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Volumn 129, Issue 5, 2008, Pages 282-290

Changes in dihydrolipoamide dehydrogenase expression and activity during postnatal development and aging in the rat brain

Author keywords

Aging; Brain; Dihydrolipoamide dehydrogenase; Mitochondria; Oxidative stress; Postnatal development; Reactive oxygen species

Indexed keywords

DIHYDROLIPOAMIDE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; REACTIVE OXYGEN METABOLITE;

EID: 41249087100     PISSN: 00476374     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mad.2008.01.006     Document Type: Article
Times cited : (36)

References (80)
  • 1
    • 0028793538 scopus 로고
    • Postnatal development of the complexes of the electron transport chain in synaptic mitochondria from rat brain
    • Almeida A., Brooks K.J., Sammut I., Keelan J., Davey G.P., Clark J.B., and Bates T.E. Postnatal development of the complexes of the electron transport chain in synaptic mitochondria from rat brain. Dev. Neurosci. 17 (1995) 212-218
    • (1995) Dev. Neurosci. , vol.17 , pp. 212-218
    • Almeida, A.1    Brooks, K.J.2    Sammut, I.3    Keelan, J.4    Davey, G.P.5    Clark, J.B.6    Bates, T.E.7
  • 2
    • 0037465428 scopus 로고    scopus 로고
    • Catalysis of diaphorase reactions by Mycobacterium tuberculosis lipoamide dehydrogenase occurs at the EH4 level
    • Argyrou A., Sun G., Palfey B.A., and Blanchard J.S. Catalysis of diaphorase reactions by Mycobacterium tuberculosis lipoamide dehydrogenase occurs at the EH4 level. Biochemistry 42 (2003) 2218-2228
    • (2003) Biochemistry , vol.42 , pp. 2218-2228
    • Argyrou, A.1    Sun, G.2    Palfey, B.A.3    Blanchard, J.S.4
  • 4
    • 0026083374 scopus 로고
    • Mechanisms of generation of oxygen radicals and reductive mobilization of ferritin iron by lipoamide dehydrogenase
    • Bando Y., and Aki K. Mechanisms of generation of oxygen radicals and reductive mobilization of ferritin iron by lipoamide dehydrogenase. J. Biochem. (Tokyo) 109 (1991) 450-454
    • (1991) J. Biochem. (Tokyo) , vol.109 , pp. 450-454
    • Bando, Y.1    Aki, K.2
  • 5
    • 0028619016 scopus 로고
    • Postnatal development of the complexes of the electron transport chain in isolated rat brain mitochondria
    • Bates T.E., Almeida A., Heales S.J., and Clark J.B. Postnatal development of the complexes of the electron transport chain in isolated rat brain mitochondria. Dev. Neurosci. 16 (1994) 321-327
    • (1994) Dev. Neurosci. , vol.16 , pp. 321-327
    • Bates, T.E.1    Almeida, A.2    Heales, S.J.3    Clark, J.B.4
  • 6
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett B.S., and Stadtman E.R. Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272 (1997) 20313-20316
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 7
    • 20444475852 scopus 로고    scopus 로고
    • Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations
    • Brautigam C.A., Chuang J.L., Tomchick D.R., Machius M., and Chuang D.T. Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. J. Mol. Biol. 350 (2005) 543-552
    • (2005) J. Mol. Biol. , vol.350 , pp. 543-552
    • Brautigam, C.A.1    Chuang, J.L.2    Tomchick, D.R.3    Machius, M.4    Chuang, D.T.5
  • 9
    • 33947603916 scopus 로고    scopus 로고
    • Testing for linkage and association across the dihydrolipoyl dehydrogenase gene region with Alzheimer's disease in three sample populations
    • Brown A.M., Gordon D., Lee H., Vrieze F.W., Cellini E., Bagnoli S., Nacmias B., Sorbi S., Hardy J., and Blass J.P. Testing for linkage and association across the dihydrolipoyl dehydrogenase gene region with Alzheimer's disease in three sample populations. Neurochem. Res. 32 (2007) 857-869
    • (2007) Neurochem. Res. , vol.32 , pp. 857-869
    • Brown, A.M.1    Gordon, D.2    Lee, H.3    Vrieze, F.W.4    Cellini, E.5    Bagnoli, S.6    Nacmias, B.7    Sorbi, S.8    Hardy, J.9    Blass, J.P.10
  • 10
    • 0026809786 scopus 로고
