bohnensack, R.2    Kunz, W.3
  • 17
    • 0020490497 scopus 로고
    • Quantification of the contribution of various steps to the control of mitochondrial respiration
    • Groen A. K., Wanders R. J. A., Westerhoff H. V., van der Meer R., and Tager T. M. (1982) Quantification of the contribution of various steps to the control of mitochondrial respiration. J. Biol. Chem. 257, 2754-2757.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2754-2757
    • Groen, A.K.1    Wanders, R.J.A.2    Westerhoff, H.V.3    Van Der Meer, R.4    Tager, T.M.5
  • 18
    • 0023222894 scopus 로고
    • Age dependent changes in rat brain mitochondria of synaptic and non-synaptic origins
    • Harmon H. J., Nank S., and Floyd R. A. (1987) Age dependent changes in rat brain mitochondria of synaptic and non-synaptic origins. Mech. Ageing Dev. 38, 167-177.
    • (1987) Mech. Ageing Dev. , vol.38 , pp. 167-177
    • Harmon, H.J.1    Nank, S.2    Floyd, R.A.3
  • 19
    • 0024997609 scopus 로고
    • +) induces NADH dependent superoxide formation, and enhances NADH-dependent lipid peroxidation in bovine heart submitochondrial particles
    • +) induces NADH dependent superoxide formation, and enhances NADH-dependent lipid peroxidation in bovine heart submitochondrial particles. Biochem. Biophys. Res. Commun. 170, 1049-1055.
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 1049-1055
    • Hasegawa, E.1    Takeshige, K.2    Oishi, T.3    Murai, Y.4    Minikami, S.5
  • 20
    • 0015989446 scopus 로고
    • A linear steady-state treatment of enzymatic chains
    • Heinrich R. and Rapoport T. A. (1974) A linear steady-state treatment of enzymatic chains. Eur. J. Biochem. 42, 89-95.
    • (1974) Eur. J. Biochem. , vol.42 , pp. 89-95
    • Heinrich, R.1    Rapoport, T.A.2
  • 21
    • 0020329051 scopus 로고
    • Determination of adenine nucleotides and inosine in human myocardium by ion-pair reversed-phased high-performance liquid chromatography
    • Ingebrotsen O. C., Bakken A. M., Segadal L., and Farstad M. (1982) Determination of adenine nucleotides and inosine in human myocardium by ion-pair reversed-phased high-performance liquid chromatography. J. Chromatogr. 242, 119-126.
    • (1982) J. Chromatogr. , vol.242 , pp. 119-126
    • Ingebrotsen, O.C.1    Bakken, A.M.2    Segadal, L.3    Farstad, M.4
  • 23
    • 0015824267 scopus 로고
    • The control of flux
    • (Davies D. D., ed), Cambridge University Press, Cambridge
    • Kacser H. and Burns J. A. (1973) The control of flux, in Rate Control of Biological Processes (Davies D. D., ed), pp. 65-104. Cambridge University Press, Cambridge.
    • (1973) Rate Control of Biological Processes , pp. 65-104
    • Kacser, H.1    Burns, J.A.2
  • 25
    • 0018338308 scopus 로고
    • Preparation of synaptic and non-synaptic mitochondria from mammalian brain
    • (Fleischer S. and Packer L., eds), Academic Press, New York
    • Lai C. K. and Clark J. B. (1979) Preparation of synaptic and non-synaptic mitochondria from mammalian brain, in Methods in Enzymology, Vol. 55 (Fleischer S. and Packer L., eds), pp. 51-60. Academic Press, New York.
    • (1979) Methods in Enzymology , vol.55 , pp. 51-60
    • Lai, C.K.1    Clark, J.B.2
  • 26
    • 0025047351 scopus 로고
    • Normal mitochondrial genome in brain from patients with Parkinson's disease and complex I defect
    • Lestienne P., Nelson I., Riederer P., Jellinger K , and Reichmann H. (1990) Normal mitochondrial genome in brain from patients with Parkinson's disease and complex I defect. J Neurochem. 55, 1810-1812.
    • (1990) J Neurochem. , vol.55 , pp. 1810-1812
    • Lestienne, P.1    Nelson, I.2    Riederer, P.3    Jellinger, K.4    Reichmann, H.5
  • 27
  • 28
    • 0027932783 scopus 로고
    • The kinetics of threshold effects observed in mitochondrial diseases: A systemic approach
    • Letellier T., Heinrich R., Malgat M., and Mazat J. P. (1994) The kinetics of threshold effects observed in mitochondrial diseases: a systemic approach. Biochem. J. 302, 171-174.
