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Volumn 9, Issue 5, 2010, Pages 2450-2459

Mitochondrial complex i subunits are decreased in murine nonalcoholic fatty liver disease: Implication of peroxynitrite

Author keywords

Mitochondrial Respiratory Chain; Nitric oxide; Oxidative phosphorylation; Prohibitin; Tyrosine nitrated proteins

Indexed keywords

MANGANESE SUPEROXIDE DISMUTASE; MITOCHONDRIAL PROTEIN; PEROXYNITRITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); TUMOR NECROSIS FACTOR ALPHA ANTIBODY; URIC ACID;

EID: 77952012467     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr9011427     Document Type: Article
Times cited : (38)

References (46)
  • 1
    • 0033038672 scopus 로고    scopus 로고
    • Nonalcoholic fatty liver disease: A spectrum of clinical and pathological severity
    • Matteoni, C. A.; Younossi, Z. M.; Gramlich, T Nonalcoholic fatty liver disease: a spectrum of clinical and pathological severity Gastroenterology 1999, 116, 1413-9
    • (1999) Gastroenterology , vol.116 , pp. 1413-1419
    • Matteoni, C.A.1    Younossi, Z.M.2    Gramlich, T.3
  • 2
    • 85031779447 scopus 로고    scopus 로고
    • The epidemiology and risk factors of NASH
    • Farrell, G. C.; George, J.; Hall, P. de la M.; McCullough, A. J., Eds; Blackwell Publ Ltd: Malden, MA
    • McCullough, A. J. The Epidemiology and Risk Factors of NASH. In Fatty Liver Disease. NASH and Related Disorders; Farrell, G. C.; George, J.; Hall, P. de la M.; McCullough, A. J., Eds; Blackwell Publ Ltd: Malden, MA. 2005; pp 23 - 37
    • (2005) Fatty Liver Disease. NASH and Related Disorders , pp. 23-37
    • McCullough, A.J.1
  • 3
    • 0035078484 scopus 로고    scopus 로고
    • Etiopathogenesis of nonalcoholic steatohepatitis
    • Chitturi, S; Farrell, G. C. Etiopathogenesis of nonalcoholic steatohepatitis Semin. Liver Dis. 2001, 21, 27-41
    • (2001) Semin. Liver Dis. , vol.21 , pp. 27-41
    • Chitturi, S.1    Farrell, G.C.2
  • 4
    • 2642583241 scopus 로고    scopus 로고
    • The ins and outs of mitochondrial dysfunction in NASH
    • Fromenty, B; Robin, M. A.; Igoudjil, A The ins and outs of mitochondrial dysfunction in NASH Diabetes Metab. 2004, 30, 121-38
    • (2004) Diabetes Metab. , vol.30 , pp. 121-138
    • Fromenty, B.1    Robin, M.A.2    Igoudjil, A.3
  • 5
    • 18144444592 scopus 로고    scopus 로고
    • Defective hepatic mitochondrial respiratory chain in patients with nonalcoholic steatohepatitis
    • Pérez-Carreras, M.; Del Hoyo, P.; Martín, M. A. Defective hepatic mitochondrial respiratory chain in patients with nonalcoholic steatohepatitis Hepatology 2003, 38, 999-1007
    • (2003) Hepatology , vol.38 , pp. 999-1007
    • Pérez-Carreras, M.1    Del Hoyo, P.2    Martín, M.A.3
  • 6
    • 33748946183 scopus 로고    scopus 로고
    • Uric acid and anti-TNF antibody improve mitochondrial dysfunction in ob/ob mice
    • Garcia-Ruiz, I.; Rodriguez-Juan, C.; Díaz-Sanjuan, T. Uric acid and anti-TNF antibody improve mitochondrial dysfunction in ob/ob mice Hepatology 2006, 44, 581-91
    • (2006) Hepatology , vol.44 , pp. 581-591
    • Garcia-Ruiz, I.1    Rodriguez-Juan, C.2    Díaz-Sanjuan, T.3
  • 7
    • 33748957197 scopus 로고    scopus 로고
    • Mitochondrial complex I: Structural and functional aspects
    • Lenaz, G.; Fato, R.; Genova, M. L. Mitochondrial complex I: structural and functional aspects Biochim. Biophys. Acta 2006, 1757, 1406-20
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1406-1420
