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Volumn 3, Issue 6, 2012, Pages

HtrA2 deficiency causes mitochondrial uncoupling through the F 1F0-ATP synthase and consequent ATP depletion

Author keywords

ATP synthase; HtrA2; mitochondria; uncoupling

Indexed keywords

ADENOSINE TRIPHOSPHATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SERINE PROTEINASE OMI; MITOCHONDRIAL PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; REACTIVE OXYGEN METABOLITE; SERINE PROTEINASE;

EID: 84863455932     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2012.77     Document Type: Article
Times cited : (32)

References (31)
  • 2
    • 7644230386 scopus 로고    scopus 로고
    • Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice
    • Martins LM, Morrison A, Klupsch K, Fedele V, Moisoi N, Teismann P et al. Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice. Mol Cell Biol 2004; 24: 9848-9862.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 9848-9862
    • Martins, L.M.1    Morrison, A.2    Klupsch, K.3    Fedele, V.4    Moisoi, N.5    Teismann, P.6
  • 4
    • 44849115171 scopus 로고    scopus 로고
    • Genetic variability in the mitochondrial serine protease HTRA2 contributes to risk for parkinson disease
    • Bogaerts V, Nuytemans K, Reumers J, Pals P, Engelborghs S, Pickut B et al. Genetic variability in the mitochondrial serine protease HTRA2 contributes to risk for Parkinson disease. Hum Mutat 2008; 29: 832-840.
    • (2008) Hum. Mutat. , vol.29 , pp. 832-840
    • Bogaerts, V.1    Nuytemans, K.2    Reumers, J.3    Pals, P.4    Engelborghs, S.5    Pickut, B.6
  • 5
    • 77950616071 scopus 로고    scopus 로고
    • Modulation of mitochondrial function and morphology by interaction of Omi/HtrA2 with the mitochondrial fusion factor OPA1
    • Kieper N, Holmstrom KM, Ciceri D, Fiesel FC, Wolburg H, Ziviani E et al. Modulation of mitochondrial function and morphology by interaction of Omi/HtrA2 with the mitochondrial fusion factor OPA1. Exp Cell Res 2010; 316: 1213-1224.
    • (2010) Exp. Cell Res. , vol.316 , pp. 1213-1224
    • Kieper, N.1    Holmstrom, K.M.2    Ciceri, D.3    Fiesel, F.C.4    Wolburg, H.5    Ziviani, E.6
  • 6
    • 67650718212 scopus 로고    scopus 로고
    • Drosophila HtrA2 is dispensable for apoptosis but acts downstream of PINK1 independently from Parkin
    • Tain LS, Chowdhury RB, Tao RN, Plun-Favreau H, Moisoi N, Martins LM et al. Drosophila HtrA2 is dispensable for apoptosis but acts downstream of PINK1 independently from Parkin. Cell Death Differ 2009; 16: 1118-1125.
    • (2009) Cell Death Differ. , vol.16 , pp. 1118-1125
    • Tain, L.S.1    Chowdhury, R.B.2    Tao, R.N.3    Plun-Favreau, H.4    Moisoi, N.5    Martins, L.M.6
  • 8
    • 0034307759 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and glutamate excitotoxicity in cultured cerebellar granule cells
    • Ward MW, Rego AC, Frenguelli BG, Nicholls DG. Mitochondrial membrane potential and glutamate excitotoxicity in cultured cerebellar granule cells. J Neurosci 2000; 20: 7208-7219.
    • (2000) J. Neurosci. , vol.20 , pp. 7208-7219
    • Ward, M.W.1    Rego, A.C.2    Frenguelli, B.G.3    Nicholls, D.G.4
  • 9
    • 0035869336 scopus 로고    scopus 로고
    • Mitochondria control ampa/kainate receptor-induced cytoplasmic calcium deregulation in rat cerebellar granule cells
    • Rego AC, Ward MW, Nicholls DG. Mitochondria control ampa/kainate receptor-induced cytoplasmic calcium deregulation in rat cerebellar granule cells. J Neurosci 2001; 21: 1893-1901.
    • (2001) J. Neurosci. , vol.21 , pp. 1893-1901
    • Rego, A.C.1    Ward, M.W.2    Nicholls, D.G.3
  • 10
    • 77049233362 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation I kinetics of oxygen utilization
    • Chance B, Williams GR. Respiratory enzymes in oxidative phosphorylation. I. Kinetics of oxygen utilization. J Biol Chem 1955; 217: 383-393.
    • (1955) J. Biol. Chem. , vol.217 , pp. 383-393
    • Chance, B.1    Williams, G.R.2
