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Volumn 7, Issue 3, 2014, Pages 500-509

Oxidative post-translational modifications develop LONP1 dysfunction in pressure overload heart failure

Author keywords

Heart failure; Mitochondria; Post translational; Protein processing

Indexed keywords

CATALASE; CYSTEINE; ENDOPEPTIDASE LA; SUPEROXIDE DISMUTASE; TYROSINE;

EID: 84902782383     PISSN: 19413289     EISSN: 19413297     Source Type: Journal    
DOI: 10.1161/CIRCHEARTFAILURE.113.001062     Document Type: Article
Times cited : (55)

References (37)
  • 1
    • 84880673845 scopus 로고    scopus 로고
    • Pharmacological approaches to restore mitochondrial function
    • Andreux PA, Houtkooper RH, Auwerx J. Pharmacological approaches to restore mitochondrial function. Nat Rev Drug Discov. 2013;12:465-483.
    • (2013) Nat Rev Drug Discov , vol.12 , pp. 465-483
    • Andreux, P.A.1    Houtkooper, R.H.2    Auwerx, J.3
  • 5
    • 77953871095 scopus 로고    scopus 로고
    • Assembly factors and ATP-dependent proteases in cytochrome c oxidase biogenesis
    • Stiburek L, Zeman J. Assembly factors and ATP-dependent proteases in cytochrome c oxidase biogenesis. Biochim Biophys Acta. 2010;1797:1149-1158.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1149-1158
    • Stiburek, L.1    Zeman, J.2
  • 6
    • 84862783606 scopus 로고    scopus 로고
    • Substrate-and isoform-specific proteome stability in normal and stressed cardiac mitochondria
    • Lau E, Wang D, Zhang J, Yu H, Lam MP, Liang X, Zong N, Kim TY, Ping P. Substrate-and isoform-specific proteome stability in normal and stressed cardiac mitochondria. Circ Res. 2012;110:1174-1178.
    • (2012) Circ Res , vol.110 , pp. 1174-1178
    • Lau, E.1    Wang, D.2    Zhang, J.3    Yu, H.4    Lam, M.P.5    Liang, X.6    Zong, N.7    Kim, T.Y.8    Ping, P.9
  • 7
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota DA, Davies KJ. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat Cell Biol. 2002;4:674-680.
    • (2002) Nat Cell Biol , vol.4 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.2
  • 8
    • 41949134709 scopus 로고    scopus 로고
    • Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates
    • Lee I, Suzuki CK. Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates. Biochim Biophys Acta. 2008;1784:727-735.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 727-735
    • Lee, I.1    Suzuki, C.K.2
  • 9
    • 31344455097 scopus 로고    scopus 로고
    • Proteomic analysis of mitochondrial protein turnover: Identification of novel substrate proteins of the matrix protease pim1
    • Major T, von Janowsky B, Ruppert T, Mogk A, Voos W. Proteomic analysis of mitochondrial protein turnover: identification of novel substrate proteins of the matrix protease pim1. Mol Cell Biol. 2006;26:762-776.
    • (2006) Mol Cell Biol , vol.26 , pp. 762-776
    • Major, T.1    Von Janowsky, B.2    Ruppert, T.3    Mogk, A.4    Voos, W.5
  • 13
    • 77950989801 scopus 로고    scopus 로고
    • AMPKalpha2 deletion causes aberrant expression and activation of NAD(P)H oxidase and consequent endothelial dysfunction in vivo: Role of 26S proteasomes
    • Wang S, Zhang M, Liang B, Xu J, Xie Z, Liu C, Viollet B, Yan D, Zou MH. AMPKalpha2 deletion causes aberrant expression and activation of NAD(P)H oxidase and consequent endothelial dysfunction in vivo: role of 26S proteasomes. Circ Res. 2010;106:1117-1128.
    • (2010) Circ Res , vol.106 , pp. 1117-1128
    • Wang, S.1    Zhang, M.2    Liang, B.3    Xu, J.4    Xie, Z.5    Liu, C.6    Viollet, B.7    Yan, D.8    Zou, M.H.9
  • 16
    • 46649090918 scopus 로고    scopus 로고
    • Protein tyrosine nitration-functional alteration or just a biomarker?
    • Souza JM, Peluffo G, Radi R. Protein tyrosine nitration-functional alteration or just a biomarker? Free Radic Biol Med. 2008;45:357-366.
    • (2008) Free Radic Biol Med , vol.45 , pp. 357-366
    • Souza, J.M.1    Peluffo, G.2    Radi, R.3
  • 17
    • 5544237716 scopus 로고    scopus 로고
    • Reactive oxygen species as mediators of angiogenesis signaling: Role of NAD(P)H oxidase
    • Ushio-Fukai M, Alexander RW. Reactive oxygen species as mediators of angiogenesis signaling: role of NAD(P)H oxidase. Mol Cell Biochem. 2004;264:85-97.
    • (2004) Mol Cell Biochem , vol.264 , pp. 85-97
    • Ushio-Fukai, M.1    Alexander, R.W.2
  • 18
    • 38749126464 scopus 로고    scopus 로고
    • Towards the control of intracellular protein turnover: Mitochondrial Lon protease inhibitors versus proteasome inhibitors
    • Bayot A, Basse N, Lee I, Gareil M, Pirotte B, Bulteau AL, Friguet B, Reboud-Ravaux M. Towards the control of intracellular protein turnover: mitochondrial Lon protease inhibitors versus proteasome inhibitors. Biochimie. 2008;90:260-269.
