메뉴 건너뛰기




Volumn 1659, Issue 2-3, 2004, Pages 232-239

Strategies for treating disorders of the mitochondrial genome

Author keywords

Alloptic expression; Antigenomic hypothesis; Mithocondrial tRNA import; mtDNA disease; Treatment of mtDNA disease

Indexed keywords

DNA;

EID: 9644307915     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.09.003     Document Type: Conference Paper
Times cited : (28)

References (56)
  • 1
    • 0042422222 scopus 로고    scopus 로고
    • Nutritional cofactor treatment in mitochondrial disorders
    • B. Marriage, M.T. Clandinin, and D.M. Glerum Nutritional cofactor treatment in mitochondrial disorders J. Am. Diet. Assoc. 103 2003 1029 1038
    • (2003) J. Am. Diet. Assoc. , vol.103 , pp. 1029-1038
    • Marriage, B.1    Clandinin, M.T.2    Glerum, D.M.3
  • 2
    • 1842469055 scopus 로고    scopus 로고
    • Nutritional and exercise-based therapies in the treatment of mitochondrial disease
    • D.J. Mahoney, G. Parise, and M.A. Tarnopolsky Nutritional and exercise-based therapies in the treatment of mitochondrial disease Curr. Opin. Clin. Nutr. Metab. Care 5 2002 619 629
    • (2002) Curr. Opin. Clin. Nutr. Metab. Care , vol.5 , pp. 619-629
    • Mahoney, D.J.1    Parise, G.2    Tarnopolsky, M.A.3
  • 4
    • 0024121557 scopus 로고
    • Assembly of functional proton-translocating ATPase complex in yeast mitochondria with cytoplasmically synthesised subunit 8, a polypeptide normally encoded by the organelle
    • P. Nagley, L.B. Farrell, D.P. Gearing, D. Nero, S. Meltzer, and R.J. Devenish Assembly of functional proton-translocating ATPase complex in yeast mitochondria with cytoplasmically synthesised subunit 8, a polypeptide normally encoded by the organelle Proc. Natl. Acad. Sci. 85 1988 2091 2095
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 2091-2095
    • Nagley, P.1    Farrell, L.B.2    Gearing, D.P.3    Nero, D.4    Meltzer, S.5    Devenish, R.J.6
  • 5
    • 0036544631 scopus 로고    scopus 로고
    • Rescue of a deficiency in ATP synthesis by transfer of MTATP6, a mitochondrial DNA-encoded gene, to the nucleus
    • G. Manfredi, J. Fu, J. Ojaimi, J.E. Sadlock, J.Q. Kwong, J. Guy, and E.A. Schon Rescue of a deficiency in ATP synthesis by transfer of MTATP6, a mitochondrial DNA-encoded gene, to the nucleus Nat. Genet. 30 2002 394 399
    • (2002) Nat. Genet. , vol.30 , pp. 394-399
    • Manfredi, G.1    Fu, J.2    Ojaimi, J.3    Sadlock, J.E.4    Kwong, J.Q.5    Guy, J.6    Schon, E.A.7
  • 6
    • 0036544881 scopus 로고    scopus 로고
    • A roundabout route to gene therapy
    • D.M. Turnbull, and R.N. Lightowlers A roundabout route to gene therapy Nat. Genet. 30 2002 345 346
    • (2002) Nat. Genet. , vol.30 , pp. 345-346
    • Turnbull, D.M.1    Lightowlers, R.N.2
  • 8
    • 0242349697 scopus 로고    scopus 로고
    • Limitations of allotopic expression of mitochondrial genes in mammalian cells
    • J. Oca-Cossio, L. Kenyon, H. Hao, and C.T. Moraes Limitations of allotopic expression of mitochondrial genes in mammalian cells Genetics 165 2003 707 720
    • (2003) Genetics , vol.165 , pp. 707-720
    • Oca-Cossio, J.1    Kenyon, L.2    Hao, H.3    Moraes, C.T.4
  • 9
    • 0028932673 scopus 로고
    • Limitations to in vivo import of hydrophobic proteins into yeast mitochondria. The case of a cytoplasmically synthesized apocytochrome b
    • M.G. Claros, J. Perea, Y. Shu, F.A. Samatey, J.L. Popot, and C. Jacq Limitations to in vivo import of hydrophobic proteins into yeast mitochondria. The case of a cytoplasmically synthesized apocytochrome b Eur. J. Biochem. 228 1995 762 771