    • (1994) Biochem. J. , vol.302 , pp. 171-174
    • Letellier, T.1    Heinrich, R.2    Malgat, M.3    Mazat, J.P.4
  • 30
    • 0000765915 scopus 로고
    • Value of control theory in the study of cellular metabolism - Biomedical implications
    • Malgat M., Letellier T., Jouvaille S. L., and Mazat J. P. (1995) Value of control theory in the study of cellular metabolism - biomedical implications. J. Biol. Systems 3, 165-175.
    • (1995) J. Biol. Systems , vol.3 , pp. 165-175
    • Malgat, M.1    Letellier, T.2    Jouvaille, S.L.3    Mazat, J.P.4
  • 33
    • 0025952644 scopus 로고
    • Distribution of control of oxidative phosphorylation in mitochondria oxidizing NAD-linked substrates
    • Moreno-Sanchez R , Devars S., Lopez-Gomez F., Uribe A., and Corona N. (1991) Distribution of control of oxidative phosphorylation in mitochondria oxidizing NAD-linked substrates. Biochim. Biophys. Acta 1060, 284-292.
    • (1991) Biochim. Biophys. Acta , vol.1060 , pp. 284-292
    • Moreno-Sanchez, R.1    Devars, S.2    Lopez-Gomez, F.3    Uribe, A.4    Corona, N.5
  • 34
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase is reduced in Alzheimer's disease
    • Mutisya E. M , Bowling A. C., and Beal M. F. (1994) Cortical cytochrome oxidase is reduced in Alzheimer's disease. J. Neurochem. 63, 2179-2184.
    • (1994) J. Neurochem. , vol.63 , pp. 2179-2184
    • Mutisya, E.M.1    Bowling, A.C.2    Beal, M.F.3
  • 35
    • 0025149002 scopus 로고
    • Quantitative-determination of deleted mitochondrial-DNA relative to normal DNA in parkinsonian striatum by a kinetic PCR analysis
    • Ozawa T., Tanaka M., Ikebe S., Ohno K., Kondon T., and Mizuno Y. (1990) Quantitative-determination of deleted mitochondrial-DNA relative to normal DNA in parkinsonian striatum by a kinetic PCR analysis. Biochem. Biophys. Res. Commun. 172, 483-489.
    • (1990) Biochem. Biophys. Res. Commun. , vol.172 , pp. 483-489
    • Ozawa, T.1    Tanaka, M.2    Ikebe, S.3    Ohno, K.4    Kondon, T.5    Mizuno, Y.6
  • 36
    • 0001889165 scopus 로고
    • Subfractionation of mitochondria and isolation of the proteins of oxidative phosphorylation
    • (Darley-Usmar V. M., Rickwood D., and Wilson M. T., eds), IRL Press, London
    • Ragan C. I., Wilson M. T., Darley-Usmar V. M., and Lowe P. N. (1987) Subfractionation of mitochondria and isolation of the proteins of oxidative phosphorylation, in Mitochondria, A Practical Approach (Darley-Usmar V. M., Rickwood D., and Wilson M. T., eds), pp. 79-112. IRL Press, London.
    • (1987) Mitochondria, a Practical Approach , pp. 79-112
    • Ragan, C.I.1    Wilson, M.T.2    Darley-Usmar, V.M.3    Lowe, P.N.4
  • 43
    • 0028107084 scopus 로고
    • The control of mitochondrial oxidations by complex III in rat muscle and liver mitochondria
    • Taylor R. W., Birch-Machin M. A., Bartlett K., Lowerson S. A., and Turnbull D. M. (1994) The control of mitochondrial oxidations by complex III in rat muscle and liver mitochondria. J. Biol. Chem. 269, 3523-3528.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3523-3528
    • Taylor, R.W.1    Birch-Machin, M.A.2    Bartlett, K.3    Lowerson, S.A.4    Turnbull, D.M.5
  • 44
    • 0029055587 scopus 로고
    • Might environmental factors contribute to neurodegenerative diseases?
    • Tipton K. F. (1995) Might environmental factors contribute to neurodegenerative diseases? Biochem. Soc. Trans. 23, 429-435.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 429-435
    • Tipton, K.F.1
  • 45
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens J. F. and Boveris A. (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
  • 46
    • 2042432480 scopus 로고
    • Cytochrome oxidase from beef heart mitochondria
    • Wharton D. C. and Tzagoloff A. (1967) Cytochrome oxidase from beef heart mitochondria. Methods Enzymol. 10, 245-250.
    • (1967) Methods Enzymol. , vol.10 , pp. 245-250
    • Wharton, D.C.1    Tzagoloff, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.