    • Lenaz, G.1    Fato, R.2    Genova, M.L.3
  • 9
    • 0034691658 scopus 로고    scopus 로고
    • Biophysical and structural characterization of proton-translocating NADH-dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia lipolytica
    • Djafarzadeh, R.; Kerscher, S.; Zwicker, K. Biophysical and structural characterization of proton-translocating NADH-dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia lipolytica Biochim. Biophys. Acta 2000, 1459, 230-8
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 230-238
    • Djafarzadeh, R.1    Kerscher, S.2    Zwicker, K.3
  • 10
    • 0038160473 scopus 로고    scopus 로고
    • Analysis of the subunit composition of complex i from bovine heart mitochondria
    • Carroll, J.; Fearnley, I. M.; Shannon, R. J. Analysis of the subunit composition of complex I from bovine heart mitochondria Mol. Cell. Proteomics 2003, 2, 117-26
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 117-126
    • Carroll, J.1    Fearnley, I.M.2    Shannon, R.J.3
  • 11
    • 0038771142 scopus 로고    scopus 로고
    • The nuclear encoded subunits of complex i from bovine heart mitochondria
    • Hirst, J.; Carroll, J.; Fearnley, I. M. The nuclear encoded subunits of complex I from bovine heart mitochondria Biochim. Biophys. Acta 2003, 1604, 135-50
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 135-150
    • Hirst, J.1    Carroll, J.2    Fearnley, I.M.3
  • 12
    • 0029924286 scopus 로고    scopus 로고
    • Electrophoretic techniques for isolation and quantification of oxidative phosphorylation complexes from human tissues
    • DOI 10.1016/S0076-6879(96)64048-8
    • Schägger, H. Electrophoretic techniques for isolation and quantification of oxidative pohosphorylation complexes from human tissues Methods Enzymol. 1996, 264, 555-66 (Pubitemid 26089337)
    • (1996) Methods in Enzymology , vol.264 , pp. 555-566
    • Schagger, H.1
  • 13
    • 0036024975 scopus 로고    scopus 로고
    • Blue native electrophoresis to study mitochondrial and other protein complexes
    • Nijmans, L. G. J.; Henderson, N. S.; Holt, I. J. Blue native electrophoresis to study mitochondrial and other protein complexes Methods 2002, 26, 327-34
    • (2002) Methods , vol.26 , pp. 327-334
    • Nijmans, L.G.J.1    Henderson, N.S.2    Holt, I.J.3
  • 14
    • 0040338446 scopus 로고    scopus 로고
    • Tumor necrosis factor-α increases ATP content in metabolically inhibited L929 cells preceding cell death
    • Sánchez-Alcázar, J. A.; Ruíz-Cabello, J; Hernández-Muñoz, I Tumor necrosis factor-α increases ATP content in metabolically inhibited L929 cells preceding cell death J. Biol. Chem. 1997, 272, 30167-77
    • (1997) J. Biol. Chem. , vol.272 , pp. 30167-30177
    • Sánchez-Alcázar, J.A.1    Ruíz-Cabello, J.2    Hernández-Muñoz, I.3
  • 15
    • 0035937748 scopus 로고    scopus 로고
    • Human complex i defects can be resolved by monoclonal antibody analysis into distinct subunit assembly patterns
    • Triepels, R. H.; Hanson, B. J.; van den Heuve, L. P. Human complex I defects can be resolved by monoclonal antibody analysis into distinct subunit assembly patterns J. Biol. Chem. 2001, 276, 8892-7
    • (2001) J. Biol. Chem. , vol.276 , pp. 8892-8897
    • Triepels, R.H.1    Hanson, B.J.2    Van Den Heuve, L.P.3
  • 16
    • 0041935939 scopus 로고    scopus 로고
    • US National Institute of Health. Bethesda. Maryland., 1997-2007
    • Rasband, W. S. ImageJ. US National Institute of Health. Bethesda. Maryland. http://rsb.info.nih.gov/ij/, 1997-2007.
