메뉴 건너뛰기




Volumn 21, Issue 5, 2008, Pages 1074-1085

Measurement of protein sulfhydryls in response to cellular oxidative stress using gel electrophoresis and multiplexed fluorescent imaging analysis

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; MALEIMIDE; MENADIONE; OXIDIZING AGENT; TERT BUTYL HYDROPEROXIDE; THIOL DERIVATIVE; FLUORESCENT DYE; MALEIMIDE DERIVATIVE; PHOSPHINE DERIVATIVE; PROTEIN; TRI N BUTYLPHOSPHINE; TRI-N-BUTYLPHOSPHINE;

EID: 47549092593     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx8000708     Document Type: Article
Times cited : (6)

References (47)
  • 1
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge, W. (2002) Free radicals in the physiological control of cell function. Physiol. Rev. 82, 47-95.
    • (2002) Physiol. Rev , vol.82 , pp. 47-95
    • Droge, W.1
  • 3
    • 9944235916 scopus 로고    scopus 로고
    • The role of cysteine residues as redox-sensitive regulatory switches
    • Bardford, D. (2004) The role of cysteine residues as redox-sensitive regulatory switches. Curr. Opin. Chem. Biol. 14, 679-686.
    • (2004) Curr. Opin. Chem. Biol , vol.14 , pp. 679-686
    • Bardford, D.1
  • 4
    • 33750915802 scopus 로고    scopus 로고
    • Regulation of signal transduction through protein cysteine oxidation
    • Cross, J. V., and Templeton, D. J. (2006) Regulation of signal transduction through protein cysteine oxidation. Antiox. Redox Signal. 8, 1819-1827.
    • (2006) Antiox. Redox Signal , vol.8 , pp. 1819-1827
    • Cross, J.V.1    Templeton, D.J.2
  • 5
    • 0036893153 scopus 로고    scopus 로고
    • Redox and oxygen-sensitive transcription factors in the regulation of oxidant-mediated lung injury: Role for nuclear factor-κB
    • Haddad, J. J. (2002) Redox and oxygen-sensitive transcription factors in the regulation of oxidant-mediated lung injury: role for nuclear factor-κB. Critical Care 6, 481-490.
    • (2002) Critical Care , vol.6 , pp. 481-490
    • Haddad, J.J.1
  • 6
    • 33846934941 scopus 로고    scopus 로고
    • A classification scheme for redox-based modifications of proteins
    • Forrester, M. T., and Stamler, J. S. (2007) A classification scheme for redox-based modifications of proteins. Am. J.Respir. Cell Mol. Biol. 36, 135-137.
    • (2007) Am. J.Respir. Cell Mol. Biol , vol.36 , pp. 135-137
    • Forrester, M.T.1    Stamler, J.S.2
  • 8
    • 37549071817 scopus 로고    scopus 로고
    • Oxidative stress and antioxidants in the pathogenesis of pulmonary fibrosis: A potential role for nrf2
    • Walters, D. M., Cho, H. Y., and Kleeberger, S. R. (2008) Oxidative stress and antioxidants in the pathogenesis of pulmonary fibrosis: a potential role for nrf2. Antiox. Redox. Signal. 10, 321-332.
    • (2008) Antiox. Redox. Signal , vol.10 , pp. 321-332
    • Walters, D.M.1    Cho, H.Y.2    Kleeberger, S.R.3
  • 9
    • 84889312510 scopus 로고    scopus 로고
    • Oxidative damage to proteins: Structural modifications and consequences in cell function
    • Dalle-Donne, I, Scaloni, A, and Butterfield, D. A, Eds, pp, John Wiley and Sons, NJ
    • Cabiscol, E. and Ros, J. (2006) Oxidative damage to proteins: Structural modifications and consequences in cell function. In: Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases. (Dalle-Donne, I., Scaloni, A., and Butterfield, D. A., Eds.), pp 399-472, John Wiley and Sons, NJ.