    • (2008) Biochimie , vol.90 , pp. 260-269
    • Bayot, A.1    Basse, N.2    Lee, I.3    Gareil, M.4    Pirotte, B.5    Bulteau, A.L.6    Friguet, B.7    Reboud-Ravaux, M.8
  • 19
    • 9644301105 scopus 로고    scopus 로고
    • Age-related impairment of mitochondrial matrix aconitase and ATP-stimulated protease in rat liver and heart
    • Delaval E, Perichon M, Friguet B. Age-related impairment of mitochondrial matrix aconitase and ATP-stimulated protease in rat liver and heart. Eur J Biochem. 2004;271:4559-4564.
    • (2004) Eur J Biochem , vol.271 , pp. 4559-4564
    • Delaval, E.1    Perichon, M.2    Friguet, B.3
  • 20
    • 0037517056 scopus 로고    scopus 로고
    • Changes in rat liver mitochondria with aging. Lon proteaselike reactivity and N(epsilon)-carboxymethyllysine accumulation in the matrix
    • Bakala H, Delaval E, Hamelin M, Bismuth J, Borot-Laloi C, Corman B, Friguet B. Changes in rat liver mitochondria with aging. Lon proteaselike reactivity and N(epsilon)-carboxymethyllysine accumulation in the matrix. Eur J Biochem. 2003;270:2295-2302.
    • (2003) Eur J Biochem , vol.270 , pp. 2295-2302
    • Bakala, H.1    Delaval, E.2    Hamelin, M.3    Bismuth, J.4    Borot-Laloi, C.5    Corman, B.6    Friguet, B.7
  • 21
    • 48349134855 scopus 로고    scopus 로고
    • Inactivation of brain mitochondrial Lon protease by peroxynitrite precedes electron transport chain dysfunction
    • Stanyer L, Jorgensen W, Hori O, Clark JB, Heales SJ. Inactivation of brain mitochondrial Lon protease by peroxynitrite precedes electron transport chain dysfunction. Neurochem Int. 2008;53:95-101.
    • (2008) Neurochem Int , vol.53 , pp. 95-101
    • Stanyer, L.1    Jorgensen, W.2    Hori, O.3    Clark, J.B.4    Heales, S.J.5
  • 22
    • 45149128904 scopus 로고    scopus 로고
    • Mitochondrial protein quality control by the proteasome involves ubiquitination and the protease Omi
    • Radke S, Chander H, Schäfer P, Meiss G, Krüger R, Schulz JB, Germain D. 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    Schäfer, P.3    Meiss, G.4    Krüger, R.5    Schulz, J.B.6    Germain, D.7
  • 23
    • 84876374189 scopus 로고    scopus 로고
    • Role of the ubiquitin proteasome system in the heart
    • Pagan J, Seto T, Pagano M, Cittadini A. Role of the ubiquitin proteasome system in the heart. Circ Res. 2013;112:1046-1058.
    • (2013) Circ Res , vol.112 , pp. 1046-1058
    • Pagan, J.1    Seto, T.2    Pagano, M.3    Cittadini, A.4
  • 27
    • 76649093912 scopus 로고    scopus 로고
    • Degradation of an intramitochondrial protein by the cytosolic proteasome
    • Azzu V, Brand MD. Degradation of an intramitochondrial protein by the cytosolic proteasome. J Cell Sci. 2010;123(Pt 4):578-585.
    • (2010) J Cell Sci , vol.123 , Issue.PART 4 , pp. 578-585
    • Azzu, V.1    Brand, M.D.2
  • 31
    • 33645474310 scopus 로고    scopus 로고
    • Differential protein expression in hypertrophic heart with and without hypertension in spontaneously hypertensive rats
    • Jin X, Xia L, Wang LS, Shi JZ, Zheng Y, Chen WL, Zhang L, Liu ZG, Chen GQ, Fang NY. Differential protein expression in hypertrophic heart with and without hypertension in spontaneously hypertensive rats. Proteomics. 2006;6:1948-1956.
    • (2006) Proteomics , vol.6 , pp. 1948-1956
    • Jin, X.1    Xia, L.2    Wang, L.S.3    Shi, J.Z.4    Zheng, Y.5    Chen, W.L.6    Zhang, L.7    Liu, Z.G.8    Chen, G.Q.9    Fang, N.Y.10
  • 32
    • 84555188518 scopus 로고    scopus 로고
    • Mitochondrial proteome remodelling in pressure overload- induced heart failure: The role of mitochondrial oxidative stress
    • Dai DF, Hsieh EJ, Liu Y, Chen T, Beyer RP, Chin MT, MacCoss MJ, Rabinovitch PS. Mitochondrial proteome remodelling in pressure overload- induced heart failure: the role of mitochondrial oxidative stress. Cardiovasc Res. 2012;93:79-88.
    • (2012) Cardiovasc Res , vol.93 , pp. 79-88
    • Dai, D.F.1    Hsieh, E.J.2    Liu, Y.3    Chen, T.4    Beyer, R.P.5    Chin, M.T.6    Maccoss, M.J.7    Rabinovitch, P.S.8
  • 33
    • 66749100634 scopus 로고    scopus 로고
    • Alterations of mitochondrial enzymes contribute to cardiac hypertrophy before hypertension development in spontaneously hypertensive rats
    • Meng C, Jin X, Xia L, Shen SM, Wang XL, Cai J, Chen GQ, Wang LS, Fang NY. Alterations of mitochondrial enzymes contribute to cardiac hypertrophy before hypertension development in spontaneously hypertensive rats. J Proteome Res. 2009;8:2463-2475.
    • (2009) J Proteome Res , vol.8 , pp. 2463-2475
    • Meng, C.1    Jin, X.2    Xia, L.3    Shen, S.M.4    Wang, X.L.5    Cai, J.6    Chen, G.Q.7    Wang, L.S.8    Fang, N.Y.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.