메뉴 건너뛰기




Volumn 1658, Issue 1-2, 2004, Pages 89-94

Bioenergetics of mitochondrial diseases associated with mtDNA mutations

Author keywords

ATP synthase; Complex I; Cytochrome oxidase subunit III; LHON; Mitochondrial cytopathy; NARP

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CYTOCHROME C OXIDASE; MITOCHONDRIAL DNA; REACTIVE OXYGEN METABOLITE;

EID: 3543045616     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.03.013     Document Type: Review
Times cited : (93)

References (44)
  • 2
    • 0033040309 scopus 로고    scopus 로고
    • Mitochondrial encephalomyopathies: The enigma of genotype versus phenotype
    • Morgan-Hughes J.A., Hanna M.G. Mitochondrial encephalomyopathies: the enigma of genotype versus phenotype. Biochim. Biophys. Acta. 1410:1999;125-145
    • (1999) Biochim. Biophys. Acta , vol.1410 , pp. 125-145
    • Morgan-Hughes, J.A.1    Hanna, M.G.2
  • 3
    • 0035824814 scopus 로고    scopus 로고
    • A critical appraisal of the mitochondrial Coenzyme Q pool
    • Lenaz G. A critical appraisal of the mitochondrial Coenzyme Q pool. FEBS Lett. 509:2001;151-155
    • (2001) FEBS Lett. , vol.509 , pp. 151-155
    • Lenaz, G.1
  • 4
    • 0036139856 scopus 로고    scopus 로고
    • The mitochondrial production of reactive oxygen species: Mechanisms and implications in human pathology
    • Lenaz G. The mitochondrial production of reactive oxygen species: mechanisms and implications in human pathology. IUBMB Life. 52:2001;159-164
    • (2001) IUBMB Life , vol.52 , pp. 159-164
    • Lenaz, G.1
  • 5
    • 0037406049 scopus 로고    scopus 로고
    • Pathogenic expression of homoplasmic mtDNA mutations needs a complex nuclear-mitochondrial interaction
    • Carelli V., Giordano C., D'Amati G. Pathogenic expression of homoplasmic mtDNA mutations needs a complex nuclear-mitochondrial interaction. Trends Genet. 19:2003;257-262
    • (2003) Trends Genet. , vol.19 , pp. 257-262
    • Carelli, V.1    Giordano, C.2    D'Amati, G.3
  • 6
    • 0024448458 scopus 로고
    • Human cells lacking mtDNA: Repopulation with exogenous mitochondria by complementation
    • King M.P., Attardi G. Human cells lacking mtDNA: repopulation with exogenous mitochondria by complementation. Science. 246:1989;500-503
    • (1989) Science , vol.246 , pp. 500-503
    • King, M.P.1    Attardi, G.2
  • 7
    • 77957170634 scopus 로고    scopus 로고
    • Leber's hereditary optic neuropathy
    • A.H.V. Schapira, & S. Di Mauro. Boston: Butterworth-Heinemann
    • Carelli V. Leber's hereditary optic neuropathy. Schapira A.H.V., Di Mauro S. Mitochondrial Disorders in Neurology. 2nd ed.:2002;115-142 Butterworth-Heinemann, Boston
    • (2002) Mitochondrial Disorders in Neurology 2nd Ed. , pp. 115-142
    • Carelli, V.1
  • 9
    • 0033137153 scopus 로고    scopus 로고
    • The enigmatic relationship between mitochondrial dysfunction and Leber's hereditary optic neruopathy
    • Brown M.D. The enigmatic relationship between mitochondrial dysfunction and Leber's hereditary optic neruopathy. J. Neurol. Sci. 165:1999;1-5
    • (1999) J. Neurol. Sci. , vol.165 , pp. 1-5
    • Brown, M.D.1
  • 11
    • 0025995774 scopus 로고
    • Electron transfer properties of NADH:ubiquinone reductase in the ND1/3460 and the ND4/11778 mutations of the Leber hereditary optic neuroretinopathy (LHON)