    • (2006) Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases , pp. 399-472
    • Cabiscol, E.1    Ros, J.2
  • 10
    • 0037015035 scopus 로고    scopus 로고
    • Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants
    • Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., and Talalay, P. (2002) Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc. Natl. Acad. Sci. U.S.A. 99, 11908-11913.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 11908-11913
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Cole, R.N.3    Itoh, K.4    Wakabayashi, N.5    Katoh, Y.6    Yamamoto, M.7    Talalay, P.8
  • 11
    • 24744453945 scopus 로고    scopus 로고
    • Specific patterns of electrophile adduction trigger Keap1 ubiquitination and Nrf2 activation
    • Hong, F., Sckhar, K. R., Freeman, M. L., and Liebler, D. C. (2005) Specific patterns of electrophile adduction trigger Keap1 ubiquitination and Nrf2 activation. J. Biol. Chem. 280, 31768-31775.
    • (2005) J. Biol. Chem , vol.280 , pp. 31768-31775
    • Hong, F.1    Sckhar, K.R.2    Freeman, M.L.3    Liebler, D.C.4
  • 12
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarachi, K., Engel, J. D., and Yamamoto, M. (1999) Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev. 13, 76-86.
    • (1999) Genes Dev , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarachi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 15
    • 48949098494 scopus 로고    scopus 로고
    • Involvement of oxidants in the etiology of chronic airway diseases: Proteomic approaches to identify redox properties in epithelial cell signaling and inflammation
    • Dalle-Donne, I, Scaloni, A, and Butterfield, D. A, Eds, pp, John Wiley and Sons, NJ
    • Van der Vliet, A., Reynaert, N. L., Bove, P. F., Ckless, K., Greul, A., Hristova, M., and Janssen-Heininger, Y. (2006) Involvement of oxidants in the etiology of chronic airway diseases: Proteomic approaches to identify redox properties in epithelial cell signaling and inflammation. In: Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases. (Dalle-Donne, I., Scaloni, A., and Butterfield, D. A., Eds.), pp 831-876, John Wiley and Sons, NJ.
    • (2006) Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases , pp. 831-876
    • Van der Vliet, A.1    Reynaert, N.L.2    Bove, P.F.3    Ckless, K.4    Greul, A.5    Hristova, M.6    Janssen-Heininger, Y.7
  • 16
    • 0037205455 scopus 로고    scopus 로고
    • Proteomics analysis of cellular response to oxidative stress: Evidence for in vivo overoxidation of peroxiredoxins at their active site
    • Rabilloud, T., Heller, M., Gasnier, F., Luche, S., Rey, C., Aebersold, R., Benahmed, M., Louisot, P., and Lunard, J. (2002) Proteomics analysis of cellular response to oxidative stress: evidence for in vivo overoxidation of peroxiredoxins at their active site. J. Biol. Chem. 277, 19396-19401.
    • (2002) J. Biol. Chem , vol.277 , pp. 19396-19401
    • Rabilloud, T.1    Heller, M.2    Gasnier, F.3    Luche, S.4    Rey, C.5    Aebersold, R.6    Benahmed, M.7    Louisot, P.8    Lunard, J.9
  • 17
    • 33645683071 scopus 로고    scopus 로고
    • Transgenic mice overexpressing peroxiredoxin 6 show increased resistance to lung injury in hyperoxia
    • Wang, Y., Phelan, S. A., Manevich, Y., Feinstein, S. I., and Fisher, A. B. (2006) Transgenic mice overexpressing peroxiredoxin 6 show increased resistance to lung injury in hyperoxia. Am. J. Respir. Cell Mol. Biol. 34, 481-486.