    • Changes of malic enzyme activity in the developing rat brain are due to both the increase of mitochondrial protein content and the increase of specific activity
    • Bukato G., Kochan Z., and Swierczynski J. Changes of malic enzyme activity in the developing rat brain are due to both the increase of mitochondrial protein content and the increase of specific activity. Int. J. Biochem. 24 (1992) 267-273
    • (1992) Int. J. Biochem. , vol.24 , pp. 267-273
    • Bukato, G.1    Kochan, Z.2    Swierczynski, J.3
  • 11
    • 33644869456 scopus 로고    scopus 로고
    • How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex
    • Ciszak E.M., Makal A., Hong Y.S., Vettaikkorumakankauv A.K., Korotchkina L.G., and Patel M.S. How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex. J. Biol. Chem. 281 (2006) 648-655
    • (2006) J. Biol. Chem. , vol.281 , pp. 648-655
    • Ciszak, E.M.1    Makal, A.2    Hong, Y.S.3    Vettaikkorumakankauv, A.K.4    Korotchkina, L.G.5    Patel, M.S.6
  • 13
    • 4143132973 scopus 로고
    • Metabolism of rat brain mitochondria during postnatal development
    • Dahl D.R., and Samson Jr. F.E. Metabolism of rat brain mitochondria during postnatal development. Am. J. Physiol. 196 (1959) 470-472
    • (1959) Am. J. Physiol. , vol.196 , pp. 470-472
    • Dahl, D.R.1    Samson Jr., F.E.2
  • 14
    • 0035890871 scopus 로고    scopus 로고
    • Selectivity of protein oxidative damage during aging in Drosophila melanogaster
    • Das N., Levine R.L., Orr W.C., and Sohal R.S. Selectivity of protein oxidative damage during aging in Drosophila melanogaster. Biochem. J. 360 (2001) 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
  • 15
    • 0030249761 scopus 로고    scopus 로고
    • Effect of age and caloric intake on protein oxidation in different brain regions and on behavioral functions of the mouse
    • Dubey A., Forster M.J., Lal H., and Sohal R.S. Effect of age and caloric intake on protein oxidation in different brain regions and on behavioral functions of the mouse. Arch. Biochem. Biophys. 333 (1996) 189-197
    • (1996) Arch. Biochem. Biophys. , vol.333 , pp. 189-197
    • Dubey, A.1    Forster, M.J.2    Lal, H.3    Sohal, R.S.4
  • 16
    • 0034113956 scopus 로고    scopus 로고
    • Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system 2. Crystal structures of H- and L-proteins
    • Faure M., Bourguignon J., Neuburger M., MacHerel D., Sieker L., Ober R., Kahn R., Cohen-Addad C., and Douce R. Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system 2. Crystal structures of H- and L-proteins. Eur. J. Biochem. 267 (2000) 2890-2898
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2890-2898
    • Faure, M.1    Bourguignon, J.2    Neuburger, M.3    MacHerel, D.4    Sieker, L.5    Ober, R.6    Kahn, R.7    Cohen-Addad, C.8    Douce, R.9
  • 17
    • 0029978498 scopus 로고    scopus 로고
    • Age-related losses of cognitive function and motor skills in mice are associated with oxidative protein damage in the brain
    • Forster M.J., Dubey A., Dawson K.M., Stutts W.A., Lal H., and Sohal R.S. Age-related losses of cognitive function and motor skills in mice are associated with oxidative protein damage in the brain. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 4765-4769
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 4765-4769
    • Forster, M.J.1    Dubey, A.2    Dawson, K.M.3    Stutts, W.A.4    Lal, H.5    Sohal, R.S.6
  • 18
    • 2942558370 scopus 로고    scopus 로고
    • New insights into protein S-nitrosylation. Mitochondria as a model system
    • Foster M.W., and Stamler J.S. New insights into protein S-nitrosylation. Mitochondria as a model system. J. Biol. Chem. 279 (2004) 25891-25897
    • (2004) J. Biol. Chem. , vol.279 , pp. 25891-25897
    • Foster, M.W.1    Stamler, J.S.2
  • 19
    • 0037155880 scopus 로고    scopus 로고
    • Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase
