메뉴 건너뛰기




Volumn 473, Issue , 2010, Pages 251-264

A Simple Method to Systematically Study Oxidatively Modified Proteins in Biological Samples and Its Applications

Author keywords

Cysteine oxidation; Functional redox proteomics; Reactive oxygen species

Indexed keywords

CYSTEINE; PROTEIN;

EID: 77956219883     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/S0076-6879(10)73013-5     Document Type: Chapter
Times cited : (16)

References (41)
  • 2
    • 0036745407 scopus 로고    scopus 로고
    • Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis
    • Baty, J.W., Hampton, M.B., Winterbourn, C.C., Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis. Proteomics 2 (2002), 1261–1266.
    • (2002) Proteomics , vol.2 , pp. 1261-1266
    • Baty, J.W.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 3
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett, B.S., 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
  • 4
    • 0942276251 scopus 로고    scopus 로고
    • A detergent- and cyanogen bromide-free method for integral membrane proteomics: Application to Halobacterium purple membranes and the human epidermal membrane proteome
    • Blonder, J., Conrads, T.P., Yu, L.R., Terunuma, A., Janini, G.M., Issaq, H.J., Vogel, J.C., Veenstra, T.D., A detergent- and cyanogen bromide-free method for integral membrane proteomics: Application to Halobacterium purple membranes and the human epidermal membrane proteome. Proteomics 4 (2004), 31–45.
    • (2004) Proteomics , vol.4 , pp. 31-45
    • Blonder, J.1    Conrads, T.P.2    Yu, L.R.3    Terunuma, A.4    Janini, G.M.5    Issaq, H.J.6    Vogel, J.C.7    Veenstra, T.D.8
  • 5
    • 1342323673 scopus 로고    scopus 로고
    • Oxidative stress, toxicology, and pharmacology of CYP2E1
    • Caro, A.A., Cederbaum, A.I., Oxidative stress, toxicology, and pharmacology of CYP2E1. Annu. Rev. Pharmacol. Toxicol. 44 (2004), 27–42.
    • (2004) Annu. Rev. Pharmacol. Toxicol. , vol.44 , pp. 27-42
    • Caro, A.A.1    Cederbaum, A.I.2
  • 6
    • 57249095767 scopus 로고    scopus 로고
    • Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions
    • Catalá, A., Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions. Chem. Phys. Lipids 157 (2009), 1–11.
    • (2009) Chem. Phys. Lipids , vol.157 , pp. 1-11
    • Catalá, A.1
  • 7
    • 31844443064 scopus 로고    scopus 로고
    • Inhibition of human mitochondrial aldehyde dehydrogenase by 4-hydroxynon-2-enal and 4-oxonon-2-enal
    • Doorn, J.A., Hurley, T.D., Petersen, D.R., Inhibition of human mitochondrial aldehyde dehydrogenase by 4-hydroxynon-2-enal and 4-oxonon-2-enal. Chem. Res. Toxicol. 19 (2006), 102–110.
    • (2006) Chem. Res. Toxicol. , vol.19 , pp. 102-110
    • Doorn, J.A.1    Hurley, T.D.2    Petersen, D.R.3
  • 8
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer, H., Schaur, R.J., Zollner, H., Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 11 (1991), 81–128.
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 9
    • 22544478126 scopus 로고    scopus 로고
    • Regulation of cys-based protein tyrosine phosphatases via reactive oxygen and nitrogen species in mast cells and basophils
    • Heneberg, P., Dráber, P., Regulation of cys-based protein tyrosine phosphatases via reactive oxygen and nitrogen species in mast cells and basophils. Curr. Med. Chem. 12 (2005), 1859–1871.
    • (2005) Curr. Med. Chem. , vol.12 , pp. 1859-1871
    • Heneberg, P.1    Dráber, P.2
  • 11
    • 0035849715 scopus 로고    scopus 로고
    • The biotin switch method for the detection of S-nitrosylated proteins
    • Jaffrey, S.R., Snyder, S.H., The biotin switch method for the detection of S-nitrosylated proteins. Sci. STKE, 2006, 2001, pL1.
