메뉴 건너뛰기




Volumn 48, Issue 2, 2014, Pages 168-179

The Hsp60 folding machinery is crucial for manganese superoxide dismutase folding and function

Author keywords

Hsp60; MnSOD; Neurodegeneration; Oxidative stress; SPG13

Indexed keywords

CHAPERONIN 60; MANGANESE SUPEROXIDE DISMUTASE;

EID: 84890015010     PISSN: 10715762     EISSN: 10292470     Source Type: Journal    
DOI: 10.3109/10715762.2013.858147     Document Type: Article
Times cited : (51)

References (44)
  • 1
    • 0034626774 scopus 로고    scopus 로고
    • Why do we age?
    • TB Austad S.N.
    • TB, Austad, SN. Why do we age? Nature 2000; 408: 233-238.
    • (2000) Nature , vol.408 , pp. 233-238
  • 2
    • 34648831384 scopus 로고    scopus 로고
    • Alzheimer's disease: A lesson from mitochondrial dysfunction
    • Moreira PI, Santos MS, Oliveira CR. Alzheimer's disease: A lesson from mitochondrial dysfunction. Antioxid Redox Signal 2007; 9: 1621-1630.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 1621-1630
    • Moreira, P.I.1    Santos, M.S.2    Oliveira, C.R.3
  • 3
    • 37049004489 scopus 로고    scopus 로고
    • Mitochondria in the aetiology and pathogenesis of Parkinson's disease
    • Schapira AH. Mitochondria in the aetiology and pathogenesis of Parkinson's disease. Lancet Neurol 2008; 7: 97-109.
    • (2008) Lancet Neurol , vol.7 , pp. 97-109
    • Schapira, A.H.1
  • 4
    • 0030813067 scopus 로고    scopus 로고
    • Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis
    • Ferrante RJ, Browne SE, Shinobu LA, Bowling AC, Baik MJ, MacGarvey U, et al. Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis. J Neurochem 1997; 69: 2064-2074.
    • (1997) J Neurochem , vol.69 , pp. 2064-2074
    • Ferrante, R.J.1    Browne, S.E.2    Shinobu, L.A.3    Bowling, A.C.4    Baik, M.J.5    MacGarvey, U.6
  • 5
    • 0029082389 scopus 로고
    • Oxidative damage to protein in sporadic motor neuron disease spinal cord
    • Shaw PJ, Ince PG, Falkous G, Mantle D. Oxidative damage to protein in sporadic motor neuron disease spinal cord. Ann Neurol 1995; 38: 691-695.
    • (1995) Ann Neurol , vol.38 , pp. 691-695
    • Shaw, P.J.1    Ince, P.G.2    Falkous, G.3    Mantle, D.4
  • 6
    • 67651154308 scopus 로고    scopus 로고
    • Haploinsufficiency of AFG3L2, the gene responsible for spinocerebellar ataxia type 28, causes mitochondriamediated Purkinje cell dark degeneration
    • Maltecca F, Magnoni R, Cerri F, Cox GA, Quattrini A, Casari G. Haploinsufficiency of AFG3L2, the gene responsible for spinocerebellar ataxia type 28, causes mitochondriamediated Purkinje cell dark degeneration. J Neurosci 2009; 29: 9244-9254.
    • (2009) J Neurosci , vol.29 , pp. 9244-9254
    • Maltecca, F.1    Magnoni, R.2    Cerri, F.3    Cox, G.A.4    Quattrini, A.5    Casari, G.6
  • 7
    • 0036241765 scopus 로고    scopus 로고
    • Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60
    • Hansen JJ, Durr A, Cournu-Rebeix I, Georgopoulos C, Ang D, Nielsen MN, et al. Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. Am J Hum Genet 2002; 70: 1328-1332.
