메뉴 건너뛰기




Volumn 34, Issue 2, 2011, Pages 465-475

Toxic response caused by a misfolding variant of the mitochondrial protein short-chain acyl-CoA dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

BUTYRYL COENZYME A DEHYDROGENASE; ENZYME VARIANT; MESSENGER RNA; SUPEROXIDE DISMUTASE;

EID: 79955699713     PISSN: 01418955     EISSN: 15732665     Source Type: Journal    
DOI: 10.1007/s10545-010-9255-7     Document Type: Article
Times cited : (13)

References (37)
  • 1
    • 0026020414 scopus 로고
    • Fatty acid oxidation and ketogenesis by astrocytes in primary culture
    • Auestad N, Korsak RA, Morrow JW, Edmond J (1991) Fatty acid oxidation and ketogenesis by astrocytes in primary culture. J Neurochem 56:1376-1386
    • (1991) J Neurochem , vol.56 , pp. 1376-1386
    • Auestad, N.1    Korsak, R.A.2    Morrow, J.W.3    Edmond, J.4
  • 2
    • 56349099660 scopus 로고    scopus 로고
    • Suppression mechanisms of COX assembly defects in yeast and human: Insights into the COX assembly process
    • Barrientos A, Gouget K, Horn D, Soto IC, Fontanesi F (2009) Suppression mechanisms of COX assembly defects in yeast and human: insights into the COX assembly process. Biochim Biophys Acta 1793:97-107
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 97-107
    • Barrientos, A.1    Gouget, K.2    Horn, D.3    Soto, I.C.4    Fontanesi, F.5
  • 3
    • 0036775158 scopus 로고    scopus 로고
    • Heme oxygenase-1: Redox regulation and role in the hepatic response to oxidative stress
    • Bauer M, Bauer I (2002) Heme oxygenase-1: redox regulation and role in the hepatic response to oxidative stress. Antioxid Redox Signal 4:749-758 (Pubitemid 35246937)
    • (2002) Antioxidants and Redox Signaling , vol.4 , Issue.5 , pp. 749-758
    • Bauer, M.1    Bauer, I.2
  • 4
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • DOI 10.1016/0092-8674(94)90131-7
    • Behl C, Davis JB, Lesley R, Schubert D (1994) Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 77:817-827 (Pubitemid 24187680)
    • (1994) Cell , vol.77 , Issue.6 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 6
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • DOI 10.1083/jcb.200211046
    • Chen H, Detmer SA, Ewald AJ, Griffin EE, Fraser SE, Chan DC (2003) Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J Cell Biol 160:189-200 (Pubitemid 36254953)
    • (2003) Journal of Cell Biology , vol.160 , Issue.2 , pp. 189-200
    • Chen, H.1    Detmer, S.A.2    Ewald, A.J.3    Griffin, E.E.4    Fraser, S.E.5    Chan, D.C.6
  • 7
    • 58049088157 scopus 로고    scopus 로고
    • Oxidant stress stimulates expression of the human peroxiredoxin 6 gene by a transcriptional mechanism involving an antioxidant response element
    • Chowdhury I, Mo Y, Gao L, Kazi A, Fisher AB, Feinstein SI (2009) Oxidant stress stimulates expression of the human peroxiredoxin 6 gene by a transcriptional mechanism involving an antioxidant response element. Free Radic Biol Med 46:146-153
    • (2009) Free Radic Biol Med , vol.46 , pp. 146-153
    • Chowdhury, I.1    Mo, Y.2    Gao, L.3    Kazi, A.4    Fisher, A.B.5    Feinstein, S.I.6
  • 9
    • 23044498270 scopus 로고    scopus 로고
    • Down-regulation of Hsp60 expression by RNAi impairs folding of medium-chain acyl-CoA dehydrogenase wild-type and disease-associated proteins
    • DOI 10.1016/j.ymgme.2005.04.003, PII S1096719205001150
    • Corydon TJ, Hansen J, Bross P, Jensen TG (2005) Down-regulation of Hsp60 expression by RNAi impairs folding of medium-chain acyl-CoA dehydrogenase wild-type and disease-associated proteins. Mol Genet Metab 85:260-270 (Pubitemid 41074109)
    • (2005) Molecular Genetics and Metabolism , vol.85 , Issue.4 , pp. 260-270
    • Corydon, T.J.1    Hansen, J.2    Bross, P.3    Jensen, T.G.4
  • 10
    • 0033214782 scopus 로고    scopus 로고
    • 1 complex
    • DOI 10.1093/emboj/18.19.5226
    • Cruciat CM, Hell K, Folsch H, Neupert W, Stuart RA (1999) Bcs1p, an AAA-family member, is a chaperone for the assembly of the cytochrome bc(1) complex. EMBO J 18:5226-5233 (Pubitemid 29465573)