    • (2001) Sci. STKE , vol.2006 , pp. pL1
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 13
    • 0034255470 scopus 로고    scopus 로고
    • Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH
    • Kim, J.R., Yoon, H.W., Kwon, K.S., Lee, S.R., Rhee, S.G., Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH. Anal. Biochem. 283 (2000), 214–221.
    • (2000) Anal. Biochem. , vol.283 , pp. 214-221
    • Kim, J.R.1    Yoon, H.W.2    Kwon, K.S.3    Lee, S.R.4    Rhee, S.G.5
  • 14
    • 0141509963 scopus 로고    scopus 로고
    • Constitutive induction of p-Erk1/2 accompanied by reduced activities of protein phosphatases 1 and 2A and MKP3 due to reactive oxygen species during cellular senescence
    • Kim, H.S., Song, M.C., Kwak, I.H., Park, T.J., Lim, I.K., Constitutive induction of p-Erk1/2 accompanied by reduced activities of protein phosphatases 1 and 2A and MKP3 due to reactive oxygen species during cellular senescence. J. Biol. Chem. 278 (2003), 37497–37510.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37497-37510
    • Kim, H.S.1    Song, M.C.2    Kwak, I.H.3    Park, T.J.4    Lim, I.K.5
  • 15
    • 33644500142 scopus 로고    scopus 로고
    • Increased oxidation and degradation of cytosolic proteins in alcohol-exposed mouse liver and hepatoma cells
    • Kim, B.J., Hood, B.L., Aragon, R.A., Hardwick, J.P., Conrads, T.P., Veenstra, T.D., Song, B.J., Increased oxidation and degradation of cytosolic proteins in alcohol-exposed mouse liver and hepatoma cells. Proteomics 6 (2006), 1250–1260.
    • (2006) Proteomics , vol.6 , pp. 1250-1260
    • Kim, B.J.1    Hood, B.L.2    Aragon, R.A.3    Hardwick, J.P.4    Conrads, T.P.5    Veenstra, T.D.6    Song, B.J.7
  • 16
    • 33746379603 scopus 로고    scopus 로고
    • JNK- and p38 kinase mediated phosphorylation of Bax leads to its activation, mitochondrial translocation and apoptosis of human hepatoma HepG2 cells
    • Kim, B.J., Ryu, S.W., Song, B.J., JNK- and p38 kinase mediated phosphorylation of Bax leads to its activation, mitochondrial translocation and apoptosis of human hepatoma HepG2 cells. J. Biol. Chem. 281 (2006), 21256–21265.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21256-21265
    • Kim, B.J.1    Ryu, S.W.2    Song, B.J.3
  • 18
    • 0035849714 scopus 로고    scopus 로고
    • S-nitrosylation is emerging as a specific and fundamental posttranslational protein modification: Head-to-head comparison with O-phosphorylation
    • Lane, P., Hao, G., Gross, S.S., S-nitrosylation is emerging as a specific and fundamental posttranslational protein modification: Head-to-head comparison with O-phosphorylation. Sci. STKE, 2006, 2001, RE1.
    • (2001) Sci. STKE , vol.2006 , pp. RE1
    • Lane, P.1    Hao, G.2    Gross, S.S.3
  • 19
    • 0028181674 scopus 로고
    • 6-methylguanine-DNA-methyltransferase
    • 6-methylguanine-DNA-methyltransferase. Carcinogenesis 15 (1994), 443–447.
    • (1994) Carcinogenesis , vol.15 , pp. 443-447
    • Laval, F.1    Wink, D.A.2
  • 21
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin, M.T., Beal, M.F., Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443 (2006), 787–795.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 22
    • 67649933847 scopus 로고    scopus 로고
    • Chemistry and biology of DNA containing 1, N(2)-deoxyguanosine adducts of the alpha, beta-unsaturated aldehydes acrolein, crotonaldehyde, and 4-hydroxynonenal
    • Minko, I.G., Kozekov, I.D., Harris, T.M., Rizzo, C.J., Lloyd, R.S., Stone, M.P., Chemistry and biology of DNA containing 1, N(2)-deoxyguanosine adducts of the alpha, beta-unsaturated aldehydes acrolein, crotonaldehyde, and 4-hydroxynonenal. Chem. Res. Toxicol. 22 (2009), 759–778.