    • Majander A., Huoponen K., Savontaus M.-L., Nikoskelainen E.K., Wikstrom M. Electron transfer properties of NADH:ubiquinone reductase in the ND1/3460 and the ND4/11778 mutations of the Leber hereditary optic neuroretinopathy (LHON). FEBS Lett. 292:1991;289-292
    • (1991) FEBS Lett. , vol.292 , pp. 289-292
    • Majander, A.1    Huoponen, K.2    Savontaus, M.-L.3    Nikoskelainen, E.K.4    Wikstrom, M.5
  • 14
    • 0028858473 scopus 로고
    • The 14484 ND6 mtDNA mutation in Leber hereditary optic neuropathy does not affect fibroblast complex I activity
    • Cock H.R., Cooper J.M., Schapira A.H.V. The 14484 ND6 mtDNA mutation in Leber hereditary optic neuropathy does not affect fibroblast complex I activity. Am. J. Hum. Genet. 57:1995;1501-1502
    • (1995) Am. J. Hum. Genet. , vol.57 , pp. 1501-1502
    • Cock, H.R.1    Cooper, J.M.2    Schapira, A.H.V.3
  • 15
    • 0029953887 scopus 로고    scopus 로고
    • Catalytic activity of complex I in cell lines that possess replacement mutations in the ND genes in Leber's hereditary optic neuropathy
    • Majander A., Finel M., Savontaus M.-L., Nikoskelainen E., Wikstrom M. Catalytic activity of complex I in cell lines that possess replacement mutations in the ND genes in Leber's hereditary optic neuropathy. Eur. J. Biochem. 239:1996;201-207
    • (1996) Eur. J. Biochem. , vol.239 , pp. 201-207
    • Majander, A.1    Finel, M.2    Savontaus, M.-L.3    Nikoskelainen, E.4    Wikstrom, M.5
  • 16
    • 0030823106 scopus 로고    scopus 로고
    • Changes in mitochondrial complex I activity and Coenzyme Q binding site in Leber's hereditary optic neuropathy (LHON)
    • Ghelli A., Degli Esposti M., Carelli V., Lenaz G. Changes in mitochondrial complex I activity and Coenzyme Q binding site in Leber's hereditary optic neuropathy (LHON). Mol. Aspects Med. 18:1997;263-267
    • (1997) Mol. Aspects Med. , vol.18 , pp. 263-267
    • Ghelli, A.1    Degli Esposti, M.2    Carelli, V.3    Lenaz, G.4
  • 18
    • 0030056515 scopus 로고    scopus 로고
    • Mitochondrial complex I deficiency leads to increased production of superoxide radicals and induction of superoxide dismutase
    • Pitkänen S., Robinson B.H. Mitochondrial complex I deficiency leads to increased production of superoxide radicals and induction of superoxide dismutase. J. Clin. Invest. 98:1996;345-351
    • (1996) J. Clin. Invest. , vol.98 , pp. 345-351
    • Pitkänen, S.1    Robinson, B.H.2
  • 19
    • 0036182712 scopus 로고    scopus 로고
    • Optic nerve degeneration and mitochondrial dysfunction: Genetic and acquired optic neuropathies
    • Carelli V., Ross-Cisneros F.N., Sadun A.A. Optic nerve degeneration and mitochondrial dysfunction: genetic and acquired optic neuropathies. Neurochem. Int. 40:2002;573-584
    • (2002) Neurochem. Int. , vol.40 , pp. 573-584
    • Carelli, V.1    Ross-Cisneros, F.N.2    Sadun, A.A.3
  • 20
    • 0035929367 scopus 로고    scopus 로고
    • The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron-sulfur cluster N2
    • Genova M.L., Ventura B., Giuliano G., Bovina C., Formiggini G., Parenti Castelli G., Lenaz G. The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron-sulfur cluster N2. FEBS Lett. 505:2001;364-368
    • (2001) FEBS Lett. , vol.505 , pp. 364-368
    • Genova, M.L.1    Ventura, B.2    Giuliano, G.3    Bovina, C.4    Formiggini, G.5    Parenti Castelli, G.6    Lenaz, G.7