    • (1999) EMBO Journal , vol.18 , Issue.19 , pp. 5226-5233
    • Cruciat, C.-M.1    Hell, K.2    Folsch, H.3    Neupert, W.4    Stuart, R.A.5
  • 11
    • 0037707488 scopus 로고    scopus 로고
    • 13C nuclear magnetic resonance spectroscopy
    • Ebert D, Haller RG,WaltonME (2003) Energy contribution of octanoate to intact rat brain metabolism measured by 13 C nuclear magnetic resonance spectroscopy. J Neurosci 23:5928-5935 (Pubitemid 36807872)
    • (2003) Journal of Neuroscience , vol.23 , Issue.13 , pp. 5928-5935
    • Ebert, D.1    Haller, R.G.2    Walton, M.E.3
  • 12
    • 0030806863 scopus 로고    scopus 로고
    • Superoxide anion radical (O2-.), superoxide dismutases, and related matters
    • Fridovich I (1997) Superoxide anion radical (O2-.), superoxide dismutases, and related matters. J Biol Chem 272:18515-18517
    • (1997) J Biol Chem , vol.272 , pp. 18515-18517
    • Fridovich, I.1
  • 15
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381:571-579
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 16
    • 0344753404 scopus 로고
    • The enzymatic carboxylation fo butyryl coenzyme A
    • Hegre CS, Halenz DR, Lane MD (1959) The enzymatic carboxylation fo butyryl coenzyme A. J Am Chem Soc 81:6526-6527
    • (1959) J Am Chem Soc , vol.81 , pp. 6526-6527
    • Hegre, C.S.1    Halenz, D.R.2    Lane, M.D.3
  • 19
    • 0021970335 scopus 로고
    • Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme
    • Ikeda Y, Okamura-Ikeda K, Tanaka K (1985) Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme. J Biol Chem 260:1311-1325 (Pubitemid 15173654)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.2 , pp. 1311-1325
    • Ikeda, Y.1    Okamura-Ikeda, K.2    Tanaka, K.3
  • 20
    • 56049108772 scopus 로고    scopus 로고
    • Clinical outcomes of infants with short-chain acyl-coenzyme A dehydrogenase deficiency (SCADD) detected by newborn screening
    • Jethva R, Ficicioglu C (2008) Clinical outcomes of infants with short-chain acyl-coenzyme A dehydrogenase deficiency (SCADD) detected by newborn screening. Mol Genet Metab 95:241-242
    • (2008) Mol Genet Metab , vol.95 , pp. 241-242
    • Jethva, R.1    Ficicioglu, C.2
  • 23
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • DOI 10.1038/nature05292, PII NATURE05292
    • Lin MT, Beal MF (2006) Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443:787-795 (Pubitemid 44622683)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 24
    • 34147153222 scopus 로고    scopus 로고
    • Analysis of mitochondrial subunit assembly into respiratory chain complexes using Blue Native polyacrylamide gel electrophoresis
    • DOI 10.1016/j.ab.2007.02.022, PII S000326970700125X
    • McKenzie M, Lazarou M, Thorburn DR, Ryan MT (2007) Analysis of mitochondrial subunit assembly into respiratory chain complexes using Blue Native polyacrylamide gel electrophoresis. Anal Biochem 364:128-137 (Pubitemid 46559922)
    • (2007) Analytical Biochemistry , vol.364 , Issue.2 , pp. 128-137
    • McKenzie, M.1    Lazarou, M.2    Thorburn, D.R.3    Ryan, M.T.4
  • 25
    • 0025352187 scopus 로고
    • Advanced mammalian gene transfer: High titre retroviral vectors with multiple drug selection markers and a complementary helper-free packaging cell line
    • Morgenstern JP, Land H (1990) Advanced mammalian gene transfer: high titre retroviral vectors with multiple drug selection markers and a complementary helper-free packaging cell line. Nucleic Acids Res 18:3587-3596
    • (1990) Nucleic Acids Res , vol.18 , pp. 3587-3596
    • Morgenstern, J.P.1    Land, H.2
  • 26
    • 62449244004 scopus 로고    scopus 로고
    • Cell death: Protein misfolding and neurodegenerative diseases
    • Nakamura T, Lipton SA (2009) Cell death: protein misfolding and neurodegenerative diseases. Apoptosis 14:455-468
    • (2009) Apoptosis , vol.14 , pp. 455-468
    • Nakamura, T.1    Lipton, S.A.2