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 759-778
    • Minko, I.G.1    Kozekov, I.D.2    Harris, T.M.3    Rizzo, C.J.4    Lloyd, R.S.5    Stone, M.P.6
  • 23
    • 27544510276 scopus 로고    scopus 로고
    • Inhibition of mitochondrial aldehyde dehydrogenase by nitric oxide-mediated S-nitrosylation
    • Moon, K.H., Kim, B.J., Song, B.J., Inhibition of mitochondrial aldehyde dehydrogenase by nitric oxide-mediated S-nitrosylation. [FEBS Lett]. 579 (2005), 6115–6120.
    • (2005) [FEBS Lett]. , vol.579 , pp. 6115-6120
    • Moon, K.H.1    Kim, B.J.2    Song, B.J.3
  • 24
    • 33751003258 scopus 로고    scopus 로고
    • Inactivation of oxidized and S-nitrosylated mitochondrial proteins in alcoholic fatty liver of rats
    • Moon, K.H., Hood, B.L., Kim, B.J., Hardwick, J.P., Conrads, T.P., Veenstra, T.D., Song, B.J., Inactivation of oxidized and S-nitrosylated mitochondrial proteins in alcoholic fatty liver of rats. Hepatology 44 (2006), 1218–1230.
    • (2006) Hepatology , vol.44 , pp. 1218-1230
    • Moon, K.H.1    Hood, B.L.2    Kim, B.J.3    Hardwick, J.P.4    Conrads, T.P.5    Veenstra, T.D.6    Song, B.J.7
  • 25
    • 34547666779 scopus 로고    scopus 로고
    • Inactivation of cytosolic aldehyde dehydrogenase via S-nitrosylation in ethanol-exposed rat liver
    • Moon, K.H., Abdelmegeed, M.A., Song, B.J., Inactivation of cytosolic aldehyde dehydrogenase via S-nitrosylation in ethanol-exposed rat liver. FEBS Lett. 581 (2007), 3967–3972.
    • (2007) FEBS Lett. , vol.581 , pp. 3967-3972
    • Moon, K.H.1    Abdelmegeed, M.A.2    Song, B.J.3
  • 27
    • 53549125568 scopus 로고    scopus 로고
    • Mechanism of 3, 4-methylenedioxymethamphetamine (MDMA, ecstasy)-mediated mitochondrial dysfunction in rat liver
    • Moon, K.H., Upreti, V.V., Yu, L.R., Lee, I.J., Ye, X., Eddington, N.D., Veenstra, T.D., Song, B.J., Mechanism of 3, 4-methylenedioxymethamphetamine (MDMA, ecstasy)-mediated mitochondrial dysfunction in rat liver. Proteomics 8 (2008), 3906–3918.
    • (2008) Proteomics , vol.8 , pp. 3906-3918
    • Moon, K.H.1    Upreti, V.V.2    Yu, L.R.3    Lee, I.J.4    Ye, X.5    Eddington, N.D.6    Veenstra, T.D.7    Song, B.J.8
  • 28
    • 73449119542 scopus 로고    scopus 로고
    • Inhibition of hepatic mitochondrial aldehyde dehydrogenase by carbon tetrachloride through JNK-mediated phosphorylation
    • Moon, K.H., Lee, Y.M., Song, B.J., Inhibition of hepatic mitochondrial aldehyde dehydrogenase by carbon tetrachloride through JNK-mediated phosphorylation. Free Radic. Biol. Med. 48 (2010), 391–398.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 391-398
    • Moon, K.H.1    Lee, Y.M.2    Song, B.J.3
  • 30
    • 58849156556 scopus 로고    scopus 로고
    • Molecular mechanisms of alcoholic fatty liver
    • Purohit, V., Gao, B., Song, B.J., Molecular mechanisms of alcoholic fatty liver. Alcohol. Clin. Exp. Res. 33 (2009), 191–205.
    • (2009) Alcohol. Clin. Exp. Res. , vol.33 , pp. 191-205
    • Purohit, V.1    Gao, B.2    Song, B.J.3
  • 31
    • 49349115115 scopus 로고    scopus 로고
    • Protein and lipid nitration: Role in redox signaling and injury
    • Rubbo, H., Radi, R., Protein and lipid nitration: Role in redox signaling and injury. Biochim. Biophys. Acta 1780 (2008), 1318–1824.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 1318-1824
    • Rubbo, H.1    Radi, R.2
  • 32
    • 0031678654 scopus 로고    scopus 로고
    • Nitric oxide inactivates rat hepatic methionine adenosyltransferase in vivo by S-nitrosylation
