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Volumn 35, Issue 10, 2003, Pages 1229-1239

Proteomic identification of age-dependent protein nitration in rat skeletal muscle

Author keywords

3 Nitrotyrosine; Aging; Free radicals; Proteomics; Skeletal muscle

Indexed keywords

ALPHA CRYSTALLIN; CREATINE KINASE; ENOLASE; FRUCTOSE BISPHOSPHATE ALDOLASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR; SUCCINATE DEHYDROGENASE; TRIOSEPHOSPHATE ISOMERASE; TROPONIN I;

EID: 0242321030     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(03)00500-8     Document Type: Article
Times cited : (111)

References (41)
  • 1
    • 77049308856 scopus 로고
    • Aging, a theory based on free radicals and radiation chemistry
    • Harman D. Aging, a theory based on free radicals and radiation chemistry. J. Gerontol. 2:1956;298-300.
    • (1956) J. Gerontol. , vol.2 , pp. 298-300
    • Harman, D.1
  • 2
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • Beal M.F. Oxidatively modified proteins in aging and disease. Free Radic. Biol. Med. 32:2002;797-803.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 797-803
    • Beal, M.F.1
  • 3
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman E.R. Protein oxidation and aging. Science. 257:1992;1220-1224.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 4
    • 0025301715 scopus 로고
    • Covalent modification reactions are marking steps in protein turnover
    • Stadtman E.R. Covalent modification reactions are marking steps in protein turnover. Biochemistry. 29:1990;6323-6331.
    • (1990) Biochemistry , vol.29 , pp. 6323-6331
    • Stadtman, E.R.1
  • 5
    • 0036628724 scopus 로고    scopus 로고
    • Role of oxidative stress and protein oxidation in the aging process
    • Sohal R.S. Role of oxidative stress and protein oxidation in the aging process. Free Radic. Biol. Med. 33:2002;37-44.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 37-44
    • Sohal, R.S.1
  • 7
    • 0034152767 scopus 로고    scopus 로고
    • Oxidative stress in bacteria and protein damage by reactive oxygen species
    • Cabiscol E., Tamarit J., Ros J. Oxidative stress in bacteria and protein damage by reactive oxygen species. Int. Microbiol. 3:2000;3-8.
    • (2000) Int. Microbiol. , vol.3 , pp. 3-8
    • Cabiscol, E.1    Tamarit, J.2    Ros, J.3
  • 10
    • 0034641689 scopus 로고    scopus 로고
    • Identification of oxidant-sensitive proteins: TNF-α induces protein glutathionation
    • Sullivan D.M., Wehr N.B., Fergusson M.M., Levine R.L., Finkel T. Identification of oxidant-sensitive proteins TNF-α induces protein glutathionation . Biochemistry. 39:2000;11121-11128.
    • (2000) Biochemistry , vol.39 , pp. 11121-11128
    • Sullivan, D.M.1    Wehr, N.B.2    Fergusson, M.M.3    Levine, R.L.4    Finkel, T.5
  • 13
    • 0034925593 scopus 로고    scopus 로고
    • Tyrosine nitration: Localization, quantification, consequences for protein function and signal transduction
    • Greenacre S.A., Ischiropoulos H. Tyrosine nitration localization, quantification, consequences for protein function and signal transduction . Free Radic. Res. 34:2001;541-581.
    • (2001) Free Radic. Res. , vol.34 , pp. 541-581
    • Greenacre, S.A.1    Ischiropoulos, H.2
  • 14
    • 0029682870 scopus 로고    scopus 로고
    • Oxidative damage and tyrosine nitration from peroxynitrite
    • Beckman J.S. Oxidative damage and tyrosine nitration from peroxynitrite. Chem. Res. Toxicol. 9:1996;836-844.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 836-844
    • Beckman, J.S.1
  • 15
    • 0037172177 scopus 로고    scopus 로고
    • The rate constant of the reaction of superoxide with nitrogen monoxide: Approaching the diffusion limit
    • Nauser T., Koppenol W.H. The rate constant of the reaction of superoxide with nitrogen monoxide approaching the diffusion limit . J. Phys. Chem. A. 106:2002;4084-4086.
    • (2002) J. Phys. Chem. A , vol.106 , pp. 4084-4086
    • Nauser, T.1    Koppenol, W.H.2
  • 16
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad and ugly
    • Beckman J.S., Koppenol W.H. Nitric oxide, superoxide, and peroxynitrite the good, the bad and ugly . Am. J. Physiol. 271:1996;C1424-C1427.