    • (2006) Am. J. Respir. Cell Mol. Biol , vol.34 , pp. 481-486
    • Wang, Y.1    Phelan, S.A.2    Manevich, Y.3    Feinstein, S.I.4    Fisher, A.B.5
  • 18
    • 33947096960 scopus 로고    scopus 로고
    • Mechanistic basis for inflammation and tumor promotion in lungs of 2,6-di-tert-butyl-4-methylphenol-treated mice: Electrophilic metabolites alkylate and inactivate antioxidant enzymes
    • Meier, B. W., Gomez, J. D., Kirichenko, O. V., and Thompson, J. A. (2007) Mechanistic basis for inflammation and tumor promotion in lungs of 2,6-di-tert-butyl-4-methylphenol-treated mice: electrophilic metabolites alkylate and inactivate antioxidant enzymes. Chem. Res. Toxicol. 20, 199-207.
    • (2007) Chem. Res. Toxicol , vol.20 , pp. 199-207
    • Meier, B.W.1    Gomez, J.D.2    Kirichenko, O.V.3    Thompson, J.A.4
  • 19
    • 34250806432 scopus 로고    scopus 로고
    • Thiol-disulfide oxidoreduction of protein cysteines: Old methods revisited for proteomics
    • Dalle-Donne, I, Scaloni, A, and Butterfield, D. A, Eds, pp, John Wiley and Sons, NJ
    • Bonetto, V. and Ghezzi, P. (2006) Thiol-disulfide oxidoreduction of protein cysteines: Old methods revisited for proteomics. In: Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases. (Dalle-Donne, I., Scaloni, A., and Butterfield, D. A., Eds.), pp 101-122, John Wiley and Sons, NJ.
    • (2006) Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases , pp. 101-122
    • Bonetto, V.1    Ghezzi, P.2
  • 20
    • 0036745407 scopus 로고    scopus 로고
    • Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis
    • Baty, J. W., Hampton, M. B., and Winterbourn, C. C. (2002) Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis. Proteomics 2, 1261-1266.
    • (2002) Proteomics , vol.2 , pp. 1261-1266
    • Baty, J.W.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 21
    • 33750030779 scopus 로고    scopus 로고
    • Detection of reversible protein thiol modifications in tissues
    • Rogers, L. K., Leinweber, B. L., and Smith, C. V. (2006) Detection of reversible protein thiol modifications in tissues. Anal. Biochem. 358, 171-184.
    • (2006) Anal. Biochem , vol.358 , pp. 171-184
    • Rogers, L.K.1    Leinweber, B.L.2    Smith, C.V.3
  • 22
  • 23
    • 0021671419 scopus 로고
    • Alterations in intracellular SH homeostasis during metabolism of menadione by isolated rat hepatocytes
    • Dimonte, D., Ross, D., Bellomo, G., Eklow, L., and Orrenius, S. (1984) Alterations in intracellular SH homeostasis during metabolism of menadione by isolated rat hepatocytes. Arch. Biochem. Biophys. 235, 334-342.
    • (1984) Arch. Biochem. Biophys , vol.235 , pp. 334-342
    • Dimonte, D.1    Ross, D.2    Bellomo, G.3    Eklow, L.4    Orrenius, S.5
  • 24
    • 1642409412 scopus 로고    scopus 로고
    • Cy5 maleimide labeling for sensitive detection of free thiols in native protein extracts: Identification of seed proteins targeted by barley thioredoxin h isoforms
    • Maeda, K., Finnie, C., and Svensson, B. (2004) Cy5 maleimide labeling for sensitive detection of free thiols in native protein extracts: identification of seed proteins targeted by barley thioredoxin h isoforms. Biochem. J. 378, 497-507.
    • (2004) Biochem. J , vol.378 , pp. 497-507
    • Maeda, K.1    Finnie, C.2    Svensson, B.3
  • 26
    • 18844447205 scopus 로고    scopus 로고
    • Saturation labeling with cysteine-reactive cyanine fluorescent dyes provides increased sensitivity for protein expression profiling of laser-microdissected clinical specimens
    • Greengauz-Roberts, O., Stoppler, H., Nomura, S., Yamaguchi, H., Goldenring, J. R., Podolsky, R. H., Lee, J. R., and Dynan, W. S. (2005) Saturation labeling with cysteine-reactive cyanine fluorescent dyes provides increased sensitivity for protein expression profiling of laser-microdissected clinical specimens. Proteomics 5, 1746-57.