  • 21
    • 0036319021 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the mitochondrial electron transfer chain
    • Liu Y., Fiskum G., Schubert D. Generation of reactive oxygen species by the mitochondrial electron transfer chain. J. Neurochem. 80:2002;780-787
    • (2002) J. Neurochem. , vol.80 , pp. 780-787
    • Liu, Y.1    Fiskum, G.2    Schubert, D.3
  • 22
    • 0036903625 scopus 로고    scopus 로고
    • Complex I-mediated reactive oxygen species generation: Modulation by cytochrome c and NAD(P)+ oxidation-reduction state
    • Kushnareva Y., Murphy A.N., Andreyev A. Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation-reduction state. Biochem. J. 368:2002;545-553
    • (2002) Biochem. J. , vol.368 , pp. 545-553
    • Kushnareva, Y.1    Murphy, A.N.2    Andreyev, A.3
  • 23
    • 0033522924 scopus 로고    scopus 로고
    • Titrating the effects of mitochondrial complex I impairment in the cell physiology
    • Barrientos A., Moraes C.T. Titrating the effects of mitochondrial complex I impairment in the cell physiology. J. Biol. Chem. 274:1999;16188-16197
    • (1999) J. Biol. Chem. , vol.274 , pp. 16188-16197
    • Barrientos, A.1    Moraes, C.T.2
  • 24
    • 0037423202 scopus 로고    scopus 로고
    • Leber's hereditary optic neuropathy (LHON) pathogenic mutations induce mitochondrial-dependent apoptotic death in transmitochondrial cells incubated with galactose medium
    • Ghelli, Zanna C., Porcelli A.M., Schapira A.H.V., Martinuzzi A., Carelli V., Rugolo M. Leber's hereditary optic neuropathy (LHON) pathogenic mutations induce mitochondrial-dependent apoptotic death in transmitochondrial cells incubated with galactose medium. J. Biol. Chem. 278:2003;4145-4150
    • (2003) J. Biol. Chem. , vol.278 , pp. 4145-4150
    • Ghelli1    Zanna, C.2    Porcelli, A.M.3    Schapira, A.H.V.4    Martinuzzi, A.5    Carelli, V.6    Rugolo, M.7
  • 25
  • 27
    • 0027451284 scopus 로고
    • The mutation at 8993 of mitochondrial DNA is a common cause of Leigh syndrome
    • Santorelli F.M., Shanske S., Macaya A., DeVivo D.C., Di Mauro S. The mutation at 8993 of mitochondrial DNA is a common cause of Leigh syndrome. Ann. Neurol. 34:1993;827-834
    • (1993) Ann. Neurol. , vol.34 , pp. 827-834
    • Santorelli, F.M.1    Shanske, S.2    MacAya, A.3    Devivo, D.C.4    Di Mauro, S.5
  • 28
    • 0034635388 scopus 로고    scopus 로고
    • Catalytic activities of mitochondrial ATP synthase in patients with mitochondrial DNA T8993G mutation in the ATPase-6 gene encoding subunit a
    • Baracca A., Barogi S., Carelli V., Lenaz G., Solaini G. Catalytic activities of mitochondrial ATP synthase in patients with mitochondrial DNA T8993G mutation in the ATPase-6 gene encoding subunit a. J. Biol. Chem. 275:2000;4177-4182
    • (2000) J. Biol. Chem. , vol.275 , pp. 4177-4182
    • Baracca, A.1    Barogi, S.2    Carelli, V.3    Lenaz, G.4    Solaini, G.5
  • 30
    • 0028936818 scopus 로고
    • Correlation between the clinical symptoms and the proportion of mitochondrial DNA carrying the 8993 mtDNA mutation in the NARP syndrome
    • Makela-Bengs P., Suomalainen A., Majander A., Rapola J., Kalimo H., Nuutila A., Pihko H. Correlation between the clinical symptoms and the proportion of mitochondrial DNA carrying the 8993 mtDNA mutation in the NARP syndrome. Pediatr. Res. 37:1995;634-639