    • (1996) Am. J. Physiol. , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 17
    • 0033564289 scopus 로고    scopus 로고
    • Protein modification during biological aging: Selective tyrosine nitration of the SERCA2 isoform of the sarcoplasmic reticulum Ca-ATPase in skeletal muscle
    • Viner R.I., Ferrington D.A., Williams T.D., Bigelow D.J., Schöneich C. Protein modification during biological aging selective tyrosine nitration of the SERCA2 isoform of the sarcoplasmic reticulum Ca-ATPase in skeletal muscle . Biochem. J. 340:1999;657-669.
    • (1999) Biochem. J. , vol.340 , pp. 657-669
    • Viner, R.I.1    Ferrington, D.A.2    Williams, T.D.3    Bigelow, D.J.4    Schöneich, C.5
  • 19
    • 0027425836 scopus 로고
    • Reactive oxygen in skeletal muscle. III. Contractility of unfatigued muscle
    • Reid M.B., Khawli F.A., Moody M.R. Reactive oxygen in skeletal muscle. III. Contractility of unfatigued muscle. J. Appl. Physiol. 75:1993;1081-1087.
    • (1993) J. Appl. Physiol. , vol.75 , pp. 1081-1087
    • Reid, M.B.1    Khawli, F.A.2    Moody, M.R.3
  • 21
    • 0037205291 scopus 로고    scopus 로고
    • Antioxidant improves smooth muscle sarco/endoplasmic reticulum Ca(2+)-ATPase function and lowers tyrosine nitration in hypercholesteromia and improves nitric oxide-induced relaxation
    • Adachi T., Matsui R., Xu S., Kirber M., Lazar H.L., Sharov V.S., Schöneich C., Cohen R.A. Antioxidant improves smooth muscle sarco/endoplasmic reticulum Ca(2+)-ATPase function and lowers tyrosine nitration in hypercholesteromia and improves nitric oxide-induced relaxation. Circ. Res. 90:2002;1114-1121.
    • (2002) Circ. Res. , vol.90 , pp. 1114-1121
    • Adachi, T.1    Matsui, R.2    Xu, S.3    Kirber, M.4    Lazar, H.L.5    Sharov, V.S.6    Schöneich, C.7    Cohen, R.A.8
  • 22
    • 0034630358 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of membrane proteins using immobilized pH gradients
    • Molloy M.P. Two-dimensional electrophoresis of membrane proteins using immobilized pH gradients. Anal. Biochem. 280:2000;1-10.
    • (2000) Anal. Biochem. , vol.280 , pp. 1-10
    • Molloy, M.P.1
  • 23
    • 0021988172 scopus 로고
    • Simplified method for silver staining of proteins in polyacrylamide gels and the mechanisms of silver staining
    • Heukeshoven J., Dernick R. Simplified method for silver staining of proteins in polyacrylamide gels and the mechanisms of silver staining. Electrophoresis. 6:1985;103-112.
    • (1985) Electrophoresis , vol.6 , pp. 103-112
    • Heukeshoven, J.1    Dernick, R.2
  • 24
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins form silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins form silver-stained polyacrylamide gels. Anal. Chem. 68:1996;850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 25
    • 0034535649 scopus 로고    scopus 로고
    • Decription of the long-term lipogenic effects of dietary carbohydrates in male Fisher 344 rats
    • Lingelbach L.B., McDonald R.B. Decription of the long-term lipogenic effects of dietary carbohydrates in male Fisher 344 rats. J. Nutr. 130:2000;3077-3084.
    • (2000) J. Nutr. , vol.130 , pp. 3077-3084
    • Lingelbach, L.B.1    McDonald, R.B.2
  • 26
    • 0031057542 scopus 로고    scopus 로고
    • Effect of food restriction on life span and immune functions in long-lived Fisher-344 x Brown Norway F1 rats
    • Fernandes G., Venkatraman J.T., Turturro A., Attwood V.G., Hart R.W. Effect of food restriction on life span and immune functions in long-lived Fisher-344 x Brown Norway F1 rats. J. Clin. Immunol. 17:1997;85-95.
    • (1997) J. Clin. Immunol. , vol.17 , pp. 85-95
    • Fernandes, G.1    Venkatraman, J.T.2    Turturro, A.3    Attwood, V.G.4    Hart, R.W.5
  • 28
    • 0031888036 scopus 로고    scopus 로고
    • High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry
    • Ducret A., Van Oostveen I., Eng J.K., Yates J.R. III, Aebersold R. High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry. Protein Sci. 7:1998;706-719.
    • (1998) Protein Sci. , vol.7 , pp. 706-719
    • Ducret, A.1    Van Oostveen, I.2    Eng, J.K.3    Yates J.R. III4    Aebersold, R.5