    • Gazaryan I.G., Krasnikov B.F., Ashby G.A., Thorneley R.N., Kristal B.S., and Brown A.M. Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase. J. Biol. Chem. 277 (2002) 10064-10072
    • (2002) J. Biol. Chem. , vol.277 , pp. 10064-10072
    • Gazaryan, I.G.1    Krasnikov, B.F.2    Ashby, G.A.3    Thorneley, R.N.4    Kristal, B.S.5    Brown, A.M.6
  • 21
    • 0028955221 scopus 로고
    • Inactivation of heart dihydrolipoamide dehydrogenase by copper Fenton systems. Effect of thiol compounds and metal chelators
    • Gutierrez-Correa J., and Stoppani A.O. Inactivation of heart dihydrolipoamide dehydrogenase by copper Fenton systems. Effect of thiol compounds and metal chelators. Free Radic. Res. 22 (1995) 239-250
    • (1995) Free Radic. Res. , vol.22 , pp. 239-250
    • Gutierrez-Correa, J.1    Stoppani, A.O.2
  • 22
    • 0032994403 scopus 로고    scopus 로고
    • Inactivation of myocardial dihydrolipoamide dehydrogenase by myeloperoxidase systems: effect of halides, nitrite and thiol compounds
    • Gutierrez-Correa J., and Stoppani A.O. Inactivation of myocardial dihydrolipoamide dehydrogenase by myeloperoxidase systems: effect of halides, nitrite and thiol compounds. Free Radic. Res. 30 (1999) 105-117
    • (1999) Free Radic. Res. , vol.30 , pp. 105-117
    • Gutierrez-Correa, J.1    Stoppani, A.O.2
  • 23
    • 0027737467 scopus 로고
    • Functional maturation of creatine kinase in rat brain
    • Holtzman D., Tsuji M., Wallimann T., and Hemmer W. Functional maturation of creatine kinase in rat brain. Dev. Neurosci. 15 (1993) 261-270
    • (1993) Dev. Neurosci. , vol.15 , pp. 261-270
    • Holtzman, D.1    Tsuji, M.2    Wallimann, T.3    Hemmer, W.4
  • 25
    • 2942557132 scopus 로고    scopus 로고
    • Dihydrolipoamide dehydrogenase from porcine heart catalyzes NADH-dependent scavenging of nitric oxide
    • Igamberdiev A.U., Bykova N.V., Ens W., and Hill R.D. Dihydrolipoamide dehydrogenase from porcine heart catalyzes NADH-dependent scavenging of nitric oxide. FEBS Lett. 568 (2004) 146-150
    • (2004) FEBS Lett. , vol.568 , pp. 146-150
    • Igamberdiev, A.U.1    Bykova, N.V.2    Ens, W.3    Hill, R.D.4
  • 26
    • 0037082118 scopus 로고    scopus 로고
    • Specificity of age-related carbonylation of plasma proteins in the mouse and rat
    • Jana C.K., Das N., and Sohal R.S. Specificity of age-related carbonylation of plasma proteins in the mouse and rat. Arch. Biochem. Biophys. 397 (2002) 433-439
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 433-439
    • Jana, C.K.1    Das, N.2    Sohal, R.S.3
  • 27
    • 0026723971 scopus 로고
    • A structural model for human dihydrolipoamide dehydrogenase
    • Jentoft J.E., Shoham M., Hurst D., and Patel M.S. A structural model for human dihydrolipoamide dehydrogenase. Proteins 14 (1992) 88-101
    • (1992) Proteins , vol.14 , pp. 88-101
    • Jentoft, J.E.1    Shoham, M.2    Hurst, D.3    Patel, M.S.4
  • 28
    • 0031445917 scopus 로고    scopus 로고
    • Targeted disruption of the murine dihydrolipoamide dehydrogenase gene (Dld) results in perigastrulation lethality
    • Johnson M.T., Yang H.S., Magnuson T., and Patel M.S. Targeted disruption of the murine dihydrolipoamide dehydrogenase gene (Dld) results in perigastrulation lethality. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 14512-14517
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 14512-14517
    • Johnson, M.T.1    Yang, H.S.2    Magnuson, T.3    Patel, M.S.4
  • 29
    • 0034894613 scopus 로고    scopus 로고
    • Postnatal development of energy metabolism in the rat brain
    • Kalous M., Rauchova H., and Drahota Z. Postnatal development of energy metabolism in the rat brain. Physiol. Res. 50 (2001) 315-319
    • (2001) Physiol. Res. , vol.50 , pp. 315-319
    • Kalous, M.1    Rauchova, H.2    Drahota, Z.3
  • 32
    • 0017408806 scopus 로고
    • Development of mitochondrial energy metabolism in rat brain
    • Land J.M., Booth R.F., Berger R., and Clark J.B. Development of mitochondrial energy metabolism in rat brain. Biochem. J. 164 (1977) 339-348