    • (1995) Eur. J. Biochem. , vol.228 , pp. 762-771
    • Claros, M.G.1    Perea, J.2    Shu, Y.3    Samatey, F.A.4    Popot, J.L.5    Jacq, C.6
  • 10
    • 0036855408 scopus 로고    scopus 로고
    • An algal nucleus-encoded subunit of mitochondrial ATP synthase rescues a defect in the analogous human mitochondrial-encoded subunit
    • J. Ojaimi, J. Pan, S. Santra, W.J. Snell, and E.A. Schon An algal nucleus-encoded subunit of mitochondrial ATP synthase rescues a defect in the analogous human mitochondrial-encoded subunit Mol. Biol. Cell 13 2002 3836 3844
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3836-3844
    • Ojaimi, J.1    Pan, J.2    Santra, S.3    Snell, W.J.4    Schon, E.A.5
  • 11
    • 0024288671 scopus 로고
    • Purification and characterization of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae
    • S. de Vries, and L.A. Grivell Purification and characterization of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae. Eur. J. Biochem. 176 1988 377 384
    • (1988) Eur. J. Biochem. , vol.176 , pp. 377-384
    • De Vries, S.1    Grivell, L.A.2
  • 12
    • 0034531991 scopus 로고    scopus 로고
    • Use of the NADH-quinone oxidoreductase (NDI1) gene of Saccharomyces cerevisiae as a possible cure for complex I defects in human cells
    • B. Seo, J. Wang, T. Flotte, T. Yagi, and A. Matsuno-Yagi Use of the NADH-quinone oxidoreductase (NDI1) gene of Saccharomyces cerevisiae as a possible cure for complex I defects in human cells J. Biol. Chem. 275 2000 37774 37778
    • (2000) J. Biol. Chem. , vol.275 , pp. 37774-37778
    • Seo, B.1    Wang, J.2    Flotte, T.3    Yagi, T.4    Matsuno-Yagi, A.5
  • 13
    • 0036764928 scopus 로고    scopus 로고
    • A single-subunit NADH-quinone oxidoreductase renders resistance to mammalian nerve cells against complex I inhibition
    • B.B. Seo, E. Nakamaru-Ogiso, T.R. Flotte, T. Yagi, and A. Matsuno-Yagi A single-subunit NADH-quinone oxidoreductase renders resistance to mammalian nerve cells against complex I inhibition Molec. Ther. 6 2002 336 341
    • (2002) Molec. Ther. , vol.6 , pp. 336-341
    • Seo, B.B.1    Nakamaru-Ogiso, E.2    Flotte, T.R.3    Yagi, T.4    Matsuno-Yagi, A.5
  • 14
    • 0035914437 scopus 로고    scopus 로고
    • Lack of complex I activity in human cells carrying a mutation in mtDNA encoded ND4 subunit is corrected by the Saccharomyces cerevisiae NADH-quinone oxidoreductase (NDI1) gene
    • Y. Bai, P. Hajek, A. Chomyn, E. Chan, B. Seo, A. Matsuno-Yagi, T. Yagi, and G. Attardi Lack of complex I activity in human cells carrying a mutation in mtDNA encoded ND4 subunit is corrected by the Saccharomyces cerevisiae NADH-quinone oxidoreductase (NDI1) gene J. Biol. Chem. 276 2001 38808 38813
    • (2001) J. Biol. Chem. , vol.276 , pp. 38808-38813
    • Bai, Y.1    Hajek, P.2    Chomyn, A.3    Chan, E.4    Seo, B.5    Matsuno-Yagi, A.6    Yagi, T.7    Attardi, G.8
  • 16
    • 0029853167 scopus 로고    scopus 로고
    • Striking differences in mitochondrial tRNA import between different plant species
    • R. Kumar, L. Marechal-Drouard, K. Akama, and I. Small Striking differences in mitochondrial tRNA import between different plant species Mol. Gen. Genet. 252 1996 404 411
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 404-411
    • Kumar, R.1    Marechal-Drouard, L.2    Akama, K.3    Small, I.4
  • 17
    • 0034578344 scopus 로고    scopus 로고
    • Mitochondrial tRNA import: Are there distinct mechanisms?