  • 29
    • 0035241690 scopus 로고    scopus 로고
    • Mass spectrometry in proteomics
    • Aebersold R., Goodlett D.R. Mass spectrometry in proteomics. Chem. Rev. 101:2001;269-295.
    • (2001) Chem. Rev. , vol.101 , pp. 269-295
    • Aebersold, R.1    Goodlett, D.R.2
  • 30
    • 4244042780 scopus 로고    scopus 로고
    • Isoelectric focusing nonporous RP HPLC: A two-dimensional liquid-phase separation method for mapping of cellular proteins with identification using MALDI-TOF mass spectrometry
    • Wall D.B., Kachman M.T., Gong S., Hinderer R., Parus S., Misek D.E., Hanash S.M., Lubman D.M. Isoelectric focusing nonporous RP HPLC a two-dimensional liquid-phase separation method for mapping of cellular proteins with identification using MALDI-TOF mass spectrometry . Anal. Chem. 73:2001;1219-1227.
    • (2001) Anal. Chem. , vol.73 , pp. 1219-1227
    • Wall, D.B.1    Kachman, M.T.2    Gong, S.3    Hinderer, R.4    Parus, S.5    Misek, D.E.6    Hanash, S.M.7    Lubman, D.M.8
  • 31
    • 0030982143 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in mammalian cells
    • Grune T., Reinheckel T., Davies K.S. Degradation of oxidized proteins in mammalian cells. FASEB J. 11:1997;526-534.
    • (1997) FASEB J. , vol.11 , pp. 526-534
    • Grune, T.1    Reinheckel, T.2    Davies, K.S.3
  • 32
    • 0031105564 scopus 로고    scopus 로고
    • Proteasome inactivation upon aging and on oxidation-effect of HSP 90
    • Conconi M., Friguet B. Proteasome inactivation upon aging and on oxidation-effect of HSP 90. Mol. Biol. Rep. 24:1997;45-50.
    • (1997) Mol. Biol. Rep. , vol.24 , pp. 45-50
    • Conconi, M.1    Friguet, B.2
  • 34
    • 0034282468 scopus 로고    scopus 로고
    • Oxidative stress promotes specific protein damage in Saccharomyces cervisiae
    • Cabiscol E., Piulats E., Echave P., Herrero E., Ros J. Oxidative stress promotes specific protein damage in Saccharomyces cervisiae. J. Biol. Chem. 275:2000;27393-27398.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27393-27398
    • Cabiscol, E.1    Piulats, E.2    Echave, P.3    Herrero, E.4    Ros, J.5
  • 35
    • 0032579371 scopus 로고    scopus 로고
    • Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress
    • Tamarit J., Cabiscol E., Ros J. Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. J. Biol. Chem. 273:1998;3027-3032.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3027-3032
    • Tamarit, J.1    Cabiscol, E.2    Ros, J.3
  • 36
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: Dihydropyrimidinase-related protein 2, α-enolase and heat shock cognate 71
    • Castegna A., Aksenov M., Thongbookerd V., Klein J.B., Pierce W.M., Booze R., Markesbery W.R., Butterfield D.A. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II dihydropyrimidinase- related protein 2, α-enolase and heat shock cognate 71 . J. Neurochem. 82:2002;1524-1532.
    • (2002) J. Neurochem. , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongbookerd, V.3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6    Markesbery, W.R.7    Butterfield, D.A.8
  • 38
    • 0026341897 scopus 로고
    • Alpha B-crystallin in skeletal muscle: Purification and localization
    • Atomi Y., Yamada S., Strohman R., Nonomura Y. Alpha B-crystallin in skeletal muscle purification and localization . J. Biochem. (Tokyo). 110:1991;812-822.
    • (1991) J. Biochem. (Tokyo) , vol.110 , pp. 812-822
    • Atomi, Y.1    Yamada, S.2    Strohman, R.3    Nonomura, Y.4
  • 39
    • 0037096983 scopus 로고    scopus 로고
    • Effects of modifications of α-crystallin on its chaperone and other properties
    • Derham B.K., Harding J.J. Effects of modifications of α-crystallin on its chaperone and other properties. Biochem. J. 364:2002;711-717.
    • (2002) Biochem. J. , vol.364 , pp. 711-717
    • Derham, B.K.1    Harding, J.J.2
  • 40
    • 0028921023 scopus 로고
    • Effects of ageing on the motor unit
    • Larsson L., Ansved T. Effects of ageing on the motor unit. Prog. Neurobiol. 45:1995;397-458.
    • (1995) Prog. Neurobiol. , vol.45 , pp. 397-458
    • Larsson, L.1    Ansved, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.