메뉴 건너뛰기




Volumn 7, Issue 9, 2008, Pages 3868-3878

Immediate protein targets of photodynamic treatment in carcinoma cells

Author keywords

Biotinylation; Carbonylation; Cysteine; Identification; Oxidation; Photodynamic treatment; Protein; Thiol

Indexed keywords

ARTICLE; CARCINOMA CELL; CONTROLLED STUDY; HUMAN; HUMAN CELL; MASS SPECTROMETRY; PHOTODYNAMIC THERAPY; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTEOMICS; TUMOR CELL; AFFINITY CHROMATOGRAPHY; APOPTOSIS; DRUG EFFECT; METABOLISM; OXIDATIVE STRESS; PATHOLOGY; PHOTOCHEMOTHERAPY; SQUAMOUS CELL CARCINOMA; TANDEM MASS SPECTROMETRY; TUMOR CELL LINE;

EID: 55249096730     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr800189q     Document Type: Article
Times cited : (39)

References (35)
  • 2
    • 0033794124 scopus 로고    scopus 로고
    • Signaling pathways in cell death and survival after photodynamic therapy
    • Moor, A. C. E. Signaling pathways in cell death and survival after photodynamic therapy. J. Photochem. Photobiol. 2000, 57, 1-13.
    • (2000) J. Photochem. Photobiol , vol.57 , pp. 1-13
    • Moor, A.C.E.1
  • 6
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee, S. R.; Kwon, K. S.; Kim, S. R.; Rhee, S. G. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J. Biol. Chem. 1998, 273 (25), 15366-14372.
    • (1998) J. Biol. Chem , vol.273 , Issue.25 , pp. 15366-14372
    • Lee, S.R.1    Kwon, K.S.2    Kim, S.R.3    Rhee, S.G.4
  • 7
    • 0034733807 scopus 로고    scopus 로고
    • Redox-dependent signal transduction
    • Finkel, T. Redox-dependent signal transduction. FEBS Lett. 2000, 476, 52-54.
    • (2000) FEBS Lett , vol.476 , pp. 52-54
    • Finkel, T.1
  • 8
    • 4344604345 scopus 로고    scopus 로고
    • Selectivity of protein carbonylation in the apoptotic response to oxidative stress associated with photodynamic therapy: A cell biochemical and proteomic investigation
    • Magi, B.; Ettorre, A.; Liberatori, S.; Bini, L.; Andreassi, M.; Frosali, S.; Neri, P.; Pallini, V.; Di Stefano, A. Selectivity of protein carbonylation in the apoptotic response to oxidative stress associated with photodynamic therapy: a cell biochemical and proteomic investigation. Cell Death Differ. 2004, 11, 842-852.
    • (2004) Cell Death Differ , vol.11 , pp. 842-852
    • Magi, B.1    Ettorre, A.2    Liberatori, S.3    Bini, L.4    Andreassi, M.5    Frosali, S.6    Neri, P.7    Pallini, V.8    Di Stefano, A.9
  • 10
    • 0032504189 scopus 로고    scopus 로고
    • Reactive oxygen species- and dimerization-induced activation of apoptosis signal-regulating kinase 1 in tumor necrosis factor-a signal transduction
    • Gotoh, Y.; Cooper, J. A. Reactive oxygen species- and dimerization-induced activation of apoptosis signal-regulating kinase 1 in tumor necrosis factor-a signal transduction. J. Biol. Chem. 1998, 273 (28), 17477-17482.
    • (1998) J. Biol. Chem , vol.273 , Issue.28 , pp. 17477-17482
    • Gotoh, Y.1    Cooper, J.A.2
  • 11
    • 35348846777 scopus 로고    scopus 로고
    • Photodynamic therapy with the phthalocyanine photosen- sitizer Pc4: The case experience with preclinical mechanistic and early clinical-translational studies
    • Miller, J. D.; Baron, E. D.; Scull, H.; Hsia, A.; Berlin, J. C.; McCormick, T.; Colussi, V.; Kenney, M. E.; Copper, K. D.; Oleinick, N. L. Photodynamic therapy with the phthalocyanine photosen- sitizer Pc4: The case experience with preclinical mechanistic and early clinical-translational studies. Toxicol. Appl. Pharmacol. 2007, 224, 290-299.
    • (2007) Toxicol. Appl. Pharmacol , vol.224 , pp. 290-299
    • Miller, J.D.1    Baron, E.D.2    Scull, H.3    Hsia, A.4    Berlin, J.C.5    McCormick, T.6    Colussi, V.7    Kenney, M.E.8    Copper, K.D.9    Oleinick, N.L.10
  • 12
    • 3042523891 scopus 로고    scopus 로고
    • Proteomic analysis of carbonylated proteins in two-dimentional gel electrophoresis using avidin-fluorescein affinity staining
    • Yoo, B.-S.; Regnier, F. Proteomic analysis of carbonylated proteins in two-dimentional gel electrophoresis using avidin-fluorescein affinity staining. Electrophoresis 2004, 25, 1334-1341.
    • (2004) Electrophoresis , vol.25 , pp. 1334-1341
    • Yoo, B.-S.1    Regnier, F.2
  • 13
    • 33644500142 scopus 로고    scopus 로고
    • Increased oxidation and degradation of cytosolic proteins in alcohol-exposed mouse liver and hepatoma cells
    • Kim, B.; Hood, B.; Aragon, R.; Hardwick, J.; Conrads, T.; Veenstra, T.; Song, B. Increased oxidation and degradation of cytosolic proteins in alcohol-exposed mouse liver and hepatoma cells. Proteomics 2006, 6, 1250-1260.
    • (2006) Proteomics , vol.6 , pp. 1250-1260