    • (2002) Am J Hum Genet , vol.70 , pp. 1328-1332
    • Hansen, J.J.1    Durr, A.2    Cournu-Rebeix, I.3    Georgopoulos, C.4    Ang, D.5    Nielsen, M.N.6
  • 8
  • 9
    • 46149097136 scopus 로고    scopus 로고
    • Mitochondrial hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy
    • Magen D, Georgopoulos C, Bross P, Ang D, Segev Y, Goldsher D, et al. Mitochondrial hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy. Am J Hum Genet 2008; 83: 30-42.
    • (2008) Am J Hum Genet , vol.83 , pp. 30-42
    • Magen, D.1    Georgopoulos, C.2    Bross, P.3    Ang, D.4    Segev, Y.5    Goldsher, D.6
  • 10
    • 0036241765 scopus 로고    scopus 로고
    • Hereditary Spastic Paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial Chaperonin Hsp60
    • Hansen JJ, D ü rr A, Cournu-Rebeix I, Georgopoulos C, Ang D, Nielsen MN, et al. Hereditary Spastic Paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial Chaperonin Hsp60. Am J Hum Genet 2002; 70: 1328-1332.
    • (2002) Am J Hum Genet , vol.70 , pp. 1328-1332
    • Hansen, J.J.1    Dürr, A.2    Cournu-Rebeix, I.3    Georgopoulos, C.4    Ang, D.5    Nielsen, M.N.6
  • 12
    • 0024972083 scopus 로고
    • Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
    • Cheng MY, Hartl FU, Martin J, Pollock RA, Kalousek F, Neupert W, et al. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 1989; 337: 620-625.
    • (1989) Nature , vol.337 , pp. 620-625
    • Cheng, M.Y.1    Hartl, F.U.2    Martin, J.3    Pollock, R.A.4    Kalousek, F.5    Neupert, W.6
  • 13
    • 78149471001 scopus 로고    scopus 로고
    • Inactivation of the hereditary spastic paraplegia-Associated Hspd1 gene encoding the Hsp60 chaperone results in early embryonic lethality in mice
    • Christensen JH, Nielsen MN, Hansen J, Fuchtbauer A, Fuchtbauer EM, West M, et al. Inactivation of the hereditary spastic paraplegia-Associated Hspd1 gene encoding the Hsp60 chaperone results in early embryonic lethality in mice. Cell Stress Chaperones 2010; 15: 851-863.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 851-863
    • Christensen, J.H.1    Nielsen, M.N.2    Hansen, J.3    Fuchtbauer, A.4    Fuchtbauer, E.M.5    West, M.6
  • 16
    • 84874911348 scopus 로고    scopus 로고
    • Molecular chaperone disorders: Defective Hsp60 in neurodegeneration
    • Bross P, Magnoni R, Bie AS. Molecular chaperone disorders: Defective Hsp60 in neurodegeneration. Curr Top Med Chem 2013; 12: 2491-2503.
    • (2013) Curr Top Med Chem , vol.12 , pp. 2491-2503
    • Bross, P.1    Magnoni, R.2    Bie, A.S.3
  • 17
    • 84857030799 scopus 로고    scopus 로고
    • Neurodegeneration as a consequence of failed mitochondrial maintenance
    • Karbowski M, Neutzner A. Neurodegeneration as a consequence of failed mitochondrial maintenance. Acta Neuropathol 2012; 123: 157-171.
    • (2012) Acta Neuropathol , vol.123 , pp. 157-171
    • Karbowski, M.1    Neutzner, A.2
  • 18
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy MP. How mitochondria produce reactive oxygen species. Biochem J 2009; 417: 1-13.
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 19
    • 77952541558 scopus 로고    scopus 로고
    • The sites and topology of mitochondrial superoxide production
    • Brand MD. The sites and topology of mitochondrial superoxide production. Exp Gerontol 2010; 45: 466-472.
    • (2010) Exp Gerontol , vol.45 , pp. 466-472
    • Brand, M.D.1
  • 20
    • 0026688441 scopus 로고
    • The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles
    • Borgstahl GE, Parge HE, Hickey MJ, Beyer WF Jr, Hallewell RA, Tainer JA. The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles. Cell 1992; 71: 107-118.