    • (1977) Biochem. J. , vol.164 , pp. 339-348
    • Land, J.M.1    Booth, R.F.2    Berger, R.3    Clark, J.B.4
  • 33
    • 0021249724 scopus 로고
    • Regional development of glutamate dehydrogenase in the rat brain
    • Leong S.F., and Clark J.B. Regional development of glutamate dehydrogenase in the rat brain. J. Neurochem. 43 (1984) 106-111
    • (1984) J. Neurochem. , vol.43 , pp. 106-111
    • Leong, S.F.1    Clark, J.B.2
  • 34
    • 0021327317 scopus 로고
    • Regional enzyme development in rat brain. Enzymes of energy metabolism
    • Leong S.F., and Clark J.B. Regional enzyme development in rat brain. Enzymes of energy metabolism. Biochem. J. 218 (1984) 139-145
    • (1984) Biochem. J. , vol.218 , pp. 139-145
    • Leong, S.F.1    Clark, J.B.2
  • 35
    • 0034919355 scopus 로고    scopus 로고
    • Developmental expression of the mitochondrial pyruvate dehydrogenase complex in pea (Pisum sativum) seedlings
    • Luethy M.H., Gemel J., Johnston M.L., Mooney B.P., Miernyk J.A., and Randall D.D. Developmental expression of the mitochondrial pyruvate dehydrogenase complex in pea (Pisum sativum) seedlings. Physiol. Plant 112 (2001) 559-566
    • (2001) Physiol. Plant , vol.112 , pp. 559-566
    • Luethy, M.H.1    Gemel, J.2    Johnston, M.L.3    Mooney, B.P.4    Miernyk, J.A.5    Randall, D.D.6
  • 36
    • 0022514863 scopus 로고
    • Comparative development of the pyruvate dehydrogenase complex and citrate synthase in rat brain mitochondria
    • Malloch G.D., Munday L.A., Olson M.S., and Clark J.B. Comparative development of the pyruvate dehydrogenase complex and citrate synthase in rat brain mitochondria. Biochem. J. 238 (1986) 729-736
    • (1986) Biochem. J. , vol.238 , pp. 729-736
    • Malloch, G.D.1    Munday, L.A.2    Olson, M.S.3    Clark, J.B.4
  • 37
    • 0000537410 scopus 로고
    • Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase)
    • Massey V., Gibson Q.H., and Veeger C. Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase). Biochem. J. 77 (1960) 341-351
    • (1960) Biochem. J. , vol.77 , pp. 341-351
    • Massey, V.1    Gibson, Q.H.2    Veeger, C.3
  • 38
    • 0019995525 scopus 로고
    • Superoxide dismutase, glutathione peroxidase and catalase in developing rat brain
    • Mavelli I., Rigo A., Federico R., Ciriolo M.R., and Rotilio G. Superoxide dismutase, glutathione peroxidase and catalase in developing rat brain. Biochem. J. 204 (1982) 535-540
    • (1982) Biochem. J. , vol.204 , pp. 535-540
    • Mavelli, I.1    Rigo, A.2    Federico, R.3    Ciriolo, M.R.4    Rotilio, G.5
  • 39
    • 0142213541 scopus 로고    scopus 로고
    • Age-related increase in 4-hydroxynonenal adduction to rat heart alpha-ketoglutarate dehydrogenase does not cause loss of its catalytic activity
    • Moreau R., Heath S.H., Doneanu C.E., Lindsay J.G., and Hagen T.M. Age-related increase in 4-hydroxynonenal adduction to rat heart alpha-ketoglutarate dehydrogenase does not cause loss of its catalytic activity. Antioxid. Redox Signal. 5 (2003) 517-527
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 517-527
    • Moreau, R.1    Heath, S.H.2    Doneanu, C.E.3    Lindsay, J.G.4    Hagen, T.M.5
  • 40
    • 6344289360 scopus 로고    scopus 로고
    • Rat brain and liver mitochondria develop oxidative stress and lose enzymatic activities on aging
    • Navarro A., and Boveris A. Rat brain and liver mitochondria develop oxidative stress and lose enzymatic activities on aging. Am. J. Physiol. Regul. Integr. Comp. Physiol. 287 (2004) R1244-R1249
    • (2004) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.287
    • Navarro, A.1    Boveris, A.2
  • 41
    • 34249829274 scopus 로고    scopus 로고
    • Brain mitochondrial dysfunction in aging: conditions that improve survival, neurological performance and mitochondrial function
    • Navarro A., and Boveris A. Brain mitochondrial dysfunction in aging: conditions that improve survival, neurological performance and mitochondrial function. Front. Biosci. 12 (2007) 1154-1163
