메뉴 건너뛰기




Volumn 271, Issue 22, 2004, Pages 4559-4564

Age-related impairment of mitochondrial matrix aconitase and ATP-stimulated protease in rat liver and heart

Author keywords

Aconitase; Aging; Lon protease; Mitochondrial matrix

Indexed keywords

ACONITATE HYDRATASE; ADENOSINE TRIPHOSPHATE; ENDOPEPTIDASE LA; MATRIX PROTEIN; MITOCHONDRIAL PROTEIN; PROTEINASE; UNCLASSIFIED DRUG;

EID: 9644301105     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04422.x     Document Type: Article
Times cited : (75)

References (19)
  • 3
    • 0038199601 scopus 로고    scopus 로고
    • The role of mitochondrial oxidative stress in aging
    • Sastre, J., Pallardo, F.V. & Vina, J. (2003) The role of mitochondrial oxidative stress in aging. Free Radic. Biol. Med. 35, 1-8.
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 1-8
    • Sastre, J.1    Pallardo, F.V.2    Vina, J.3
  • 4
    • 0032526782 scopus 로고    scopus 로고
    • Age-associated changes in mitochondrial mRNA expression and translation in the Wistar rat heart
    • Hudson, E.K., Tsuchiya, N. & Hansford, R.G. (1998) Age-associated changes in mitochondrial mRNA expression and translation in the Wistar rat heart. Mech. Ageing Dev. 103, 179-193.
    • (1998) Mech. Ageing Dev. , vol.103 , pp. 179-193
    • Hudson, E.K.1    Tsuchiya, N.2    Hansford, R.G.3
  • 5
    • 0033958726 scopus 로고    scopus 로고
    • Age-related changes in activities of mitochondrial electron transport complexes in various tissues of the mouse
    • Kwong, L.K. & Sohal, R.S. (2000) Age-related changes in activities of mitochondrial electron transport complexes in various tissues of the mouse. Arch. Biochem. Biophys. 373, 16-22.
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 16-22
    • Kwong, L.K.1    Sohal, R.S.2
  • 6
    • 0035890871 scopus 로고    scopus 로고
    • Selectivity of protein oxidative damage during aging in Drosophila melanogaster
    • Das, N., Levine, R.L., Orr, W.C. & Sohal, R.S. (2001) Selectivity of protein oxidative damage during aging in Drosophila melanogaster. Biochem. J. 360, 209-216.
    • (2001) Biochem. J. , vol.360 , pp. 209-216
    • Das, N.1    Levine, R.L.2    Orr, W.C.3    Sohal, R.S.4
  • 7
    • 0030881686 scopus 로고    scopus 로고
    • Oxidative damage during aging targets mitochondrial aconitase
    • Yan, L.J., Levine, R.L. & Sohal, R.S. (1997) Oxidative damage during aging targets mitochondrial aconitase. Proc. Natl Acad. Sci. USA 94, 11168-11172.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11168-11172
    • Yan, L.J.1    Levine, R.L.2    Sohal, R.S.3
  • 8
    • 0028075773 scopus 로고
    • Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs
    • Gardner, P.R., Nguyen, D.D. & White, C.W. (1994) Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs. Proc. Natl Acad. Sci. USA 91, 12248-12252.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12248-12252
    • Gardner, P.R.1    Nguyen, D.D.2    White, C.W.3
  • 9
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota, D.A. & Davies, K.J. (2002) Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat. Cell Biol. 4, 674-680.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.2
  • 10
    • 0027367968 scopus 로고
    • A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease
    • Wang, N., Gottesman, S., Willingham, M.C., Gottesman, M.M. & Maurizi, M.R. (1993) A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease. Proc. Natl Acad. Sci. USA 90, 11247-11251.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11247-11251
    • Wang, N.1    Gottesman, S.2    Willingham, M.C.3    Gottesman, M.M.4    Maurizi, M.R.5
  • 11
    • 0023679752 scopus 로고
    • Mitochondria contain a proteolytic system which can recognize and degrade oxidatively-denatured proteins