  • 11
    • 0034740585 scopus 로고    scopus 로고
    • DeltaPsi(m)-Dependent and -independent production of reactive oxygen species by rat brain mitochondria
    • Votyakova TV, Reynolds IJ. DeltaPsi(m)-Dependent and -independent production of reactive oxygen species by rat brain mitochondria. J Neurochem 2001; 79: 266-277.
    • (2001) J. Neurochem. , vol.79 , pp. 266-277
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 13
    • 0033598828 scopus 로고    scopus 로고
    • Regulation of mitochondrial ATP synthesis by calcium: evidence for a long-term metabolic priming
    • USA
    • Jouaville LS, Pinton P, Bastianutto C, Rutter GA, Rizzuto R. Regulation of mitochondrial ATP synthesis by calcium: evidence for a long-term metabolic priming. Proc Natl Acad Sci USA 1999; 96: 13807-13812.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 13807-13812
    • Jouaville, L.S.1    Pinton, P.2    Bastianutto, C.3    Rutter, G.A.4    Rizzuto, R.5
  • 14
    • 0029994239 scopus 로고    scopus 로고
    • The relationship between mitochondrial state, ATP hydrolysis, [Mg2]i and [Ca2]i studied in isolated rat cardiomyocytes
    • Leyssens A, Nowicky AV, Patterson L, Crompton M, Duchen MR. The relationship between mitochondrial state, ATP hydrolysis, [Mg2]i and [Ca2]i studied in isolated rat cardiomyocytes. J Physiol 1996; 496 (Part 1): 111-128.
    • (1996) J. Physiol. , vol.496 , Issue.PART 1 , pp. 111-128
    • Leyssens, A.1    Nowicky, A.V.2    Patterson, L.3    Crompton, M.4    Duchen, M.R.5
  • 15
    • 33846818524 scopus 로고    scopus 로고
    • Three distinct mechanisms generate oxygen free radicals in neurons and contribute to cell death during anoxia and reoxygenation
    • Abramov AY, Scorziello A, Duchen MR. Three distinct mechanisms generate oxygen free radicals in neurons and contribute to cell death during anoxia and reoxygenation. J Neurosci 2007; 27: 1129-1138.
    • (2007) J. Neurosci. , vol.27 , pp. 1129-1138
    • Abramov, A.Y.1    Scorziello, A.2    Duchen, M.R.3
  • 16
    • 0142246441 scopus 로고    scopus 로고
    • Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice
    • Jones JM, Datta P, Srinivasula SM, Ji W, Gupta S, Zhang Z et al. Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice. Nature 2003; 425: 721-727.
    • (2003) Nature , vol.425 , pp. 721-727
    • Jones, J.M.1    Datta, P.2    Srinivasula, S.M.3    Ji, W.4    Gupta, S.5    Zhang, Z.6
  • 17
    • 0018864653 scopus 로고
    • Influence of plasma-membrane depolarization on the respiration and membrane potential of internal mitochondria determined in situ
    • Scott ID, Nicholls DG. Energy transduction in intact synaptosomes. Influence of plasma-membrane depolarization on the respiration and membrane potential of internal mitochondria determined in situ. Biochem J 1980; 186: 21-33.
    • (1980) Biochem. J. , vol.186 , pp. 21-33
    • Scott, I.D.1    Nicholls, D.G.2
  • 18
    • 0026612451 scopus 로고
    • F0F1-ATPase gamma subunit mutations perturb the coupling between catalysis and transport
    • Shin K, Nakamoto RK, Maeda M, Futai M. F0F1-ATPase gamma subunit mutations perturb the coupling between catalysis and transport. J Biol Chem 1992; 267: 20835-20839.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20835-20839
    • Shin, K.1    Nakamoto, R.K.2    Maeda, M.3    Futai, M.4
  • 19
    • 0028177540 scopus 로고
    • Suppressor mutations in F1 subunit epsilon recouple ATP-driven HP translocation in uncoupled Q42E subunit c mutant of Escherichia coli F1F0 ATP synthase
    • Zhang Y, Oldenburg M, Fillingame RH. Suppressor mutations in F1 subunit epsilon recouple ATP-driven H translocation in uncoupled Q42E subunit c mutant of Escherichia coli F1F0 ATP synthase. J Biol Chem 1994; 269: 10221-10224.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10221-10224
    • Zhang, Y.1    Oldenburg, M.2    Fillingame, R.H.3
  • 22
    • 60849097548 scopus 로고    scopus 로고
    • Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response