    • (2007) Front. Biosci. , vol.12 , pp. 1154-1163
    • Navarro, A.1    Boveris, A.2
  • 42
    • 33847059997 scopus 로고    scopus 로고
    • The mitochondrial energy transduction system and the aging process
    • Navarro A., and Boveris A. The mitochondrial energy transduction system and the aging process. Am. J. Physiol. Cell Physiol. 292 (2007) C670-C686
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Navarro, A.1    Boveris, A.2
  • 43
    • 1342309919 scopus 로고    scopus 로고
    • Beneficial effects of moderate exercise on mice aging: survival, behavior, oxidative stress, and mitochondrial electron transfer
    • Navarro A., Gomez C., Lopez-Cepero J.M., and Boveris A. Beneficial effects of moderate exercise on mice aging: survival, behavior, oxidative stress, and mitochondrial electron transfer. Am. J. Physiol. Regul. Integr. Comp. Physiol. 286 (2004) R505-R511
    • (2004) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.286
    • Navarro, A.1    Gomez, C.2    Lopez-Cepero, J.M.3    Boveris, A.4
  • 44
    • 0007390697 scopus 로고    scopus 로고
    • Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. 1. Biochemical studies
    • Neuburger M., Polidori A.M., Pietre E., Faure M., Jourdain A., Bourguignon J., Pucci B., and Douce R. Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. 1. Biochemical studies. Eur. J. Biochem. 267 (2000) 2882-2889
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2882-2889
    • Neuburger, M.1    Polidori, A.M.2    Pietre, E.3    Faure, M.4    Jourdain, A.5    Bourguignon, J.6    Pucci, B.7    Douce, R.8
  • 45
    • 0032991061 scopus 로고    scopus 로고
    • Ubiquinone is reduced by lipoamide dehydrogenase and this reaction is potently stimulated by zinc
    • Olsson J.M., Xia L., Eriksson L.C., and Bjornstedt M. Ubiquinone is reduced by lipoamide dehydrogenase and this reaction is potently stimulated by zinc. FEBS Lett. 448 (1999) 190-192
    • (1999) FEBS Lett. , vol.448 , pp. 190-192
    • Olsson, J.M.1    Xia, L.2    Eriksson, L.C.3    Bjornstedt, M.4
  • 46
    • 0032239976 scopus 로고    scopus 로고
    • Lipoic acid as an antioxidant: the role of dihydrolipoamide dehydrogenase
    • Armstrong D. (Ed), Humana Press, Totowa, NJ
    • Patel M.S., and Hong Y.S. Lipoic acid as an antioxidant: the role of dihydrolipoamide dehydrogenase. In: Armstrong D. (Ed). Free Radical and Antioxidant Protocols (1998), Humana Press, Totowa, NJ 337-346
    • (1998) Free Radical and Antioxidant Protocols , pp. 337-346
    • Patel, M.S.1    Hong, Y.S.2
  • 47
    • 0025221771 scopus 로고
    • Molecular biology and biochemistry of pyruvate dehydrogenase complexes
    • Patel M.S., and Roche T.E. Molecular biology and biochemistry of pyruvate dehydrogenase complexes. FASEB J. 4 (1990) 3224-3233
    • (1990) FASEB J. , vol.4 , pp. 3224-3233
    • Patel, M.S.1    Roche, T.E.2
  • 49
    • 33646708957 scopus 로고    scopus 로고
    • Proteomics analysis provides insight into caloric restriction mediated oxidation and expression of brain proteins associated with age-related impaired cellular processes: Mitochondrial dysfunction, glutamate dysregulation and impaired protein synthesis
    • Poon H.F., Shepherd H.M., Reed T.T., Calabrese V., Stella A.M., Pennisi G., Cai J., Pierce W.M., Klein J.B., and Butterfield D.A. Proteomics analysis provides insight into caloric restriction mediated oxidation and expression of brain proteins associated with age-related impaired cellular processes: Mitochondrial dysfunction, glutamate dysregulation and impaired protein synthesis. Neurobiol. Aging 27 (2006) 1020-1034
    • (2006) Neurobiol. Aging , vol.27 , pp. 1020-1034
    • Poon, H.F.1    Shepherd, H.M.2    Reed, T.T.3    Calabrese, V.4    Stella, A.M.5    Pennisi, G.6    Cai, J.7    Pierce, W.M.8    Klein, J.B.9    Butterfield, D.A.10
  • 50
    • 38149109254 scopus 로고    scopus 로고
    • Mass spectrometry-based survey of age-associated protein carbonylation in rat brain mitochondria