    • ImageJ
    • Rasband, W.S.1
  • 17
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔCT method
    • Livak, K. J.; Schmittgen, T. D. Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔCT method Methods 2001, 25, 402-8
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 18
    • 0033775615 scopus 로고    scopus 로고
    • Absolute quantification of mRNA using real-time reverse transcription polymerase chain reaction assay
    • Bustin, S. A. Absolute quantification of mRNA using real-time reverse transcription polymerase chain reaction assay J. Mol. Endocrinol. 2000, 25, 169-93
    • (2000) J. Mol. Endocrinol. , vol.25 , pp. 169-193
    • Bustin, S.A.1
  • 19
    • 0141510019 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial complex i due to peroxynitrite. Identification of reactive tyrosines by mass spectrometry
    • Murray, J.; Taylor, S. W.; Zhang, B. Oxidative damage to mitochondrial complex I due to peroxynitrite. Identification of reactive tyrosines by mass spectrometry J. Biol. Chem. 2003, 278, 37223-30
    • (2003) J. Biol. Chem. , vol.278 , pp. 37223-37230
    • Murray, J.1    Taylor, S.W.2    Zhang, B.3
  • 20
    • 2642552056 scopus 로고    scopus 로고
    • Nonalcoholic steatohepatitis (NASH) is associated with hepatocytes mitochondrial DNA depletion
    • Haque, M.; Mirshahi, F.; Campbell-Sargent, C. Nonalcoholic steatohepatitis (NASH) is associated with hepatocytes mitochondrial DNA depletion Hepatology 2002, 36 (Suppl.) 403A
    • (2002) Hepatology , vol.36 , Issue.SUPPL.
    • Haque, M.1    Mirshahi, F.2    Campbell-Sargent, C.3
  • 21
    • 0031469841 scopus 로고    scopus 로고
    • Analysis of a form of oxidative DNA damage 8-hydroxy-20-deoxyguanosine, as a marker of cellular oxidative stress during carcinogenesis
    • Kasai, H. Analysis of a form of oxidative DNA damage 8-hydroxy-20- deoxyguanosine, as a marker of cellular oxidative stress during carcinogenesis Mutat. Res. 1997, 387, 147-63
    • (1997) Mutat. Res. , vol.387 , pp. 147-163
    • Kasai, H.1
  • 22
    • 0031032817 scopus 로고    scopus 로고
    • Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress
    • Yakes, F. M.; Van Houten, B. Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 514-9
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 514-519
    • Yakes, F.M.1    Van Houten, B.2
  • 23
    • 7044264899 scopus 로고    scopus 로고
    • Oxidative DNA damage and DNA repair enzyme expression are inversely related in murine models of fatty liver disease
    • Gao, D.; Wei, C.; Chen, L Oxidative DNA damage and DNA repair enzyme expression are inversely related in murine models of fatty liver disease Am. J. Physiol.: Gastrointest. Liver Physiol. 2004, 287, G1070-7
    • (2004) Am. J. Physiol.: Gastrointest. Liver Physiol. , vol.287 , pp. 1070-1077
    • Gao, D.1    Wei, C.2    Chen, L.3
  • 24
    • 0034640248 scopus 로고    scopus 로고
    • Hydrogen peroxide- and peroxynitrite-induced mitochondrial DNA damage and dysfunction in vascular endothelial and smooth muscle cells
    • Ballinger, S. W.; Patterson, C.; Yan, C. N. Hydrogen peroxide- and peroxynitrite-induced mitochondrial DNA damage and dysfunction in vascular endothelial and smooth muscle cells Circ. Res. 2000, 86, 960-6
    • (2000) Circ. Res. , vol.86 , pp. 960-966
    • Ballinger, S.W.1    Patterson, C.2    Yan, C.N.3
  • 25
    • 27144508153 scopus 로고    scopus 로고
    • Peroxynitrite-Induced mitochondrial and endonuclease-mediated nuclear DNA damage in acetaminophen Hepatotoxicity
    • Cover, C.; Mansouri, A.; Knight, T. R. Peroxynitrite-Induced mitochondrial and endonuclease-mediated nuclear DNA damage in acetaminophen Hepatotoxicity J. Pharmacol. Exp. Ther. 2005, 315, 879-87
    • (2005) J. Pharmacol. Exp. Ther. , vol.315 , pp. 879-887
    • Cover, C.1    Mansouri, A.2    Knight, T.R.3
  • 27
    • 0029135397 scopus 로고
    • Formation of 8-nitroguanine by the reaction of guanine with peroxynitrite in vitro
    • Yermilov, V.; Rubio, J.; Becchi, M. Formation of 8-nitroguanine by the reaction of guanine with peroxynitrite in vitro Carcinogenesis 1995, 16, 2045-50