    • (1992) Cell , vol.71 , pp. 107-118
    • Borgstahl, G.E.1    Parge, H.E.2    Hickey, M.J.3    Beyer Jr., W.F.4    Hallewell, R.A.5    Tainer, J.A.6
  • 21
    • 63349087445 scopus 로고    scopus 로고
    • Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation
    • Tahara EB, Navarete FD, Kowaltowski AJ. Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation. Free Radic Biol Med 2009; 46: 1283-1297.
    • (2009) Free Radic Biol Med , vol.46 , pp. 1283-1297
    • Tahara, E.B.1    Navarete, F.D.2    Kowaltowski, A.J.3
  • 22
    • 79955664111 scopus 로고    scopus 로고
    • Mitochondrial protein quality control during biogenesis and aging
    • Baker BM, Haynes CM. Mitochondrial protein quality control during biogenesis and aging. Trends Biochem Sci 2011; 36: 254-261.
    • (2011) Trends Biochem Sci , vol.36 , pp. 254-261
    • Baker, B.M.1    Haynes, C.M.2
  • 25
    • 79955831977 scopus 로고    scopus 로고
    • Proteomics reveals that redox regulation is disrupted in patients with ethylmalonic encephalopathy
    • Palmfeldt J, Vang S, Stenbroen V, Pavlou E, Baycheva M, Buchal G, et al. Proteomics reveals that redox regulation is disrupted in patients with ethylmalonic encephalopathy. J Proteome Res 2011; 10: 2389-2396.
    • (2011) J Proteome Res , vol.10 , pp. 2389-2396
    • Palmfeldt, J.1    Vang, S.2    Stenbroen, V.3    Pavlou, E.4    Baycheva, M.5    Buchal, G.6
  • 26
    • 75149164344 scopus 로고    scopus 로고
    • Measurement of superoxide dismutase, catalase and glutathione peroxidase in cultured cells and tissue
    • Weydert CJ, Cullen JJ. Measurement of superoxide dismutase, catalase and glutathione peroxidase in cultured cells and tissue. Nat Protoc 2010; 5: 51-66.
    • (2010) Nat Protoc , vol.5 , pp. 51-66
    • Weydert, C.J.1    Cullen, J.J.2
  • 27
    • 43049159563 scopus 로고    scopus 로고
    • Decreased expression of the mitochondrial matrix proteases Lon and ClpP in cells from a patient with hereditary spastic paraplegia (SPG13)
    • Hansen J, Corydon TJ, Palmfeldt J, Durr A, Fontaine B, Nielsen MN, et al. Decreased expression of the mitochondrial matrix proteases Lon and ClpP in cells from a patient with hereditary spastic paraplegia (SPG13). Neuroscience 2008; 153: 474-482.
    • (2008) Neuroscience , vol.153 , pp. 474-482
    • Hansen, J.1    Corydon, T.J.2    Palmfeldt, J.3    Durr, A.4    Fontaine, B.5    Nielsen, M.N.6
  • 29
    • 0033562350 scopus 로고    scopus 로고
    • Development and validation of real-Time quantitative reverse transcriptasepolymerase chain reaction for monitoring gene expression in cardiac myocytes in vitro
    • Winer J, Jung CK, Shackel I, Williams PM. Development and validation of real-Time quantitative reverse transcriptasepolymerase chain reaction for monitoring gene expression in cardiac myocytes in vitro. Anal Biochem 1999; 270: 41-49.
    • (1999) Anal Biochem , vol.270 , pp. 41-49
    • Winer, J.1    Jung, C.K.2    Shackel, I.3    Williams, P.M.4
  • 30
    • 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, Stenbroen V, Kjeldsen M, Ensenauer R, et al. 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 2008; 124: 43-56.
