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Volumn 652, Issue 1-3, 2011, Pages 15-22

The β-adrenoceptor agonist isoproterenol promotes the activity of respiratory chain complex i and lowers cellular reactive oxygen species in fibroblasts and heart myoblasts

Author keywords

adrenoceptor agonists; Complex I; Isoproterenol; Mitochondria; Reactive oxygen species cellular balance

Indexed keywords

ADENYLATE CYCLASE; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; ISOPRENALINE; OKADAIC ACID; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

EID: 78650867108     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejphar.2010.11.016     Document Type: Article
Times cited : (33)

References (35)
  • 3
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH: Quinone oxidoreductase (complex I)
    • U. Brandt Energy converting NADH: quinone oxidoreductase (complex I) Annu. Rev. Biochem. 75 2006 69 92
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 69-92
    • Brandt, U.1
  • 4
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • E. Cadenas, and K.J. Davies Mitochondrial free radical generation, oxidative stress, and aging Free Radic. Biol. Med. 29 2000 222 230
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 7
    • 77049233362 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. I. Kinetics of oxygen utilization
    • B. Chance, and G.R. Williams Respiratory enzymes in oxidative phosphorylation. I. Kinetics of oxygen utilization J. Biol. Chem. 217 1955 383 393
    • (1955) J. Biol. Chem. , vol.217 , pp. 383-393
    • Chance, B.1    Williams, G.R.2
  • 8
    • 61649101759 scopus 로고    scopus 로고
    • Control of OXPHOS efficiency by complex i in brain mitochondria
    • T. Cocco, C. Pacelli, P. Sgobbo, and G. Villani Control of OXPHOS efficiency by complex I in brain mitochondria Neurobiol. Aging 30 2009 622 629
    • (2009) Neurobiol. Aging , vol.30 , pp. 622-629
    • Cocco, T.1    Pacelli, C.2    Sgobbo, P.3    Villani, G.4
  • 9
    • 0028949133 scopus 로고
    • Adenylyl cyclases and the interaction between calcium and cAMP signaling
    • D.M. Cooper, N. Mons, and J.W. Karpen Adenylyl cyclases and the interaction between calcium and cAMP signaling Nature 374 1995 421 424
    • (1995) Nature , vol.374 , pp. 421-424
    • Cooper, D.M.1    Mons, N.2    Karpen, J.W.3
  • 10
    • 78651001645 scopus 로고
    • A microspectrophotometric method for the determination of cytochrome oxidase
    • S.J. Cooperstein, and A. Lararow A microspectrophotometric method for the determination of cytochrome oxidase J. Biol. Chem. 189 1951 665 670
    • (1951) J. Biol. Chem. , vol.189 , pp. 665-670
    • Cooperstein, S.J.1    Lararow, A.2
  • 11
    • 39849104755 scopus 로고    scopus 로고
    • CAMP-dependent protein kinase regulates the mitochondrial import of the nuclear encoded NDUFS4 subunit of complex i
    • D. De Rasmo, D. Panelli, A.M. Sardanelli, and S. Papa cAMP-dependent protein kinase regulates the mitochondrial import of the nuclear encoded NDUFS4 subunit of complex I Cell. Signal. 20 2008 989 997
    • (2008) Cell. Signal. , vol.20 , pp. 989-997
    • De Rasmo, D.1    Panelli, D.2    Sardanelli, A.M.3    Papa, S.4
  • 12
    • 68749094302 scopus 로고    scopus 로고
    • CAMP response element-binding protein (CREB) is imported into mitochondria and promotes protein synthesis
    • D. De Rasmo, A. Signorile, E. Roca, and S. Papa cAMP response element-binding protein (CREB) is imported into mitochondria and promotes protein synthesis FEBS J. 276 2009 4325 4333
