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Volumn 10, Issue 14, 2010, Pages 2692-2700

Quantitative evaluation of tryptophan oxidation in actin and troponin I from skeletal muscles using a rat model of acute oxidative stress

Author keywords

Alpha skeletal actin; Animal proteomics; Kynurenine; MS MS; Protein oxidation; ROS

Indexed keywords

5 HYDROXYTRYPTOPHAN; ACTIN; KYNURENINE; TROPONIN I; TRYPTOPHAN;

EID: 77954692363     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000147     Document Type: Article
Times cited : (31)

References (32)
  • 1
    • 71449123049 scopus 로고    scopus 로고
    • Effects of tryptophan and 5-hydroxytryptophan on the hepatic cell membrane rigidity due to oxidative stress
    • Reyes-Gonzales, M. C., Fuentes-Broto, L., Martinez-Ballarin, E., Miana-Mena, F. J. et al., Effects of tryptophan and 5-hydroxytryptophan on the hepatic cell membrane rigidity due to oxidative stress. J. Membr. Biol. 2009, 231, 93-99.
    • (2009) J. Membr. Biol. , vol.231 , pp. 93-99
    • Reyes-Gonzales, M.C.1    Fuentes-Broto, L.2    Martinez-Ballarin, E.3    Miana-Mena, F.J.4
  • 2
    • 18444410751 scopus 로고    scopus 로고
    • Photochemistry of kynurenine, a tryptophan metabolite: Properties of the triplet state
    • Tsentalovich, Y. P., Snytnikova, O. A., Sherin, P. S., Forbes, M. D., Photochemistry of kynurenine, a tryptophan metabolite: properties of the triplet state. J. Phys. Chem. A 2005, 109, 3565-3568.
    • (2005) J. Phys. Chem. A , vol.109 , pp. 3565-3568
    • Tsentalovich, Y.P.1    Snytnikova, O.A.2    Sherin, P.S.3    Forbes, M.D.4
  • 3
    • 48449091060 scopus 로고    scopus 로고
    • Proteomic and oxidative stress analysis in human brain samples of huntington disease
    • Sorolla, M. A., Reverter-Branchat, G., Tamarit, J., Ferrer, I. et al., Proteomic and oxidative stress analysis in human brain samples of huntington disease. Free Radic. Biol. Med. 2008, 45, 667-678.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 667-678
    • Sorolla, M.A.1    Reverter-Branchat, G.2    Tamarit, J.3    Ferrer, I.4
  • 5
    • 0347991814 scopus 로고    scopus 로고
    • Histidine and lysine as targets of oxidative modification
    • DOI 10.1007/s00726-003-0015-y
    • Uchida, K., Histidine and lysine as targets of oxidative modification. Amino Acids 2003, 25 249-257. (Pubitemid 38041263)
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 249-257
    • Uchida, K.1
  • 6
    • 0036402152 scopus 로고    scopus 로고
    • Proteasome function and protein oxidation in the aged retina
    • Louie, J. L., Kapphahn, R. J., Ferrington, D. A., Proteasome function and protein oxidation in the aged retina. Exp. Eye Res. 2002, 75, 271-284.
    • (2002) Exp. Eye Res. , vol.75 , pp. 271-284
    • Louie, J.L.1    Kapphahn, R.J.2    Ferrington, D.A.3
  • 7
    • 0034881033 scopus 로고    scopus 로고
    • Oxidative stress and protein aggregation during biological aging
    • Squier, T. C., Oxidative stress and protein aggregation during biological aging. Exp. Gerontol. Mol. Aging 2001, 36, 1539-1550.
    • (2001) Exp. Gerontol. Mol. Aging , vol.36 , pp. 1539-1550
    • Squier, T.C.1
  • 8
    • 77953616825 scopus 로고    scopus 로고
    • Profiling of residue-level photo-oxidative damage in peptides
    • DOI 10.1007/s00726-009-0440-7
    • Grosvenor, A. J., Morton, J. D., Dyer, J. M., Profiling of residue-level photo-oxidative damage in peptides. Amino Acids 2009, DOI 10.1007/s00726-009- 0440-7.
    • (2009) Amino Acids
    • Grosvenor, A.J.1    Morton, J.D.2    Dyer, J.M.3
  • 9
    • 40949091390 scopus 로고    scopus 로고
    • Can tryptophan oxidation lead to lower tryptophan level in diabetes? A commentary on "Propagation of protein glycation damage involves modification of tryptophan residues via reactive oxygen species: Inhibition by pyridoxamine."
    • Jain, S. K., Can tryptophan oxidation lead to lower tryptophan level in diabetes? A commentary on "Propagation of protein glycation damage involves modification of tryptophan residues via reactive oxygen species: inhibition by pyridoxamine." Free Radic. Biol. Med. 2008, 44, 1273-1275.
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1273-1275
    • Jain, S.K.1
  • 10
    • 0038820056 scopus 로고    scopus 로고
    • Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins
    • Taylor, S. W., Fahy, E., Murray, J., Capaldi, R. A. et al., Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins. J. Biol. Chem. 2003, 278, 19587-19590.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19587-19590