    • (2005) Proteomics , vol.5 , pp. 1746-1757
    • Greengauz-Roberts, O.1    Stoppler, H.2    Nomura, S.3    Yamaguchi, H.4    Goldenring, J.R.5    Podolsky, R.H.6    Lee, J.R.7    Dynan, W.S.8
  • 27
    • 0347134635 scopus 로고    scopus 로고
    • Thiol-reactive dyes for fluorescence labeling of proteomic samples
    • Tyagarajan, K., Pretzer, E., and Wiktorowicz, J. E. (2003) Thiol-reactive dyes for fluorescence labeling of proteomic samples. Electrophoresis 24, 2348-2358.
    • (2003) Electrophoresis , vol.24 , pp. 2348-2358
    • Tyagarajan, K.1    Pretzer, E.2    Wiktorowicz, J.E.3
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 48949106267 scopus 로고    scopus 로고
    • ™ Software, MASCOT ™ Database Search Engine V2.1, Applied Biosystems, accessed January 18
    • GPS Explorer ™ Software, MASCOT ™ Database Search Engine V2.1, Applied Biosystems, accessed January 18, 2007.
    • (2007) GPS Explorer
  • 34
    • 35848929694 scopus 로고    scopus 로고
    • Analysis and validation of proteomic data generated by tandem mass spectrometry
    • Nesvizhskii, A., Vitek, O., and Aebersold, R. (2007) Analysis and validation of proteomic data generated by tandem mass spectrometry. Nature Methods 4, 787-797.
    • (2007) Nature Methods , vol.4 , pp. 787-797
    • Nesvizhskii, A.1    Vitek, O.2    Aebersold, R.3
  • 35
    • 84889442289 scopus 로고    scopus 로고
    • Use of a proteomic technique to identify oxidant sensitive thiol proteins in cultured cells
    • Dalle-Donne, I, Scaloni, A, and Butterfield, D. A, Eds, pp, John Wiley and Sons, NJ
    • Hampton, M. B., Baty, J. W., and Winterbourn, C. C. (2006) Use of a proteomic technique to identify oxidant sensitive thiol proteins in cultured cells. In: Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases. (Dalle-Donne, I., Scaloni, A., and Butterfield, D. A., Eds.), pp 253-265, John Wiley and Sons, NJ.
    • (2006) Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases , pp. 253-265
    • Hampton, M.B.1    Baty, J.W.2    Winterbourn, C.C.3
  • 36
    • 48949099489 scopus 로고    scopus 로고
    • ICAT (isotope coded affinity tag) approach to redox proteomics: Identification and quantitation of oxidant-sensitive protein SHs
    • Dalle-Donne, I, Scaloni, A, and Butterfield, D. A, Eds, pp, John Wiley and Sons, NJ
    • Sethuraman, M., McComb, M. E., Huang, H., Huang, S., Heinbeck, T., Costello, C. E., and Cohen, R. A. (2006) ICAT (isotope coded affinity tag) approach to redox proteomics: Identification and quantitation of oxidant-sensitive protein SHs. In: Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases. (Dalle-Donne, I., Scaloni, A., and Butterfield, D. A., Eds.), pp 267-285, John Wiley and Sons, NJ.
    • (2006) Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases , pp. 267-285
    • Sethuraman, M.1    McComb, M.E.2    Huang, H.3    Huang, S.4    Heinbeck, T.5    Costello, C.E.6    Cohen, R.A.7
  • 37
    • 0043166918 scopus 로고    scopus 로고
    • Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes
    • Shaw, J., Rowlinson, R., Nickson, J., Stone, T., Sweet, A., Williams, K., and Tonge, R. (2003) Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes. Proteomics 3, 1181-1195.