    • Prokai L., Yan L.J., Vera-Serrano J.L., Stevens S.M., and Forster M.J. Mass spectrometry-based survey of age-associated protein carbonylation in rat brain mitochondria. J. Mass Spectrom. 42 (2007) 1583-1589
    • (2007) J. Mass Spectrom. , vol.42 , pp. 1583-1589
    • Prokai, L.1    Yan, L.J.2    Vera-Serrano, J.L.3    Stevens, S.M.4    Forster, M.J.5
  • 51
    • 33845197506 scopus 로고    scopus 로고
    • Effects of age and caloric intake on glutathione redox state in different brain regions of C57BL/6 and DBA/2 mice
    • Rebrin I., Forster M.J., and Sohal R.S. Effects of age and caloric intake on glutathione redox state in different brain regions of C57BL/6 and DBA/2 mice. Brain Res. 1127 (2007) 10-18
    • (2007) Brain Res. , vol.1127 , pp. 10-18
    • Rebrin, I.1    Forster, M.J.2    Sohal, R.S.3
  • 52
    • 12244293660 scopus 로고    scopus 로고
    • S-nitroso proteome of Mycobacterium tuberculosis: enzymes of intermediary metabolism and antioxidant defense
    • Rhee K.Y., Erdjument-Bromage H., Tempst P., and Nathan C.F. S-nitroso proteome of Mycobacterium tuberculosis: enzymes of intermediary metabolism and antioxidant defense. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 467-472
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 467-472
    • Rhee, K.Y.1    Erdjument-Bromage, H.2    Tempst, P.3    Nathan, C.F.4
  • 53
    • 0028786786 scopus 로고
    • Developmental changes of the adenine nucleotide translocation in rat brain
    • Schonfeld P., and Bohnensack R. Developmental changes of the adenine nucleotide translocation in rat brain. Biochim. Biophys. Acta 1232 (1995) 75-80
    • (1995) Biochim. Biophys. Acta , vol.1232 , pp. 75-80
    • Schonfeld, P.1    Bohnensack, R.2
  • 54
    • 33646354917 scopus 로고    scopus 로고
    • Rotenone-like action of the branched-chain phytanic acid induces oxidative stress in mitochondria
    • Schonfeld P., and Reiser G. Rotenone-like action of the branched-chain phytanic acid induces oxidative stress in mitochondria. J. Biol. Chem. 281 (2006) 7136-7142
    • (2006) J. Biol. Chem. , vol.281 , pp. 7136-7142
    • Schonfeld, P.1    Reiser, G.2
  • 55
    • 33846191139 scopus 로고    scopus 로고
    • Ca(2+) storage capacity of rat brain mitochondria declines during the postnatal development without change in ROS production capacity
    • Schonfeld P., and Reiser G. Ca(2+) storage capacity of rat brain mitochondria declines during the postnatal development without change in ROS production capacity. Antioxid. Redox Signal. 9 (2007) 191-199
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 191-199
    • Schonfeld, P.1    Reiser, G.2
  • 56
    • 0015217036 scopus 로고
    • Microbial lipoamide dehydrogenase. Purification and some characteristics of the enzyme derived from selected microorganisms
    • Scouten W.H., and McManus I.R. Microbial lipoamide dehydrogenase. Purification and some characteristics of the enzyme derived from selected microorganisms. Biochim. Biophys. Acta 227 (1971) 248-263
    • (1971) Biochim. Biophys. Acta , vol.227 , pp. 248-263
    • Scouten, W.H.1    McManus, I.R.2
  • 60
    • 0019839652 scopus 로고
    • Isolation of a specific lipoamide dehydrogenase for a branched-chain keto acid dehydrogenase from Pseudomonas putida
    • Sokatch J.R., McCully V., Gebrosky J., and Sokatch D.J. Isolation of a specific lipoamide dehydrogenase for a branched-chain keto acid dehydrogenase from Pseudomonas putida. J. Bacteriol. 148 (1981) 639-646
    • (1981) J. Bacteriol. , vol.148 , pp. 639-646
    • Sokatch, J.R.1    McCully, V.2    Gebrosky, J.3    Sokatch, D.J.4
  • 61
    • 0025048534 scopus 로고
    • Catalysis of nitrofuran redox-cycling and superoxide anion production by heart lipoamide dehydrogenase
    • Sreider C.M., Grinblat L., and Stoppani A.O. Catalysis of nitrofuran redox-cycling and superoxide anion production by heart lipoamide dehydrogenase. Biochem. Pharmacol. 40 (1990) 1849-1857