  • 27
    • 67650281238 scopus 로고    scopus 로고
    • Mitochondrial proteomics on human fibroblasts for identification of metabolic imbalance and cellular stress
    • Palmfeldt J, Vang S, Stenbroen V et al (2009) Mitochondrial proteomics on human fibroblasts for identification of metabolic imbalance and cellular stress. Proteome Sci 7:20
    • (2009) Proteome Sci , vol.7 , pp. 20
    • Palmfeldt, J.1    Vang, S.2    Stenbroen, V.3
  • 29
    • 46949109490 scopus 로고    scopus 로고
    • The ACADS gene variation spectrum in 114 patients with short-chain acyl-CoA dehydrogenase (SCAD) deficiency is dominated by missense variations leading to protein misfolding at the cellular level
    • Pedersen CB, Kolvraa S, Kolvraa A et al (2008) The ACADS gene variation spectrum in 114 patients with short-chain acyl-CoA dehydrogenase (SCAD) deficiency is dominated by missense variations leading to protein misfolding at the cellular level. Hum Genet 124:43-56
    • (2008) Hum Genet , vol.124 , pp. 43-56
    • Pedersen, C.B.1    Kolvraa, S.2    Kolvraa, A.3
  • 30
    • 77951978533 scopus 로고    scopus 로고
    • Misfolding of short-chain acyl-CoA dehydrogenase leads to mitochondrial fission and oxidative stress
    • Schmidt SP, Corydon TJ, Pedersen CB, Bross P, Gregersen N (2010) Misfolding of short-chain acyl-CoA dehydrogenase leads to mitochondrial fission and oxidative stress. Mol Genet Metab 100:155-162
    • (2010) Mol Genet Metab , vol.100 , pp. 155-162
    • Schmidt, S.P.1    Corydon, T.J.2    Pedersen, C.B.3    Bross, P.4    Gregersen, N.5
  • 31
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • DOI 10.1038/20959
    • Shimizu S, Narita M, Tsujimoto Y (1999) Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399:483-487 (Pubitemid 29258855)
    • (1999) Nature , vol.399 , Issue.6735 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 32
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • DOI 10.1007/s00109-003-0464-5
    • Stefani M, Dobson CM (2003) Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J Mol Med 81:678-699 (Pubitemid 37491594)
    • (2003) Journal of Molecular Medicine , vol.81 , Issue.11 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 33
    • 0033555567 scopus 로고    scopus 로고
    • Short-chain acyl-CoA dehydrogenase deficiency: A cause of ophthalmoplegia and multicore myopathy
    • Tein I, Haslam RH, Rhead WJ, BennettMJ, Becker LE, Vockley J (1999) Short-chain acyl-CoA dehydrogenase deficiency: a cause of ophthalmoplegia and multicore myopathy. Neurology 52:366-372 (Pubitemid 29059066)
    • (1999) Neurology , vol.52 , Issue.2 , pp. 366-372
    • Tein, I.1    Haslam, R.H.A.2    Rhead, W.J.3    Bennett, M.J.4    Becker, L.E.5    Vockley, J.6
  • 34
    • 38049177259 scopus 로고    scopus 로고
    • Short-chain acyl-CoA dehydrogenase gene mutation (c.319 C>T) presents with clinical heterogeneity and is candidate founder mutation in individuals of Ashkenazi Jewish origin
    • Tein I, Elpeleg O, Ben-Zeev B et al (2008) Short-chain acyl-CoA dehydrogenase gene mutation (c.319 C>T) presents with clinical heterogeneity and is candidate founder mutation in individuals of Ashkenazi Jewish origin. Mol Genet Metab 93:179-189
    • (2008) Mol Genet Metab , vol.93 , pp. 179-189
    • Tein, I.1    Elpeleg, O.2    Ben-Zeev, B.3
  • 36
    • 51649085510 scopus 로고    scopus 로고
    • Short-chain acyl-CoA dehydrogenase (SCAD) deficiency: An examination of the medical and neurodevelopmental characteristics of 14 cases identified through newborn screening or clinical symptoms
    • Waisbren SE, Levy HL, Noble M et al (2008) Short-chain acyl-CoA dehydrogenase (SCAD) deficiency: an examination of the medical and neurodevelopmental characteristics of 14 cases identified through newborn screening or clinical symptoms. Mol Genet Metab 95:39-45
    • (2008) Mol Genet Metab , vol.95 , pp. 39-45
    • Waisbren, S.E.1    Levy, H.L.2    Noble, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.