    • (2003) Proteomics , vol.3 , pp. 1181-1195
    • Shaw, J.1    Rowlinson, R.2    Nickson, J.3    Stone, T.4    Sweet, A.5    Williams, K.6    Tonge, R.7
  • 39
    • 0036669447 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis; better than a poke in the ICAT?
    • Patton, W. F., Schulenberg, B., and Steinberg, T. H. (2002) Two-dimensional gel electrophoresis; better than a poke in the ICAT? Curr. Opin. Biotechnol 13, 321-328.
    • (2002) Curr. Opin. Biotechnol , vol.13 , pp. 321-328
    • Patton, W.F.1    Schulenberg, B.2    Steinberg, T.H.3
  • 40
    • 0025330175 scopus 로고
    • Non-enzymatic covalent binding of radioactivity from [14C]thiourea to rat lung protein
    • Hollinger, M. A., and Giri, S. N. (1990) Non-enzymatic covalent binding of radioactivity from [14C]thiourea to rat lung protein. Toxicol. Lett. 52, 1-5.
    • (1990) Toxicol. Lett , vol.52 , pp. 1-5
    • Hollinger, M.A.1    Giri, S.N.2
  • 41
    • 0028355875 scopus 로고
    • Protein S-thiolation in hepatocytes stimulated by t-butyl hydroperoxide, menadione, and neutrophils
    • Chai, Y. C., Hendrich, S., and Thomas, J. A. (1994) Protein S-thiolation in hepatocytes stimulated by t-butyl hydroperoxide, menadione, and neutrophils. Arch. Biochem. Biophys. 310, 264-272.
    • (1994) Arch. Biochem. Biophys , vol.310 , pp. 264-272
    • Chai, Y.C.1    Hendrich, S.2    Thomas, J.A.3
  • 42
    • 3242773844 scopus 로고    scopus 로고
    • Proteomic capacity of recent fluorescent dyes for protein staining
    • Chevalier, F., Rofidal, V., Vanova, P., Bergoin, A., and Rossignol, M. (2004) Proteomic capacity of recent fluorescent dyes for protein staining. Phytochemistry 65, 1499-1506.
    • (2004) Phytochemistry , vol.65 , pp. 1499-1506
    • Chevalier, F.1    Rofidal, V.2    Vanova, P.3    Bergoin, A.4    Rossignol, M.5
  • 44
    • 0036401454 scopus 로고    scopus 로고
    • Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis
    • Lind, C., Gerdes, R., Hamnell, Y., Schuppe-Koistinen, I., von Lowenhielm, H. B., Holmgren, A., and Cotgreave, I. A. (2002) Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis. Arch. Biochem. Biophys. 406, 229-240.
    • (2002) Arch. Biochem. Biophys , vol.406 , pp. 229-240
    • Lind, C.1    Gerdes, R.2    Hamnell, Y.3    Schuppe-Koistinen, I.4    von Lowenhielm, H.B.5    Holmgren, A.6    Cotgreave, I.A.7
  • 46
    • 22944478928 scopus 로고    scopus 로고
    • Identification of proteins adducted by reactive naphthalene metabolites in vitro
    • Isbell, M. A., Morin, D., Boland, B., Buckpitt, A. R., Salemi, M. R., and Presley, J. (2005) Identification of proteins adducted by reactive naphthalene metabolites in vitro. Proteomics 5, 4197-1204.
    • (2005) Proteomics , vol.5 , pp. 4197-1204
    • Isbell, M.A.1    Morin, D.2    Boland, B.3    Buckpitt, A.R.4    Salemi, M.R.5    Presley, J.6
  • 47
    • 26844454132 scopus 로고    scopus 로고
    • Wu, J., and Thomassen, M. J. (2005) Differential proteomic analysis of bronchoalveolar lavage fluid in asthmatics following segmental antigen challenge. Mol. Cell. Proteomics 4.9, 1251-1264.
    • Wu, J., and Thomassen, M. J. (2005) Differential proteomic analysis of bronchoalveolar lavage fluid in asthmatics following segmental antigen challenge. Mol. Cell. Proteomics 4.9, 1251-1264.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.