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 1849-1857
    • Sreider, C.M.1    Grinblat, L.2    Stoppani, A.O.3
  • 63
    • 33845999916 scopus 로고    scopus 로고
    • Dihydrolipoyl dehydrogenase as a source of reactive oxygen species inhibited by caloric restriction and involved in Saccharomyces cerevisiae aging
    • Tahara E.B., Barros M.H., Oliveira G.A., Netto L.E., and Kowaltowski A.J. Dihydrolipoyl dehydrogenase as a source of reactive oxygen species inhibited by caloric restriction and involved in Saccharomyces cerevisiae aging. FASEB J. 21 (2007) 274-283
    • (2007) FASEB J. , vol.21 , pp. 274-283
    • Tahara, E.B.1    Barros, M.H.2    Oliveira, G.A.3    Netto, L.E.4    Kowaltowski, A.J.5
  • 64
    • 0017067595 scopus 로고
    • Differential reactivity of the two active site cysteine residues generated on reduction of pig heart lipoamide dehydrogenase
    • Thorpe C., and Williams Jr. C.H. Differential reactivity of the two active site cysteine residues generated on reduction of pig heart lipoamide dehydrogenase. J. Biol. Chem. 251 (1976) 3553-3557
    • (1976) J. Biol. Chem. , vol.251 , pp. 3553-3557
    • Thorpe, C.1    Williams Jr., C.H.2
  • 65
    • 34748907199 scopus 로고    scopus 로고
    • Carbonylation of mitochondrial proteins in Drosophila melanogaster during aging
    • Toroser D., Orr W.C., and Sohal R.S. Carbonylation of mitochondrial proteins in Drosophila melanogaster during aging. Biochem. Biophys. Res. Commun. 363 (2007) 418-424
    • (2007) Biochem. Biophys. Res. Commun. , vol.363 , pp. 418-424
    • Toroser, D.1    Orr, W.C.2    Sohal, R.S.3
  • 66
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 67
    • 0030969868 scopus 로고    scopus 로고
    • Superoxide production by the mitochondrial respiratory chain
    • Turrens J.F. Superoxide production by the mitochondrial respiratory chain. Biosci. Rep. 17 (1997) 3-8
    • (1997) Biosci. Rep. , vol.17 , pp. 3-8
    • Turrens, J.F.1
  • 68
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens J.F., Alexandre A., and Lehninger A.L. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch. Biochem. Biophys. 237 (1985) 408-414
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 69
    • 0030158597 scopus 로고    scopus 로고
    • Dihydrolipoamide dehydrogenase: structural and mechanistic aspects
    • Vettakkorumakankav N.N., and Patel M.S. Dihydrolipoamide dehydrogenase: structural and mechanistic aspects. Indian J. Biochem. Biophys. 33 (1996) 168-176
    • (1996) Indian J. Biochem. Biophys. , vol.33 , pp. 168-176
    • Vettakkorumakankav, N.N.1    Patel, M.S.2
  • 70
    • 0019500657 scopus 로고
    • NADH inhibition and NAD activation of Escherichia coli lipoamide dehydrogenase catalyzing the NADH-lipoamide reaction
    • Wilkinson K.D., and Williams Jr. C.H. NADH inhibition and NAD activation of Escherichia coli lipoamide dehydrogenase catalyzing the NADH-lipoamide reaction. J. Biol. Chem. 256 (1981) 2307-2314
    • (1981) J. Biol. Chem. , vol.256 , pp. 2307-2314
    • Wilkinson, K.D.1    Williams Jr., C.H.2
  • 71
    • 0000876731 scopus 로고
    • Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase-a family of flavoenzyme transhydrogenases
    • Muller F. (Ed), CRC Press, Boca Raton
    • Williams C.H.J. Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase-a family of flavoenzyme transhydrogenases. In: Muller F. (Ed). Chemistry and Biochemistry of Flavoenzymes, Vol. III (1992), CRC Press, Boca Raton 121-212
    • (1992) Chemistry and Biochemistry of Flavoenzymes, Vol. III , pp. 121-212
    • Williams, C.H.J.1
  • 72
    • 0035087829 scopus 로고    scopus 로고
    • Reduction of ubiquinone by lipoamide dehydrogenase. An antioxidant regenerating pathway
    • Xia L., Bjornstedt M., Nordman T., Eriksson L.C., and Olsson J.M. Reduction of ubiquinone by lipoamide dehydrogenase. An antioxidant regenerating pathway. Eur. J. Biochem. 268 (2001) 1486-1490
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1486-1490