    • Ruiz, F., Corrales, F.J., Miqued, C., Mato, J.M., Nitric oxide inactivates rat hepatic methionine adenosyltransferase in vivo by S-nitrosylation. Hepatology 28 (1998), 1051–1057.
    • (1998) Hepatology , vol.28 , pp. 1051-1057
    • Ruiz, F.1    Corrales, F.J.2    Miqued, C.3    Mato, J.M.4
  • 33
    • 2642576571 scopus 로고    scopus 로고
    • Isotope-coded affinity tag approach to identify and quantify oxidant-sensitive protein thiols
    • Sethuraman, M., McComb, M.E., Heibeck, T., Costello, C.E., Cohen, R.A., Isotope-coded affinity tag approach to identify and quantify oxidant-sensitive protein thiols. Mol. Cell. Proteomics 3 (2004), 273–278.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 273-278
    • Sethuraman, M.1    McComb, M.E.2    Heibeck, T.3    Costello, C.E.4    Cohen, R.A.5
  • 34
    • 0029829513 scopus 로고    scopus 로고
    • Ethanol-inducible cytochrome P450 2E1: Biochemistry, molecular biology, and clinical relevance: 1996 update
    • Song, B.J., Koop, D.R., Ingelman-Sundberg, M., Nanji, A., Cederbaum, A.I., Ethanol-inducible cytochrome P450 2E1: Biochemistry, molecular biology, and clinical relevance: 1996 update. Alcohol. Clin. Exp. Res. 20 (1996), 138A–146A.
    • (1996) Alcohol. Clin. Exp. Res. , vol.20 , pp. 138A-146A
    • Song, B.J.1    Koop, D.R.2    Ingelman-Sundberg, M.3    Nanji, A.4    Cederbaum, A.I.5
  • 35
    • 46149111662 scopus 로고    scopus 로고
    • Prevention of alcoholic fatty liver and mitochondrial dysfunction in the rat by long-chain polyunsaturated fatty acids
    • Song, B.J., Moon, K.H., Olsson, N.U., Salem, N. Jr., Prevention of alcoholic fatty liver and mitochondrial dysfunction in the rat by long-chain polyunsaturated fatty acids. J. Hepatol. 49 (2008), 262–273.
    • (2008) J. Hepatol. , vol.49 , pp. 262-273
    • Song, B.J.1    Moon, K.H.2    Olsson, N.U.3    Salem, N.4
  • 36
    • 0142151375 scopus 로고    scopus 로고
    • Oxidation of methionine residues of proteins: Biological consequences
    • Stadtman, E.R., Moskovitz, J., Levine, R.L., Oxidation of methionine residues of proteins: Biological consequences. Antioxid. Redox Signal. 5 (2003), 577–582.
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 577-582
    • Stadtman, E.R.1    Moskovitz, J.2    Levine, R.L.3
  • 37
    • 8744304760 scopus 로고    scopus 로고
    • Identification of oxidized mitochondrial proteins in alcohol-exposed human hepatoma cells and mouse liver
    • Suh, S.K., Hood, B.L., Kim, B.J., Conrad, T.P., Veenstra, T.D., Song, B.J., Identification of oxidized mitochondrial proteins in alcohol-exposed human hepatoma cells and mouse liver. Proteomics 4 (2004), 3401–3412.
    • (2004) Proteomics , vol.4 , pp. 3401-3412
    • Suh, S.K.1    Hood, B.L.2    Kim, B.J.3    Conrad, T.P.4    Veenstra, T.D.5    Song, B.J.6
  • 40
    • 2642579275 scopus 로고    scopus 로고
    • Expression and purification of his-tagged rat mitochondrial 3-ketoacyl-CoA thiolase wild type and His352 mutant proteins
    • Zeng, J., Li, D., Expression and purification of his-tagged rat mitochondrial 3-ketoacyl-CoA thiolase wild type and His352 mutant proteins. Protein Expr. Purif. 35 (2004), 320–326.
    • (2004) Protein Expr. Purif. , vol.35 , pp. 320-326
    • Zeng, J.1    Li, D.2
  • 41
    • 69249099667 scopus 로고    scopus 로고
    • S-Glutathionylation of the Rpn2 regulatory subunit inhibits 26S proteosomal function
    • Zmijewski, J., Banerjee, S., Abraham, E., S-Glutathionylation of the Rpn2 regulatory subunit inhibits 26S proteosomal function. J. Biol. Chem. 284 (2009), 22213–22221.
    • (2009) J. Biol. Chem. , vol.284 , pp. 22213-22221
    • Zmijewski, J.1    Banerjee, S.2    Abraham, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.