    • Moisoi N, Klupsch K, Fedele V, East P, Sharma S, Renton A et al. Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response. Cell Death Differ 2009; 16: 449-464.
    • (2009) Cell Death Differ. , vol.16 , pp. 449-464
    • Moisoi, N.1    Klupsch, K.2    Fedele, V.3    East, P.4    Sharma, S.5    Renton, A.6
  • 23
    • 45149128904 scopus 로고    scopus 로고
    • Mitochondrial protein quality control by the proteasome involves ubiquitination and the protease Omi
    • Radke S, Chander H, Schafer P, Meiss G, Kruger R, Schulz JB et al. Mitochondrial protein quality control by the proteasome involves ubiquitination and the protease Omi. J Biol Chem 2008; 283: 12681-12685.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12681-12685
    • Radke, S.1    Chander, H.2    Schafer, P.3    Meiss, G.4    Kruger, R.5    Schulz, J.B.6
  • 24
    • 77956090193 scopus 로고    scopus 로고
    • Mitochondrial protein import: from proteomics to functional mechanisms
    • Schmidt O, Pfanner N, Meisinger C. Mitochondrial protein import: from proteomics to functional mechanisms. Nat Rev Mol Cell Biol 2010; 11: 655-667.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 655-667
    • Schmidt, O.1    Pfanner, N.2    Meisinger, C.3
  • 25
    • 35748935851 scopus 로고    scopus 로고
    • The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1
    • Plun-Favreau H, Klupsch K, Moisoi N, Gandhi S, Kjaer S, Frith D et al. The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1. Nat Cell Biol 2007; 9: 1243-1252.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1243-1252
    • Plun-Favreau, H.1    Klupsch, K.2    Moisoi, N.3    Gandhi, S.4    Kjaer, S.5    Frith, D.6
  • 26
    • 79955878620 scopus 로고    scopus 로고
    • Fumonisin B1 inhibits mitochondrial respiration and deregulates calcium homeostasis-implication to mechanism of cell toxicity
    • Domijan AM, Abramov AY. Fumonisin B1 inhibits mitochondrial respiration and deregulates calcium homeostasis-implication to mechanism of cell toxicity. Int J Biochem Cell Biol 2011; 43: 897-904.
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 897-904
    • Domijan, A.M.1    Abramov, A.Y.2
  • 27
  • 28
    • 2442540299 scopus 로고    scopus 로고
    • Pro-apoptotic proteins released from the mitochondria regulate the protein composition and caspaseprocessing activity of the native Apaf-1/caspase-9 apoptosome complex
    • Twiddy D, Brown DG, Adrain C, Jukes R, Martin SJ, Cohen GM et al. Pro-apoptotic proteins released from the mitochondria regulate the protein composition and caspaseprocessing activity of the native Apaf-1/caspase-9 apoptosome complex. J Biol Chem 2004; 279: 19665-19682.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19665-19682
    • Twiddy, D.1    Brown, D.G.2    Adrain, C.3    Jukes, R.4    Martin, S.J.5    Cohen, G.M.6
  • 29
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 2001; 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 30
    • 0346218117 scopus 로고    scopus 로고
    • Pivotal role of nucleotide P2-2 receptor subunit of the ATP-gated ion channel mediating ventilatory responses to hypoxia
    • Rong W, Gourine AV, Cockayne DA, Xiang Z, Ford AP, Spyer KM et al. Pivotal role of nucleotide P2-2 receptor subunit of the ATP-gated ion channel mediating ventilatory responses to hypoxia. J Neurosci 2003; 23: 11315-11321.
    • (2003) J. Neurosci. , vol.23 , pp. 11315-11321
    • Rong, W.1    Gourine, A.V.2    Cockayne, D.A.3    Xiang, Z.4    Ford, A.P.5    Spyer, K.M.6
  • 31
    • 52049100103 scopus 로고    scopus 로고
    • A role for TASK-1 (KCNK3) channels in the chemosensory control of breathing
    • Trapp S, Aller MI, Wisden W, Gourine AV. A role for TASK-1 (KCNK3) channels in the chemosensory control of breathing. J Neurosci 2008; 28: 8844-8850.
    • (2008) J. Neurosci. , vol.28 , pp. 8844-8850
    • Trapp, S.1    Aller, M.I.2    Wisden, W.3    Gourine, A.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.