    • (1995) Carcinogenesis , vol.16 , pp. 2045-2050
    • Yermilov, V.1    Rubio, J.2    Becchi, M.3
  • 28
    • 9144267069 scopus 로고    scopus 로고
    • Structural organization of mitochondrial human complex I: Role of the ND4 and ND5 mitochondria-encoded subunits and interaction with prohibitin
    • Bourges, I.; Ramus, C.; Mousson de Camaret, B Structural organization of mitochondrial human complex I: role of the ND4 and ND5 mitochondria-encoded subunits and interaction with prohibitin Biochem. J. 2004, 383, 491-9
    • (2004) Biochem. J. , vol.383 , pp. 491-499
    • Bourges, I.1    Ramus, C.2    Mousson De Camaret, B.3
  • 29
    • 33745242989 scopus 로고    scopus 로고
    • Respiratory chain supercomplexes set the threshold for respiration defects in human mtDNA mutant cybrids
    • DAurelio, M.; Gajewski, C. D.; Lenaz, G. Respiratory chain supercomplexes set the threshold for respiration defects in human mtDNA mutant cybrids Hum. Mol. Genet. 2006, 15, 2157-69
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 2157-2169
    • Daurelio, M.1    Gajewski, C.D.2    Lenaz, G.3
  • 30
    • 12144291508 scopus 로고    scopus 로고
    • Respiratory complex III is required to maintain complex i in mammalian mitochondria
    • Acin-Pérez, R.; Bayona-Bafaluy, M. P.; Fernández-Silva, P. Respiratory complex III is required to maintain complex I in mammalian mitochondria Mol. Cell 2004, 13, 805-15
    • (2004) Mol. Cell , vol.13 , pp. 805-815
    • Acin-Pérez, R.1    Bayona-Bafaluy, M.P.2    Fernández-Silva, P.3
  • 31
    • 27144528747 scopus 로고    scopus 로고
    • Human mitochondrial complex i assembly is mediated by NDUFAF1
    • Vogel, R. O.; Janssen, R. J.; Ugalde, C. Human mitochondrial complex I assembly is mediated by NDUFAF1 FEBS J. 2005, 272, 5317-26
    • (2005) FEBS J. , vol.272 , pp. 5317-5326
    • Vogel, R.O.1    Janssen, R.J.2    Ugalde, C.3
  • 32
    • 26444488636 scopus 로고    scopus 로고
    • A molecular chaperone for mitochondrial complex i assembly is mutated in a progressive encephalopathy
    • Ogilvie, I.; Kennaway, N. G.; Shoubridge, E. A. A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy J. Clin. Invest. 2005, 115, 2784-92
    • (2005) J. Clin. Invest. , vol.115 , pp. 2784-2792
    • Ogilvie, I.1    Kennaway, N.G.2    Shoubridge, E.A.3
  • 33
    • 56349102165 scopus 로고    scopus 로고
    • Prohibitin function within mitochondria: Essential roles for cell proliferation and cristae morphogenesis
    • Merkwirth, C.; Langer, T. Prohibitin function within mitochondria: Essential roles for cell proliferation and cristae morphogenesis Biochim. Biophys. Acta 2009, 1793, 27-32
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 27-32
    • Merkwirth, C.1    Langer, T.2
  • 34
    • 0036161635 scopus 로고    scopus 로고
    • The mitochondrial PHB complex: Roles in mitochondrial respiratory complex assembly, ageing and degenerative disease
    • Nijtmans, L. G.; Artal, S. M.; Grivell, L. A. The mitochondrial PHB complex: roles in mitochondrial respiratory complex assembly, ageing and degenerative disease Cell. Mol. Life Sci. 2002, 59, 143-55
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 143-155
    • Nijtmans, L.G.1    Artal, S.M.2    Grivell, L.A.3
  • 35
    • 0032954927 scopus 로고    scopus 로고
    • Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria
    • Steglich, G.; Neupert, W.; Langer, T. Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria Mol. Cell. Biol. 1999, 19, 3435-42
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3435-3442
    • Steglich, G.1    Neupert, W.2    Langer, T.3
  • 36
    • 0034213904 scopus 로고    scopus 로고
    • Prohibitins act as a membranebound chaperone for the stabilisation of mitochondrial proteins
    • Nijtmans, L. G. J.; de Jong, L.; Artal Sanz, M. Prohibitins act as a membranebound chaperone for the stabilisation of mitochondrial proteins EMBO J.. 2000, 19, 2444-51
    • (2000) EMBO J. , vol.19 , pp. 2444-2451
    • Nijtmans, L.G.J.1    De Jong, L.2    Artal Sanz, M.3
  • 37
    • 0037453055 scopus 로고    scopus 로고