    • (2008) Hum Genet , vol.124 , pp. 43-56
    • Pedersen, C.B.1    Kolvraa, S.2    Kolvraa, A.3    Stenbroen, V.4    Kjeldsen, M.5    Ensenauer, R.6
  • 31
    • 0346100521 scopus 로고    scopus 로고
    • Recent advances in the analysis of oxidized proteins
    • Requena JR, Levine RL, Stadtman ER. Recent advances in the analysis of oxidized proteins. Amino Acids 2003; 25: 221-226.
    • (2003) Amino Acids , vol.25 , pp. 221-226
    • Requena, J.R.1    Levine, R.L.2    Stadtman, E.R.3
  • 32
    • 17844403545 scopus 로고    scopus 로고
    • Role of oxidative carbonylation in protein quality control and senescence
    • Nystrom T. Role of oxidative carbonylation in protein quality control and senescence. EMBO J 2005; 24: 1311-1317.
    • (2005) EMBO J , vol.24 , pp. 1311-1317
    • Nystrom, T.1
  • 33
    • 0030894162 scopus 로고    scopus 로고
    • Oxidative stress: Oxidants and antioxidants
    • Sies H. Oxidative stress: Oxidants and antioxidants. Exp Physiol 1997; 82: 291-295.
    • (1997) Exp Physiol , vol.82 , pp. 291-295
    • Sies, H.1
  • 34
    • 0029838063 scopus 로고    scopus 로고
    • Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice
    • Lebovitz RM, Zhang H, Vogel H, Cartwright J Jr, Dionne L, Lu N, et al. Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice. Proc Natl Acad Sci USA 1996; 93: 9782-9787.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9782-9787
    • Lebovitz, R.M.1    Zhang, H.2    Vogel, H.3    Cartwright Jr., J.4    Dionne, L.5    Lu, N.6
  • 35
    • 21044450045 scopus 로고    scopus 로고
    • Heterozygous deficiency of manganese superoxide dismutase results in severe lipid peroxidation and spontaneous apoptosis in murine myocardium in vivo
    • Strassburger M, Bloch W, Sulyok S, Schuller J, Keist AF, Schmidt A, et al. Heterozygous deficiency of manganese superoxide dismutase results in severe lipid peroxidation and spontaneous apoptosis in murine myocardium in vivo. Free Radic Biol Med 2005; 38: 1458-1470.
    • (2005) Free Radic Biol Med , vol.38 , pp. 1458-1470
    • Strassburger, M.1    Bloch, W.2    Sulyok, S.3    Schuller, J.4    Keist, A.F.5    Schmidt, A.6
  • 36
    • 12144288373 scopus 로고    scopus 로고
    • Life-long reduction in MnSOD activity results in increased DNA damage and higher incidence of cancer but does not accelerate aging
    • Van RH, Ikeno Y, Hamilton M, Pahlavani M, Wolf N, Thorpe SR, et al. Life-long reduction in MnSOD activity results in increased DNA damage and higher incidence of cancer but does not accelerate aging. Physiol Genomics 2003; 16: 29-37.
    • (2003) Physiol Genomics , vol.16 , pp. 29-37
    • Van, R.H.1    Ikeno, Y.2    Hamilton, M.3    Pahlavani, M.4    Wolf, N.5    Thorpe, S.R.6
  • 37
    • 57649171133 scopus 로고    scopus 로고
    • Evidence of oxidant damage in Huntington's disease: Translational strategies using antioxidants
    • Stack EC, Matson WR, Ferrante RJ Evidence of oxidant damage in Huntington's disease: Translational strategies using antioxidants. Ann N Y Acad Sci 2008; 1147: 79-92.
    • (2008) Ann N Y Acad Sci , vol.1147 , pp. 79-92
    • Stack, E.C.1    Matson, W.R.2    Ferrante, R.J.3
  • 38
    • 79955078128 scopus 로고    scopus 로고
    • Parkinson's syndrome and Parkinson's disease in mitochondrial disorders
    • Finsterer J. Parkinson's syndrome and Parkinson's disease in mitochondrial disorders. Mov Disord 2011; 26: 784-791.