    • Taylor, S.W.1    Fahy, E.2    Murray, J.3    Capaldi, R.A.4
  • 11
    • 31344457662 scopus 로고    scopus 로고
    • Protein oxidation in plant mitochondria detected as oxidized tryptophan
    • Moller, I. M., Kristensen, B. K., Protein oxidation in plant mitochondria detected as oxidized tryptophan. Free Radic. Biol. Med. 2006, 40, 430-435.
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 430-435
    • Moller, I.M.1    Kristensen, B.K.2
  • 12
    • 0031791713 scopus 로고    scopus 로고
    • Identification of tryptophan oxidation products in bovine alpha-crystallin
    • Finley, E. L., Dillon, J., Crouch, R. K., Schey, K. L., Identification of tryptophan oxidation products in bovine alphacrystallin. Protein Sci. 1998, 7, 2391-2397. (Pubitemid 28506955)
    • (1998) Protein Science , vol.7 , Issue.11 , pp. 2391-2397
    • Finley, E.L.1    Dillon, J.2    Crouch, R.K.3    Schey, K.L.4
  • 13
    • 0037085277 scopus 로고    scopus 로고
    • Novel protein modification by kynurenine in human lenses
    • Vazquez, S., Aquilina, J. A., Jamie, J. F., Sheil, M. M. et al., Novel protein modification by kynurenine in human lenses. J. Biol. Chem. 2002, 277, 4867-4873.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4867-4873
    • Vazquez, S.1    Aquilina, J.A.2    Jamie, J.F.3    Sheil, M.M.4
  • 14
    • 33846425366 scopus 로고    scopus 로고
    • Tryptophan 334 oxidation in bovine cytochrome c oxidase subunit I involves free radical migration
    • DOI 10.1016/j.febslet.2006.12.054, PII S0014579307000233
    • Lemma-Gray, P., Weintraub, S. T., Carroll, C. A., Musatov, A. et al., Tryptophan 334 oxidation in bovine cytochrome c oxidase subunit i involves free radical migration. FEBS Lett. 2007, 581, 437-442. (Pubitemid 46149616)
    • (2007) FEBS Letters , vol.581 , Issue.3 , pp. 437-442
    • Lemma-Gray, P.1    Weintraub, S.T.2    Carroll, C.A.3    Musatov, A.4    Robinson, N.C.5
  • 16
    • 0032143406 scopus 로고    scopus 로고
    • Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque
    • Fu, S., Davies, M. J., Stocker, R., Dean, R. T., Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque. Biochem. J. 1998, 333, 519-525. (Pubitemid 28398516)
    • (1998) Biochemical Journal , vol.333 , Issue.3 , pp. 519-525
    • Fu, S.1    Davies, M.J.2    Stocker, R.3    Dean, R.T.4
  • 17
    • 0034545719 scopus 로고    scopus 로고
    • Quantification and significance of protein oxidation in biological samples
    • Shacter, E., Quantification and significance of protein oxidation in biological samples. Drug Metab. Rev. 2000, 32, 307-326.
    • (2000) Drug Metab. Rev. , vol.32 , pp. 307-326
    • Shacter, E.1
  • 19
    • 46649095082 scopus 로고    scopus 로고
    • An oxidized tryptophan facilitates copper binding in Methylococcus capsulatus-secreted protein mope
    • Helland, R., Fjellbirkeland, A., Karlsen, O. A., Ve, T. et al., An oxidized tryptophan facilitates copper binding in Methylococcus capsulatus-secreted protein mope. J. Biol. Chem. 2008, 283, 13897-13904.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13897-13904
    • Helland, R.1    Fjellbirkeland, A.2    Karlsen, O.A.3    Ve, T.4
  • 20
    • 0035997273 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization-tandem mass spectrometry with high resolution and sensitivity for identification and characterization of proteins
    • DOI 10.1002/1615-9861(200207)2:7<868::AID-PROT868>3.0.CO;2-D
    • Bienvenut, W. V., Deon, C., Pasquarello, C., Campbell, J. M. et al., Matrix-assisted laser desorption/ionization-tandem mass spectrometry with high resolution and sensitivity for identification and characterization of proteins. Proteomics 2002, 2, 868-876. (Pubitemid 34803970)
    • (2002) Proteomics , vol.2 , Issue.7 , pp. 868-876
    • Bienvenut, W.V.1    Deon, C.2    Pasquarello, C.3    Campbell, J.M.4    Sanchez, J.-C.5    Vestal, M.L.6    Hochstrasser, D.F.7
  • 21
    • 0037637526 scopus 로고    scopus 로고
    • Identification of oxidation products and free radicals of tryptophan by mass spectrometry
    • Domingues, M. R., Domingues, P., Reis, A., Fonseca, C. et al., Identification of oxidation products and free radicals of tryptophan by mass spectrometry. J. Am. Soc. Mass Spectrom. 2003, 14, 406-416.
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 406-416
    • Domingues, M.R.1    Domingues, P.2    Reis, A.3    Fonseca, C.4
  • 22
    • 18444391517 scopus 로고    scopus 로고