    • A. Schneider, and L. Marechal-Drouard Mitochondrial tRNA import: are there distinct mechanisms? Trends Cell Biol. 10 2000 509 513
    • (2000) Trends Cell Biol. , vol.10 , pp. 509-513
    • Schneider, A.1    Marechal-Drouard, L.2
  • 18
    • 0035808426 scopus 로고    scopus 로고
    • Identification and structural characterization of nucleus-encoded transfer RNAs imported into wheat mitochondria
    • K.E. Glover, D.F. Spencer, and M.W. Gray Identification and structural characterization of nucleus-encoded transfer RNAs imported into wheat mitochondria J. Biol. Chem. 276 2001 639 648
    • (2001) J. Biol. Chem. , vol.276 , pp. 639-648
    • Glover, K.E.1    Spencer, D.F.2    Gray, M.W.3
  • 19
  • 22
    • 0035159226 scopus 로고    scopus 로고
    • The RNase P associated wih HeLa cell mitochondria contains an essential RNA component identical in sequence to that of the nuclear RNase P
    • R.S. Puranam, and G. Attardi The RNase P associated wih HeLa cell mitochondria contains an essential RNA component identical in sequence to that of the nuclear RNase P Mol. Cell. Biol. 21 2001 548 561
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 548-561
    • Puranam, R.S.1    Attardi, G.2
  • 23
    • 0031690491 scopus 로고    scopus 로고
    • Evidence for the presence of 5S rRNA in mammalian mitochondria
    • P. Magalhaes, A. Andreu, and E.A. Schon Evidence for the presence of 5S rRNA in mammalian mitochondria Mol. Biol. Cell. 9 1998 2375 2382
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 2375-2382
    • Magalhaes, P.1    Andreu, A.2    Schon, E.A.3
  • 27
    • 0029658242 scopus 로고    scopus 로고
    • A novel heteroplasmic tRNAleu(CUN) mtDNA point mutation in a sporadic patient with mitochondrial encephalomyopathy segregates rapidly in skeletal muscle and suggests an approach to therapy
    • K. Fu, R. Hartlen, T. Johns, A. Genge, G. Karpati, and E.A. Shoubridge A novel heteroplasmic tRNAleu(CUN) mtDNA point mutation in a sporadic patient with mitochondrial encephalomyopathy segregates rapidly in skeletal muscle and suggests an approach to therapy Hum. Mol. Genet. 5 1996 1835 1840
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1835-1840
    • Fu, K.1    Hartlen, R.2    Johns, T.3    Genge, A.4    Karpati, G.5    Shoubridge, E.A.6
  • 29
    • 0035894698 scopus 로고    scopus 로고
    • Manipulating mitochondrial DNA heteroplasmy by a mitochondrially-targeted endonuclease
    • S. Srivastava, and C. Moraes Manipulating mitochondrial DNA heteroplasmy by a mitochondrially-targeted endonuclease Hum. Mol. Genet. 10 2001 3093 3099
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 3093-3099
    • Srivastava, S.1    Moraes, C.2
  • 30
    • 9644269261 scopus 로고    scopus 로고
    • Shifting mitochondrial DNA heteroplasmy by mitochondrially targeted restriction endonucleases
    • M. Bayona, B. Blits, B. Battersby, E. Shoubridge, and C. Moraes Shifting mitochondrial DNA heteroplasmy by mitochondrially targeted restriction endonucleases Biochim. Biophys. Acta 1657 2004 89
    • (2004) Biochim. Biophys. Acta , vol.1657 , pp. 89
    • Bayona, M.1    Blits, B.2    Battersby, B.3    Shoubridge, E.4    Moraes, C.5
  • 31
    • 0027327280 scopus 로고
    • Fate and expression of the deleted mitochondrial DNA differ between human heteroplasmic skin fibroblast and Epstein-Barr virus transformed lymphocyte cultures
    • T. Bougeron, D. Chretien, A. Rötig, A. Munnich, and P. Rustin Fate and expression of the deleted mitochondrial DNA differ between human heteroplasmic skin fibroblast and Epstein-Barr virus transformed lymphocyte cultures J. Biol. Chem. 268 1993 19369 19376
    • (1993) J. Biol. Chem. , vol.268 , pp. 19369-19376