    • (2009) FEBS J. , vol.276 , pp. 4325-4333
    • De Rasmo, D.1    Signorile, A.2    Roca, E.3    Papa, S.4
  • 13
    • 77953551209 scopus 로고    scopus 로고
    • 2+ response element-binding protein plays a central role in the biogenesis of respiratory chain proteins in mammalian cells
    • 2+ response element-binding protein plays a central role in the biogenesis of respiratory chain proteins in mammalian cells IUBMB Life 62 2010 447 452
    • (2010) IUBMB Life , vol.62 , pp. 447-452
    • De Rasmo, D.1    Signorile, A.2    Papa, F.3    Roca, E.4    Papa, S.5
  • 16
    • 34250164233 scopus 로고    scopus 로고
    • Analysis of the assembly profiles for mitochondrial - And nuclear-DNA-encoded subunits into complex i
    • M. Lazarou, M. McKenzie, A. Ohtake, D.R. Thorburn, and M.T. Ryan Analysis of the assembly profiles for mitochondrial - and nuclear-DNA-encoded subunits into complex I Mol. Cell. Biol. 27 2007 4228 4237
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4228-4237
    • Lazarou, M.1    McKenzie, M.2    Ohtake, A.3    Thorburn, D.R.4    Ryan, M.T.5
  • 17
    • 0033858360 scopus 로고    scopus 로고
    • The contribution of mitochondrial respiratory complexes to the production of reactive oxygen species
    • H.R. McLennan, and M. Degli Esposti The contribution of mitochondrial respiratory complexes to the production of reactive oxygen species J. Bioenerg. Biomembr. 32 2000 153 162
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 153-162
    • McLennan, H.R.1    Degli Esposti, M.2
  • 18
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • M.P. Murphy How mitochondria produce reactive oxygen species Biochem. J. 417 2009 1 13
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 19
    • 84900972913 scopus 로고    scopus 로고
    • Structure, redox-coupled protomotive activity, and pathological disorders of respiratory chain complexes
    • S. Papa, V. Petruzzella, and S. Scacco Structure, redox-coupled protomotive activity, and pathological disorders of respiratory chain complexes A. Lajtha, G. Dienel, G. Gibson, Handbook of Neurochemistry and Molecular Neurobiology 2007 Springer Verlag Berlin Heidelberg 93 118
    • (2007) Handbook of Neurochemistry and Molecular Neurobiology , pp. 93-118
    • Papa, S.1    Petruzzella, V.2    Scacco, S.3
  • 24
    • 25444515720 scopus 로고    scopus 로고
    • Antioxidants modulate mitochondrial PKA and increase CREB binding to D-loop DNA of the mitochondrial genome in neurons
    • H. Ryu, J. Lee, S. Impey, R.R. Ratan, and R.J. Ferrante Antioxidants modulate mitochondrial PKA and increase CREB binding to D-loop DNA of the mitochondrial genome in neurons Proc. Natl Acad. Sci. 102 2005 13915 13920
    • (2005) Proc. Natl Acad. Sci. , vol.102 , pp. 13915-13920
    • Ryu, H.1    Lee, J.2    Impey, S.3    Ratan, R.R.4    Ferrante, R.J.5
  • 26
    • 0034625326 scopus 로고    scopus 로고
    • CAMP-dependent phosphorylation of the nuclear encoded 18-kDa (IP) subunit of respiratory complex i and activation of the complex in serum-starved mouse fibroblast cultures
    • S. Scacco, R. Vergari, R.C. Scarpulla, Z. Technikova-Dobrova, A.M. Sardanelli, R. Lambo, V. Lorusso, and S. Papa cAMP-dependent phosphorylation of the nuclear encoded 18-kDa (IP) subunit of respiratory complex I and activation of the complex in serum-starved mouse fibroblast cultures J. Biol. Chem. 275 2000 17578 17582
    • (2000) J. Biol. Chem. , vol.275 , pp. 17578-17582
    • Scacco, S.1    Vergari, R.2    Scarpulla, R.C.3    Technikova-Dobrova, Z.4    Sardanelli, A.M.5    Lambo, R.6    Lorusso, V.7    Papa, S.8