    • Xia, L.1    Bjornstedt, M.2    Nordman, T.3    Eriksson, L.C.4    Olsson, J.M.5
  • 73
    • 0036790590 scopus 로고    scopus 로고
    • Mouse heat shock transcription factor 1 deficiency alters cardiac redox homeostasis and increases mitochondrial oxidative damage
    • Yan L.J., Christians E.S., Liu L., Xiao X., Sohal R.S., and Benjamin I.J. Mouse heat shock transcription factor 1 deficiency alters cardiac redox homeostasis and increases mitochondrial oxidative damage. EMBO J. 21 (2002) 5164-5172
    • (2002) EMBO J. , vol.21 , pp. 5164-5172
    • Yan, L.J.1    Christians, E.S.2    Liu, L.3    Xiao, X.4    Sohal, R.S.5    Benjamin, I.J.6
  • 74
    • 0030881686 scopus 로고    scopus 로고
    • Oxidative damage during aging targets mitochondrial aconitase
    • Yan L.J., Levine R.L., and Sohal R.S. Oxidative damage during aging targets mitochondrial aconitase. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 11168-11172
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 11168-11172
    • Yan, L.J.1    Levine, R.L.2    Sohal, R.S.3
  • 75
    • 0034233138 scopus 로고    scopus 로고
    • Effects of aging and hyperoxia on oxidative damage to cytochrome c in the housefly, Musca domestica
    • Yan L.J., Levine R.L., and Sohal R.S. Effects of aging and hyperoxia on oxidative damage to cytochrome c in the housefly, Musca domestica. Free Radic. Biol. Med. 29 (2000) 90-97
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 90-97
    • Yan, L.J.1    Levine, R.L.2    Sohal, R.S.3
  • 76
    • 0032190196 scopus 로고    scopus 로고
    • Identification of oxidized proteins based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunochemical detection, isoelectric focusing, and microsequencing
    • Yan L.J., Orr W.C., and Sohal R.S. Identification of oxidized proteins based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunochemical detection, isoelectric focusing, and microsequencing. Anal. Biochem. 263 (1998) 67-71
    • (1998) Anal. Biochem. , vol.263 , pp. 67-71
    • Yan, L.J.1    Orr, W.C.2    Sohal, R.S.3
  • 77
    • 14044270113 scopus 로고    scopus 로고
    • Mouse HSF1 disruption perturbs redox state and increases mitochondrial oxidative stress in kidney
    • Yan L.J., Rajasekaran N.S., Sathyanarayanan S., and Benjamin I.J. Mouse HSF1 disruption perturbs redox state and increases mitochondrial oxidative stress in kidney. Antioxid. Redox Signal. 7 (2005) 465-471
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 465-471
    • Yan, L.J.1    Rajasekaran, N.S.2    Sathyanarayanan, S.3    Benjamin, I.J.4
  • 78
    • 0032573066 scopus 로고    scopus 로고
    • Mitochondrial adenine nucleotide translocase is modified oxidatively during aging
    • Yan L.J., and Sohal R.S. Mitochondrial adenine nucleotide translocase is modified oxidatively during aging. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 12896-12901
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 12896-12901
    • Yan, L.J.1    Sohal, R.S.2
  • 79
    • 34247114586 scopus 로고    scopus 로고
    • Histochemical staining and quantification of dihydrolipoamide dehydrogenase diaphorase activity using blue native PAGE
    • Yan L.J., Yang S.H., Shu H., Prokai L., and Forster M.J. Histochemical staining and quantification of dihydrolipoamide dehydrogenase diaphorase activity using blue native PAGE. Electrophoresis 28 (2007) 1036-1045
    • (2007) Electrophoresis , vol.28 , pp. 1036-1045
    • Yan, L.J.1    Yang, S.H.2    Shu, H.3    Prokai, L.4    Forster, M.J.5
  • 80
    • 28244454785 scopus 로고    scopus 로고
    • Aconitase is the main functional target of aging in the citric acid cycle of kidney mitochondria from mice
    • Yarian C.S., Toroser D., and Sohal R.S. Aconitase is the main functional target of aging in the citric acid cycle of kidney mitochondria from mice. Mech. Ageing Dev. 127 (2006) 79-84
    • (2006) Mech. Ageing Dev. , vol.127 , pp. 79-84
    • Yarian, C.S.1    Toroser, D.2    Sohal, R.S.3


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