    • Bougeron, T.1    Chretien, D.2    Rötig, A.3    Munnich, A.4    Rustin, P.5
  • 32
    • 0029079541 scopus 로고
    • Different cellular backgrounds confer a marked advantage to either mutant or wild-type mitochondrial genomes
    • D.R. Dunbar, P.A. Moonie, H.T. Jacobs, and I.J. Holt Different cellular backgrounds confer a marked advantage to either mutant or wild-type mitochondrial genomes Proc. Natl. Acad. Sci. U. S. A. 92 1995 6562 6566
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 6562-6566
    • Dunbar, D.R.1    Moonie, P.A.2    Jacobs, H.T.3    Holt, I.J.4
  • 33
    • 0030951244 scopus 로고    scopus 로고
    • Tissue-specific selection for different mtDNA genotypes in heteroplasmic mice
    • J.P. Jenuth, A.C. Peterson, and E.A. Shoubridge Tissue-specific selection for different mtDNA genotypes in heteroplasmic mice Nat. Genet. 16 1997 93 95
    • (1997) Nat. Genet. , vol.16 , pp. 93-95
    • Jenuth, J.P.1    Peterson, A.C.2    Shoubridge, E.A.3
  • 34
    • 0037313092 scopus 로고    scopus 로고
    • Nuclear genetic control of mitochondrial DNA segregation
    • B.J. Battersby, J.C. Loredo-Osti, and E.A. Shoubridge Nuclear genetic control of mitochondrial DNA segregation Nat. Genet. 33 2003 183 186
    • (2003) Nat. Genet. , vol.33 , pp. 183-186
    • Battersby, B.J.1    Loredo-Osti, J.C.2    Shoubridge, E.A.3
  • 36
    • 0142153431 scopus 로고    scopus 로고
    • Why do mammalian mitochondria possess a mismatch repair activity?
    • P.A. Mason, and R.N. Lightowlers Why do mammalian mitochondria possess a mismatch repair activity? FEBS Lett. 554 2003 6 9
    • (2003) FEBS Lett. , vol.554 , pp. 6-9
    • Mason, P.A.1    Lightowlers, R.N.2
  • 37
    • 0024448458 scopus 로고
    • Human cells lacking MTDNA: Repopulation with exogenous mitochondria by complementation
    • M.P. King, and G. Attardi 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
  • 41
    • 0031038812 scopus 로고    scopus 로고
    • Selective inhibition of mutant human mitochondrial DNA replication in vitro by peptide nucleic acids
    • R.W. Taylor, P.F. Chinnery, D.M. Turnbull, and R.N. Lightowlers Selective inhibition of mutant human mitochondrial DNA replication in vitro by peptide nucleic acids Nat. Genet. 15 1997 212 215
    • (1997) Nat. Genet. , vol.15 , pp. 212-215
    • Taylor, R.W.1    Chinnery, P.F.2    Turnbull, D.M.3    Lightowlers, R.N.4
  • 42
    • 0242404318 scopus 로고    scopus 로고
    • Blockade of plasmid replication mediated by peptide nucleic acids
    • M.R. Liebling, N.T. Jou, W. Fang, and J.S. Louie Blockade of plasmid replication mediated by peptide nucleic acids Mol. Biotechnol. 25 2003 229 240
    • (2003) Mol. Biotechnol. , vol.25 , pp. 229-240
    • Liebling, M.R.1    Jou, N.T.2    Fang, W.3    Louie, J.S.4
  • 44
    • 0035339611 scopus 로고    scopus 로고
    • Targeting of peptide nucleic acid (PNA) oligomers to miitochondria within cells by conjugation to lipophilic cations: Implications for mitochondrial DNA replication, expression and disease
    • A. Muratovska, R.N. Lightowlers, R.W. Taylor, D.M. Turnbull, R.A.J. Smith, J.A. Wilce, S.W. Martin, and M.P. Murphy Targeting of peptide nucleic acid (PNA) oligomers to miitochondria within cells by conjugation to lipophilic cations: implications for mitochondrial DNA replication, expression and disease Nucleic Acids Res. 29 2001 1852 1863
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1852-1863
    • Muratovska, A.1    Lightowlers, R.N.2    Taylor, R.W.3    Turnbull, D.M.4    Smith, R.A.J.5    Wilce, J.A.6    Martin, S.W.7    Murphy, M.P.8
  • 45
    • 0141792967 scopus 로고    scopus 로고
    • Synthesis of trifunctional PNA-benzophenone derivatives for mitochondrial targeting, selective DNA binding, and photo-cross-linking