  • 27
    • 0242414752 scopus 로고    scopus 로고
    • Pathological mutations of the human NDUFS4 gene of the 18-kDa (AQDQ) subunit of complex i affect the expression of the protein and the assembly and function of the complex
    • S. Scacco, V. Petruzzella, S. Budde, R. Vergari, R. Tamborra, D. Panelli, L.P. van den Heuvel, J.A. Smeitink, and S. Papa Pathological mutations of the human NDUFS4 gene of the 18-kDa (AQDQ) subunit of complex I affect the expression of the protein and the assembly and function of the complex J. Biol. Chem. 278 2003 44161 44167
    • (2003) J. Biol. Chem. , vol.278 , pp. 44161-44167
    • Scacco, S.1    Petruzzella, V.2    Budde, S.3    Vergari, R.4    Tamborra, R.5    Panelli, D.6    Van Den Heuvel, L.P.7    Smeitink, J.A.8    Papa, S.9
  • 28
    • 9644268262 scopus 로고    scopus 로고
    • Molecular genetics of complex I-deficient Chinese hamster cell lines
    • I.E. Scheffler, N. Yadava, and P. Potluri Molecular genetics of complex I-deficient Chinese hamster cell lines Biochim. Biophys. Acta 1659 2004 160 171
    • (2004) Biochim. Biophys. Acta , vol.1659 , pp. 160-171
    • Scheffler, I.E.1    Yadava, N.2    Potluri, P.3
  • 30
    • 0037070143 scopus 로고    scopus 로고
    • Serine (threonine) phosphatase(s) acting on cAMP-dependent phosphoproteins in mammalian mitochondria
    • A. Signorile, A.M. Sardanelli, R. Nuzzi, and S. Papa Serine (threonine) phosphatase(s) acting on cAMP-dependent phosphoproteins in mammalian mitochondria FEBS Lett. 512 2002 91 94
    • (2002) FEBS Lett. , vol.512 , pp. 91-94
    • Signorile, A.1    Sardanelli, A.M.2    Nuzzi, R.3    Papa, S.4
  • 31
    • 0031931938 scopus 로고    scopus 로고
    • New developments in cardiovascular adrenergic receptor pharmacology: Molecular mechanisms and clinical relevance
    • R.M. Smiley, M.M. Kwatra, and D.A. Schwinn New developments in cardiovascular adrenergic receptor pharmacology: molecular mechanisms and clinical relevance J. Cardiothorac. Vasc. Anesth. 12 1998 80 95
    • (1998) J. Cardiothorac. Vasc. Anesth. , vol.12 , pp. 80-95
    • Smiley, R.M.1    Kwatra, M.M.2    Schwinn, D.A.3
  • 33
    • 0035923443 scopus 로고    scopus 로고
    • Cyclic adenosine monophosphate-dependent phosphorylation of mammalian mitochondrial proteins: Enzyme and substrate characterization and functional role
    • Z. Technikova-Dobrova, A.M. Sardanelli, F. Speranza, S. Scacco, A. Signorile, V. Lorusso, and S. Papa Cyclic adenosine monophosphate-dependent phosphorylation of mammalian mitochondrial proteins: enzyme and substrate characterization and functional role Biochemistry 140 2001 13941 13947
    • (2001) Biochemistry , vol.140 , pp. 13941-13947
    • Technikova-Dobrova, Z.1    Sardanelli, A.M.2    Speranza, F.3    Scacco, S.4    Signorile, A.5    Lorusso, V.6    Papa, S.7
  • 34
    • 10044253425 scopus 로고    scopus 로고
    • AKAP signalling complexes: Focal points in space and time
    • W. Wong, and J.D. Scott AKAP signalling complexes: focal points in space and time Nat. Rev. Mol. Cell Biol. 5 2004 959 970
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 959-970
    • Wong, W.1    Scott, J.D.2
  • 35
    • 0037418550 scopus 로고    scopus 로고
    • The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: The secret unlocked
    • T. Yagi, and A. Matsuno-Yagi The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: the secret unlocked Biochemistry 42 2003 2266 2274
    • (2003) Biochemistry , vol.42 , pp. 2266-2274
    • Yagi, T.1    Matsuno-Yagi, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.