    • Marcillat, O., Zhang, Y., Lin, S.W. & Davies, K.J. (1988) Mitochondria contain a proteolytic system which can recognize and degrade oxidatively-denatured proteins. Biochem. J. 254, 677-683.
    • (1988) Biochem. J. , vol.254 , pp. 677-683
    • Marcillat, O.1    Zhang, Y.2    Lin, S.W.3    Davies, K.J.4
  • 12
    • 0037517056 scopus 로고    scopus 로고
    • Changes in rat liver mitochondria with aging. Lon protease-like reactivity and N(epsilon)-carboxymethyllysine accumulation in the matrix
    • Bakala, H., Delaval, E., Hamelin, M., Bismuth, J., Borot-Laloi, C., Corman, B. & Friguet, B. (2003) Changes in rat liver mitochondria with aging. Lon protease-like reactivity and N(epsilon)-carboxymethyllysine accumulation in the matrix. Eur. J. Biochem. 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
  • 13
    • 0020041449 scopus 로고
    • Early light microscopic changes in chronic progressive nephrosis in several strains of aging laboratory rats
    • Gray, J.E., van Zwieten, M.J. & Hollander, C.F. (1982) Early light microscopic changes in chronic progressive nephrosis in several strains of aging laboratory rats. J. Gerontol. 37, 142-150.
    • (1982) J. Gerontol. , vol.37 , pp. 142-150
    • Gray, J.E.1    Van Zwieten, M.J.2    Hollander, C.F.3
  • 14
    • 0019015732 scopus 로고
    • Postnatal development of rat liver mitochondria: State 3 respiration, adenine nucleotide translocase activity, and the net accumulation of adenine nucleotides
    • Aprille, J.R. & Asimakis, G.K. (1980) Postnatal development of rat liver mitochondria: state 3 respiration, adenine nucleotide translocase activity, and the net accumulation of adenine nucleotides. Arch. Biochem. Biophys. 201, 564-575.
    • (1980) Arch. Biochem. Biophys. , vol.201 , pp. 564-575
    • Aprille, J.R.1    Asimakis, G.K.2
  • 15
    • 0031930041 scopus 로고    scopus 로고
    • Cardiac reperfusion injury: Aging, lipid peroxidation, and mitochondrial dysfunction
    • Lucas, D.T. & Szweda, L.I. (1998) Cardiac reperfusion injury: aging, lipid peroxidation, and mitochondrial dysfunction. Proc. Natl Acad. Sci. USA 95, 510-514.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 510-514
    • Lucas, D.T.1    Szweda, L.I.2
  • 16
    • 0035968183 scopus 로고    scopus 로고
    • Modulation of mitochondrial function by hydrogen peroxide
    • Nulton-Persson, A.C. & Szweda, L.I. (2001) Modulation of mitochondrial function by hydrogen peroxide. J. Biol. Chem. 276, 23357-23361.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23357-23361
    • Nulton-Persson, A.C.1    Szweda, L.I.2
  • 17
    • 0346365099 scopus 로고    scopus 로고
    • Redox-dependent modulation of aconitase activity in intact mitochondria
    • Bulteau, A.L., Ikeda-Saito, M. & Szweda, L.I. (2003) Redox-dependent modulation of aconitase activity in intact mitochondria. Biochemistry 42, 14846-14855.
    • (2003) Biochemistry , vol.42 , pp. 14846-14855
    • Bulteau, A.L.1    Ikeda-Saito, M.2    Szweda, L.I.3
  • 18
    • 0033610079 scopus 로고    scopus 로고
    • Gene expression profile of aging and its retardation by caloric restriction
    • Lee, C.K., Klopp, R.G., Weindruch, R. & Prolla, T.A. (1999) Gene expression profile of aging and its retardation by caloric restriction. Science 285, 1390-1393.
    • (1999) Science , vol.285 , pp. 1390-1393
    • Lee, C.K.1    Klopp, R.G.2    Weindruch, R.3    Prolla, T.A.4
  • 19
    • 0037021453 scopus 로고    scopus 로고
    • Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress
    • Bota, D.A., Van Remmen, H. & Davies, K.J. (2002) Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress. FEBS Lett. 532, 103-106.
    • (2002) FEBS Lett. , vol.532 , pp. 103-106
    • Bota, D.A.1    Van Remmen, H.2    Davies, K.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.