    • Functional proteomics of nonalcoholic steatohepatitis: Mitochondrial proteins as targets of S-adenosylmethionine
    • Santamaría, E.; Avila, M. A.; Latasa, M. U. Functional proteomics of nonalcoholic steatohepatitis: Mitochondrial proteins as targets of S-adenosylmethionine Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 3065-70
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3065-3070
    • Santamaría, E.1    Avila, M.A.2    Latasa, M.U.3
  • 39
    • 0036890524 scopus 로고    scopus 로고
    • Peroxynitrite reactions and formation in mitochondria
    • Radi, R.; Cassina, A.; Hodara, R. Peroxynitrite reactions and formation in mitochondria Free Radical Biol. Med. 2002, 33, 1451-64
    • (2002) Free Radical Biol. Med. , vol.33 , pp. 1451-1464
    • Radi, R.1    Cassina, A.2    Hodara, R.3
  • 40
    • 0036244508 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite interactions with mitochondria
    • Radi, R.; Cassina, A.; Hodara, R.. Nitric oxide and peroxynitrite interactions with mitochondria Biol. Chem. 2002, 383, 401-9
    • (2002) Biol. Chem. , vol.383 , pp. 401-409
    • Radi, R.1    Cassina, A.2    Hodara, R.3
  • 41
    • 0033592423 scopus 로고    scopus 로고
    • Peroxynitrite modification of protein thiols: Oxidation, nitrosylation, and S-glutathiolation of functionally important cysteine residue(s) in the sarcoplasmic reticulum Ca-ATPase
    • Viner, R. I.; Williams, T. D.; Schoneich, C. Peroxynitrite modification of protein thiols: oxidation, nitrosylation, and S-glutathiolation of functionally important cysteine residue(s) in the sarcoplasmic reticulum Ca-ATPase Biochemistry 1999, 38, 12408-15
    • (1999) Biochemistry , vol.38 , pp. 12408-12415
    • Viner, R.I.1    Williams, T.D.2    Schoneich, C.3
  • 42
    • 0036268393 scopus 로고    scopus 로고
    • A reassessment of the peroxynitrite scavenging activity of uric acid
    • Whiteman, M.; Ketsawatsakul, U.; Halliwell, B. A reassessment of the peroxynitrite scavenging activity of uric acid Ann. N.Y. Acad. Sci. 2002, 962, 242-59
    • (2002) Ann. N.Y. Acad. Sci. , vol.962 , pp. 242-259
    • Whiteman, M.1    Ketsawatsakul, U.2    Halliwell, B.3
  • 43
    • 21344461736 scopus 로고    scopus 로고
    • Interactions of peroxynitrite with uric acid in the presence of ascorbate and thiols: Implications for uncoupling endothelial nitric oxide synthase
    • Kuzkaya, N.; Weissmann, N.; Harrison, D. G. Interactions of peroxynitrite with uric acid in the presence of ascorbate and thiols: implications for uncoupling endothelial nitric oxide synthase Biochem. Pharmacol. 2005, 70, 343-54
    • (2005) Biochem. Pharmacol. , vol.70 , pp. 343-354
    • Kuzkaya, N.1    Weissmann, N.2    Harrison, D.G.3
  • 44
    • 2342591361 scopus 로고    scopus 로고
    • Pivotal role of superoxide anion and beneficial effect of antioxidant molecules in murine steatohepatitis
    • Laurent, A.; Nicco, C.; Tran Van Nhieu, J. Pivotal role of superoxide anion and beneficial effect of antioxidant molecules in murine steatohepatitis Hepatology 2004, 39, 1277-85
    • (2004) Hepatology , vol.39 , pp. 1277-1285
    • Laurent, A.1    Nicco, C.2    Tran Van Nhieu, J.3
  • 45
    • 0035084699 scopus 로고    scopus 로고
    • Nonalcoholic steatohepatitis: Association of insulin resistance and mitochondrial abnormalities
    • Sanyal, A. J.; Campbell-Sargent, C.; Mirshahi, F. Nonalcoholic steatohepatitis: association of insulin resistance and mitochondrial abnormalities Gastroenterology 2001, 120, 1183-92
    • (2001) Gastroenterology , vol.120 , pp. 1183-1192
    • Sanyal, A.J.1    Campbell-Sargent, C.2    Mirshahi, F.3
  • 46
    • 3543008400 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiratory complex i by nitric oxide, peroxynitrite and S-nitrosothiols
    • Brown, G. C.; Borutaite, V. Inhibition of mitochondrial respiratory complex I by nitric oxide, peroxynitrite and S-nitrosothiols Biochim. Biophys. Acta 2004, 1658, 44-9
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 44-49
    • Brown, G.C.1    Borutaite, V.2


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