    • G.F. Ross, P.M. Smith, A. McGregor, D.M. Turnbull, and R.N. Lightowlers Synthesis of trifunctional PNA-benzophenone derivatives for mitochondrial targeting, selective DNA binding, and photo-cross-linking Bioconjug. Chem. 14 2003 962 966
    • (2003) Bioconjug. Chem. , vol.14 , pp. 962-966
    • Ross, G.F.1    Smith, P.M.2    McGregor, A.3    Turnbull, D.M.4    Lightowlers, R.N.5
  • 49
    • 0025932041 scopus 로고
    • A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin a
    • F.G. van der Goot, J.M. Gonzalez-Manas, J.H. Lakey, and F. Pattus A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A Nature 354 1991 408 410
    • (1991) Nature , vol.354 , pp. 408-410
    • Van Der Goot, F.G.1    Gonzalez-Manas, J.M.2    Lakey, J.H.3    Pattus, F.4
  • 50
    • 0033548529 scopus 로고    scopus 로고
    • An experimental study of mechanism and specificity of peptide nucleic acid (PNA) binding to duplex DNA
    • H. Kuhn, V.V. Demidov, P.E. Neilsen, and M.D. Frank-Kamenetski An experimental study of mechanism and specificity of peptide nucleic acid (PNA) binding to duplex DNA J. Mol. Biol. 286 1999 1337 1345
    • (1999) J. Mol. Biol. , vol.286 , pp. 1337-1345
    • Kuhn, H.1    Demidov, V.V.2    Neilsen, P.E.3    Frank-Kamenetski, M.D.4
  • 51
    • 0028194906 scopus 로고
    • Activation energy for permeation of phosphonium cations through phospholipid bilayer membrane
    • A. Ono, S. Miyauchi, M. Demura, T. Asakura, and N. Kamo Activation energy for permeation of phosphonium cations through phospholipid bilayer membrane Biochemistry 33 1994 4312 4318
    • (1994) Biochemistry , vol.33 , pp. 4312-4318
    • Ono, A.1    Miyauchi, S.2    Demura, M.3    Asakura, T.4    Kamo, N.5
  • 52
    • 9144230176 scopus 로고    scopus 로고
    • Cell-penetrating peptides do not cross mitochondrial membranes even when conjugated to a lipophilic cation: Evidence against direct passage through phospholipid bilayers
    • M.F. Ross, A. Filipovska, R.A.J. Smith, M.J. Gait, and M.P. Murphy Cell-penetrating peptides do not cross mitochondrial membranes even when conjugated to a lipophilic cation: evidence against direct passage through phospholipid bilayers Biochem. J. 2004 (in press)
    • (2004) Biochem. J.
    • Ross, M.F.1    Filipovska, A.2    Smith, R.A.J.3    Gait, M.J.4    Murphy, M.P.5
  • 53
    • 0344522705 scopus 로고    scopus 로고
    • Plant mitochondria actively import DNA via the permeability transition pore complex
    • M. Koulintchenko, Y. Konstantinov, and A. Dietrich Plant mitochondria actively import DNA via the permeability transition pore complex EMBO J. 22 2003 1245 1254
    • (2003) EMBO J. , vol.22 , pp. 1245-1254
    • Koulintchenko, M.1    Konstantinov, Y.2    Dietrich, A.3
  • 54
    • 0031916033 scopus 로고    scopus 로고
    • DQAsomes: A novel potential drug and gene delivery system made from Dequalinium
    • V. Weissig, J. Lasch, G. Erdos, H.W. Meyer, T.C. Rowe, and J. Hughes DQAsomes: a novel potential drug and gene delivery system made from Dequalinium Pharm. Res. 15 1998 334 337
    • (1998) Pharm. Res. , vol.15 , pp. 334-337
    • Weissig, V.1    Lasch, J.2    Erdos, G.3    Meyer, H.W.4    Rowe, T.C.5    Hughes, J.6
  • 55
    • 0035797116 scopus 로고    scopus 로고
    • Cationic bolasomes with delocalised charge centres as mitochondria-specific DNA delivery systems
    • V. Weissig, and V. Torchilin Cationic bolasomes with delocalised charge centres as mitochondria-specific DNA delivery systems Adv. Drug Deliv. Rev. 49 2001 127 149
    • (2001) Adv. Drug Deliv. Rev. , vol.49 , pp. 127-149
    • Weissig, V.1    Torchilin, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.