    • Shotgun identification of protein modifications from protein complexes and lens tissue
    • MacCoss, M. J., McDonald, W. H., Saraf, A., Sadygov, R. et al., Shotgun identification of protein modifications from protein complexes and lens tissue. Proc. Natl. Acad. Sci. USA 2002, 99, 7900-7905.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7900-7905
    • MacCoss, M.J.1    McDonald, W.H.2    Saraf, A.3    Sadygov, R.4
  • 23
    • 8544240825 scopus 로고    scopus 로고
    • Mass spectral evidence for carbonate-anion-radical-induced posttranslational modification of tryptophan to kynurenine in human cu, zn superoxide dismutase
    • Zhang, H., Joseph, J., Crow, J., Kalyanaraman, B., Mass spectral evidence for carbonate-anion-radical-induced posttranslational modification of tryptophan to kynurenine in human cu, zn superoxide dismutase. Free. Radic. Biol. Med. 2004, 37, 2018-2026.
    • (2004) Free. Radic. Biol. Med. , vol.37 , pp. 2018-2026
    • Zhang, H.1    Joseph, J.2    Crow, J.3    Kalyanaraman, B.4
  • 24
    • 33750102362 scopus 로고    scopus 로고
    • Dynamics of rat hepatocyte histone glycoxidation after general X-ray irradiation
    • Kuleva, N. V., Fedorova, M. A., Frolov, A. A., Dynamics of rat hepatocyte histone glycoxidation after general X-ray irradiation. Tsitologyia 2006, 48, 515-521.
    • (2006) Tsitologyia , vol.48 , pp. 515-521
    • Kuleva, N.V.1    Fedorova, M.A.2    Frolov, A.A.3
  • 25
    • 71849118358 scopus 로고    scopus 로고
    • Reversible and irreversible modifications of skeletal muscle proteins in a rat model of acute oxidative stress
    • Fedorova, M., Kuleva, N., Hoffmann, R., Reversible and irreversible modifications of skeletal muscle proteins in a rat model of acute oxidative stress. Biochim. Biophys. Acta 2009, 1792, 1185-1193.
    • (2009) Biochim. Biophys. Acta , vol.1792 , pp. 1185-1193
    • Fedorova, M.1    Kuleva, N.2    Hoffmann, R.3
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using coomassie brilliant blue g-250 and r-250
    • Neuhoff, V., Arold, N., Taube, D., Ehrhardt, W., Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using coomassie brilliant blue g-250 and r-250. Electrophoresis 1988, 9, 255-262.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 28
    • 10544244161 scopus 로고    scopus 로고
    • Linking genome and proteome by mass spectrometry: Large-scale identification of yeast proteins from two dimensional gels
    • Shevchenko, A., Jensen, O. N., Podtelejnikov, A. V., Sagliocco, F. et al., Linking genome and proteome by mass spectrometry: Large-scale identification of yeast proteins from two dimensional gels. Proc. Natl. Acad. Sci. USA 1996, 93, 14440-14445.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14440-14445
    • Shevchenko, A.1    Jensen, O.N.2    Podtelejnikov, A.V.3    Sagliocco, F.4
  • 29
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann, M., Jensen, O. N., Proteomic analysis of post-translational modifications. Nat. Biotechnol. 2003, 21, 255-261.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 30
    • 1042275615 scopus 로고    scopus 로고
    • Modification-specific proteomics: Characterization of post-translational modifications by mass spectrometry
    • Jensen, O. N., Modification-specific proteomics: Characterization of post-translational modifications by mass spectrometry. Curr. Opin. Chem. Biol. 2004, 8, 33-41.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 33-41
    • Jensen, O.N.1
  • 31
    • 51249090739 scopus 로고    scopus 로고
    • Current approaches for global post-translational modification discovery and mass spectrometric analysis
    • Hoffman, M. D., Sniatynski, M. J., Kast, J., Current approaches for global post-translational modification discovery and mass spectrometric analysis. Anal. Chim. Acta 2008, 627, 50-61.
    • (2008) Anal. Chim. Acta , vol.627 , pp. 50-61
    • Hoffman, M.D.1    Sniatynski, M.J.2    Kast, J.3
  • 32
    • 77949837372 scopus 로고    scopus 로고
    • Identification of cysteine, methionine and tryptophan residues of actin oxidized in vivo during oxidative stress
    • Fedorova, M., Kuleva, N., Hoffmann, R., Identification of cysteine, methionine and tryptophan residues of actin oxidized in vivo during oxidative stress. J. Proteome Res. 2010, 9, 1598-1609.
    • (2010) J. Proteome Res. , vol.9 , pp. 1598-1609
    • Fedorova, M.1    Kuleva, N.2    Hoffmann, R.3


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