    • (1995) Pediatr. Res. , vol.37 , pp. 634-639
    • Makela-Bengs, P.1    Suomalainen, A.2    Majander, A.3    Rapola, J.4    Kalimo, H.5    Nuutila, A.6    Pihko, H.7
  • 31
    • 0030749664 scopus 로고    scopus 로고
    • Mitochondrial disease associated with the T8993G mutation of the mitochondrial ATPase 6 gene: A clinical, biochemical and molecular study of six families
    • Uziel G., Moroni I., Lamantea E., Fratta G.M., Ciceri E., Carrara F., Zeviani M. Mitochondrial disease associated with the T8993G mutation of the mitochondrial ATPase 6 gene: a clinical, biochemical and molecular study of six families. J. Neurol. Neurosurg. Psychiatry. 63:1997;16-22
    • (1997) J. Neurol. Neurosurg. Psychiatry , vol.63 , pp. 16-22
    • Uziel, G.1    Moroni, I.2    Lamantea, E.3    Fratta, G.M.4    Ciceri, E.5    Carrara, F.6    Zeviani, M.7
  • 32
    • 0142042958 scopus 로고    scopus 로고
    • Rhodamine 123 as a probe of mitochondrial membrane potential: Evaluation of proton flux through Fo during ATP synthesis
    • Baracca A., Sgarbi G., Solaini G., Lenaz G. Rhodamine 123 as a probe of mitochondrial membrane potential: evaluation of proton flux through Fo during ATP synthesis. Biochim. Biophys. Acta. 1606:2003;137-146
    • (2003) Biochim. Biophys. Acta , vol.1606 , pp. 137-146
    • Baracca, A.1    Sgarbi, G.2    Solaini, G.3    Lenaz, G.4
  • 33
    • 0029765443 scopus 로고    scopus 로고
    • Role of uncoupled and non-coupled oxidations in maintainance of safely low levels of oxygen and its one-electron reductants
    • Skulachev V.P. Role of uncoupled and non-coupled oxidations in maintainance of safely low levels of oxygen and its one-electron reductants. Q. Rev. Biophys. 29:1996;169-202
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 169-202
    • Skulachev, V.P.1
  • 35
    • 0038352169 scopus 로고    scopus 로고
    • Site-specific antibodies against hydrophilic domains of subunit III of bovine heart cytochrome c oxidase affect enzyme function
    • Lincoln A.J., Donat N., Palmer G., Prochaska L.J. Site-specific antibodies against hydrophilic domains of subunit III of bovine heart cytochrome c oxidase affect enzyme function. Arch. Biochem. Biophys. 416:2003;81-91
    • (2003) Arch. Biochem. Biophys. , vol.416 , pp. 81-91
    • Lincoln, A.J.1    Donat, N.2    Palmer, G.3    Prochaska, L.J.4
  • 36
    • 0031812281 scopus 로고    scopus 로고
    • Intrinsic uncoupling of cytochrome c oxidase may cause the maternally inherited mitochondrial diseases MELAS and LHON
    • Mather M.W., Rottenberg H. Intrinsic uncoupling of cytochrome c oxidase may cause the maternally inherited mitochondrial diseases MELAS and LHON. FEBS Lett. 433:1998;93-97
    • (1998) FEBS Lett. , vol.433 , pp. 93-97
    • Mather, M.W.1    Rottenberg, H.2
  • 37
    • 0038408885 scopus 로고    scopus 로고
    • Subunit III of cytochrome c oxidase of Rhodobacter sphaeroides is required to maintain rapid proton uptake through the D pathway at physiologic pH
    • Gilderson G., Salomonsson L., Aagard A., Gray J., Brzezinski P., Hosler J. Subunit III of cytochrome c oxidase of Rhodobacter sphaeroides is required to maintain rapid proton uptake through the D pathway at physiologic pH. Biochemistry. 42:2003;7400-7409