    • (2011) Mov Disord , vol.26 , pp. 784-791
    • Finsterer, J.1
  • 39
    • 1342310772 scopus 로고    scopus 로고
    • Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport
    • Ferreirinha F, Quattrini A, Pirozzi M, Valsecchi V, Dina G, Broccoli V, et al. Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport. J Clin Invest 2004; 113: 231-242.
    • (2004) J Clin Invest , vol.113 , pp. 231-242
    • Ferreirinha, F.1    Quattrini, A.2    Pirozzi, M.3    Valsecchi, V.4    Dina, G.5    Broccoli, V.6
  • 40
    • 67649366086 scopus 로고    scopus 로고
    • FOXO3a is broadly neuroprotective in vitro and in vivo against insults implicated in motor neuron diseases
    • Mojsilovic-Petrovic J, Nedelsky N, Boccitto M, Mano I, Georgiades SN, Zhou W, et al. FOXO3a is broadly neuroprotective in vitro and in vivo against insults implicated in motor neuron diseases. J Neurosci 2009; 29: 8236-8247.
    • (2009) J Neurosci , vol.29 , pp. 8236-8247
    • Mojsilovic-Petrovic, J.1    Nedelsky, N.2    Boccitto, M.3    Mano, I.4    Georgiades, S.N.5    Zhou, W.6
  • 41
    • 74449090930 scopus 로고    scopus 로고
    • Post-Translational modifications of superoxide dismutase
    • Yamakura F, Kawasaki H. Post-Translational modifications of superoxide dismutase. Biochim Biophys Acta 2010; 1804: 318-325.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 318-325
    • Yamakura, F.1    Kawasaki, H.2
  • 42
    • 0034113502 scopus 로고    scopus 로고
    • Nitration of manganese superoxide dismutase in cerebrospinal fl uids is a marker for peroxynitrite-mediated oxidative stress in neurodegenerative diseases
    • Aoyama K, Matsubara K, Fujikawa Y, Nagahiro Y, Shimizu K, Umegae N, et al. Nitration of manganese superoxide dismutase in cerebrospinal fl uids is a marker for peroxynitrite-mediated oxidative stress in neurodegenerative diseases. Ann Neurol 2000; 47: 524-527.
    • (2000) Ann Neurol , vol.47 , pp. 524-527
    • Aoyama, K.1    Matsubara, K.2    Fujikawa, Y.3    Nagahiro, Y.4    Shimizu, K.5    Umegae, N.6
  • 43
    • 33646534207 scopus 로고    scopus 로고
    • Beta-Amyloid mediated nitration of manganese superoxide dismutase: Implication for oxidative stress in a APPNLH/NLH X PS-1P264L/ P264L double knock-in mouse model of Alzheimer's disease
    • Anantharaman M, Tangpong J, Keller JN, Murphy MP, Markesbery WR, Kiningham KK, St Clair DK. Beta-Amyloid mediated nitration of manganese superoxide dismutase: Implication for oxidative stress in a APPNLH/NLH X PS-1P264L/ P264L double knock-in mouse model of Alzheimer's disease. Am J Pathol 2006; 168: 1608-1618.
    • (2006) Am J Pathol , vol.168 , pp. 1608-1618
    • Anantharaman, M.1    Tangpong, J.2    Keller, J.N.3    Murphy, M.P.4    Markesbery, W.R.5    Kiningham, K.K.6    St Clair, D.K.7
  • 44
    • 41949139551 scopus 로고    scopus 로고
    • A neuronal model of Alzheimer's disease: An insight into the mechanisms of oxidative stress-mediated mitochondrial injury
    • Sompol P, Ittarat W, Tangpong J, Chen Y, Doubinskaia I, Batinic-Haberle I, et al. A neuronal model of Alzheimer's disease: An insight into the mechanisms of oxidative stress-mediated mitochondrial injury. Neuroscience 2008; 153: 120-130.
    • (2008) Neuroscience , vol.153 , pp. 120-130
    • Sompol, P.1    Ittarat, W.2    Tangpong, J.3    Chen, Y.4    Doubinskaia, I.5    Batinic-Haberle, I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.