    • (2003) Biochemistry , vol.42 , pp. 7400-7409
    • Gilderson, G.1    Salomonsson, L.2    Aagard, A.3    Gray, J.4    Brzezinski, P.5    Hosler, J.6
  • 38
    • 0037790647 scopus 로고    scopus 로고
    • A role of subunit III in proton uptake into the D pathway and a possible proton exit pathway in Rhodobacter sphaeroides cytochrome c oxidase
    • Mills D.A., Tan Z., Ferguson-Miller S., Hosler J. A role of subunit III in proton uptake into the D pathway and a possible proton exit pathway in Rhodobacter sphaeroides cytochrome c oxidase. Biochemistry. 42:2003;7410-7417
    • (2003) Biochemistry , vol.42 , pp. 7410-7417
    • Mills, D.A.1    Tan, Z.2    Ferguson-Miller, S.3    Hosler, J.4
  • 39
    • 0025879301 scopus 로고
    • Subunit III of cytochrome c oxidase is not involved in proton trasnlocation: A site-directed mutagenesis study
    • Haltia T., Saraste M.M.W. Subunit III of cytochrome c oxidase is not involved in proton trasnlocation: a site-directed mutagenesis study. EMBO J. 10:1991;2015-2021
    • (1991) EMBO J. , vol.10 , pp. 2015-2021
    • Haltia, T.1    Saraste, M.M.W.2
  • 40
    • 0034327415 scopus 로고    scopus 로고
    • A novel frameshift mutation of the mtDNA COIII gene leads to impaired assembly of cytochrome c oxidase in a patient affected by Leigh-like syndrome
    • Tiranti V., Corona P., Greco M., Taanman J.-W., Carrara F., Lamantea E., Nijtmans L., Uziel G., Zeviani M. A novel frameshift mutation of the mtDNA COIII gene leads to impaired assembly of cytochrome c oxidase in a patient affected by Leigh-like syndrome. Hum. Mol. Genet. 18:2000;2733-2742
    • (2000) Hum. Mol. Genet. , vol.18 , pp. 2733-2742
    • Tiranti, V.1    Corona, P.2    Greco, M.3    Taanman, J.-W.4    Carrara, F.5    Lamantea, E.6    Nijtmans, L.7    Uziel, G.8    Zeviani, M.9
  • 41
    • 0034607651 scopus 로고    scopus 로고
    • A pathogenic 15-base pair deletion in mitochondrial DNA-encoded cytochrome c oxidase subunit III results in the absence of functional cytochrome c oxidase
    • Hoffbuhr K.C., Davidson E., Filiano B.A., Davidson M., Kennaway N.G., King M.P. A pathogenic 15-base pair deletion in mitochondrial DNA-encoded cytochrome c oxidase subunit III results in the absence of functional cytochrome c oxidase. J. Biol. Chem. 575:2000;13994-14003
    • (2000) J. Biol. Chem. , vol.575 , pp. 13994-14003
    • Hoffbuhr, K.C.1    Davidson, E.2    Filiano, B.A.3    Davidson, M.4    Kennaway, N.G.5    King, M.P.6
  • 43
    • 0035281645 scopus 로고    scopus 로고
    • Site-directed mutations in the mitochondrially encoded subunits I and III of yeast cytochrome oxidase
    • Meunier B. Site-directed mutations in the mitochondrially encoded subunits I and III of yeast cytochrome oxidase. Biochem. J. 354:2001;407-412
    • (2001) Biochem. J. , vol.354 , pp. 407-412
    • Meunier, B.1
  • 44
    • 0033858360 scopus 로고    scopus 로고
    • The contribution of mitochondrial respiratory complexes to the production of reactive oxygen species
    • McLennan H.R., Degli Esposti M. The contribution of mitochondrial respiratory complexes to the production of reactive oxygen species. J. Bioenerg. Biomembranes. 32:2000;153-162
    • (2000) J. Bioenerg. Biomembranes , vol.32 , pp. 153-162
    • McLennan, H.R.1    Degli Esposti, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.