    • Kim, B.1    Hood, B.2    Aragon, R.3    Hardwick, J.4    Conrads, T.5    Veenstra, T.6    Song, B.7
  • 14
    • 17644362744 scopus 로고    scopus 로고
    • Affinity chromatographic selection of carbonylated proteins followed by identification of oxidation sites using tandem mass spectrometry
    • Mirzaei, H.; Regnier, F. Affinity chromatographic selection of carbonylated proteins followed by identification of oxidation sites using tandem mass spectrometry. Anal. Chem. 2005, 77(8), 2386-2392.
    • (2005) Anal. Chem , vol.77 , Issue.8 , pp. 2386-2392
    • Mirzaei, H.1    Regnier, F.2
  • 15
    • 0037218503 scopus 로고    scopus 로고
    • Proteomic method detects oxidatively induced protein carbonyls in muscles of a diabetes model otsuka long-evans tokushima fatty (OLETF) rat
    • Oh-Ishi, M.; Ueno, T.; Maeda, T. Proteomic method detects oxidatively induced protein carbonyls in muscles of a diabetes model otsuka long-evans tokushima fatty (OLETF) rat. Free Radical Biol. Med. 2003, 34 (1), 11-22.
    • (2003) Free Radical Biol. Med , vol.34 , Issue.1 , pp. 11-22
    • Oh-Ishi, M.1    Ueno, T.2    Maeda, T.3
  • 16
    • 27144441722 scopus 로고    scopus 로고
    • Oxidative modification of proteasome: Identification of an oxidation-sensitive subunit in 26S proteasome
    • Ishii, T.; Sakurai, T.; Usami, H.; Uchida, K. Oxidative modification of proteasome: identification of an oxidation-sensitive subunit in 26S proteasome. Biochemistry 2005, 44, 13893-13901.
    • (2005) Biochemistry , vol.44 , pp. 13893-13901
    • Ishii, T.1    Sakurai, T.2    Usami, H.3    Uchida, K.4
  • 17
    • 0036745407 scopus 로고    scopus 로고
    • Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis
    • Baty, J.; Hampton, M.; Winterbourn, C. Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis. Proteomics 2002, 2, 1261-1266.
    • (2002) Proteomics , vol.2 , pp. 1261-1266
    • Baty, J.1    Hampton, M.2    Winterbourn, C.3
  • 18
    • 26444506068 scopus 로고    scopus 로고
    • Correlation of relative abundance ratios derived from peptide ion chromato-grams and spectrum counting for quantitative proteomic analysis using stable isotope labeling
    • Zybailov, B.; Coleman, M.; Florens, L.; Washburn, M. Correlation of relative abundance ratios derived from peptide ion chromato-grams and spectrum counting for quantitative proteomic analysis using stable isotope labeling. Anal. Chem. 2005, 77, 6218-6224.
    • (2005) Anal. Chem , vol.77 , pp. 6218-6224
    • Zybailov, B.1    Coleman, M.2    Florens, L.3    Washburn, M.4
  • 19
    • 33750616737 scopus 로고    scopus 로고
    • Protein oxidation and proteolysis
    • Bader, N.; Grune, T. Protein oxidation and proteolysis. Biol. Chem. 2006, 387, 1351-1355.
    • (2006) Biol. Chem , vol.387 , pp. 1351-1355
    • Bader, N.1    Grune, T.2
  • 20
    • 0035861589 scopus 로고    scopus 로고
    • Photodynamic therapy induced apoptosis in epidermoid carcinoma cells
    • Lam, M.; Oleinick, N.; Nieminen, A. Photodynamic therapy induced apoptosis in epidermoid carcinoma cells. J. Biol. Chem. 2001, 276, 47379-47386.
    • (2001) J. Biol. Chem , vol.276 , pp. 47379-47386
    • Lam, M.1    Oleinick, N.2    Nieminen, A.3
  • 22
    • 0035805541 scopus 로고    scopus 로고
    • Involvement of Bcl-2 and Bax in photodynamic therapy-mediated apoptosis. Antisense Bcl-2 oligonucleotide sensitizes RIF 1 cells to photodynamic therapy apoptosis
    • Srivastava, M.; Ahmad, N.; Gupta, S.; Mukhtar, H. Involvement of Bcl-2 and Bax in photodynamic therapy-mediated apoptosis. Antisense Bcl-2 oligonucleotide sensitizes RIF 1 cells to photodynamic therapy apoptosis. J. Biol. Chem. 2001, 276, 15481-15488.
    • (2001) J. Biol. Chem , vol.276 , pp. 15481-15488
    • Srivastava, M.1    Ahmad, N.2    Gupta, S.3    Mukhtar, H.4
  • 23
  • 24
    • 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
  • 25
    • 0034282738 scopus 로고    scopus 로고
    • The CXXCXXC motif determins the folding, structure and stability of human Erol-La
    • Benham, A.; Cabibbo, A.; Fassio, A.; Bulleid, N.; Sitia, R.; Braakman, I. The CXXCXXC motif determins the folding, structure and stability of human Erol-La. EMBO J. 2000, 19, 4493-4502.
    • (2000) EMBO J , vol.19 , pp. 4493-4502
    • Benham, A.1    Cabibbo, A.2    Fassio, A.3    Bulleid, N.4    Sitia, R.5    Braakman, I.6
  • 26
    • 19444375216 scopus 로고    scopus 로고
    • Rhee, S.; Chae, H.; Kin, K. Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radical Biol. Med. 2005, 38, 1543-1552.
    • Rhee, S.; Chae, H.; Kin, K. Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radical Biol. Med. 2005, 38, 1543-1552.
  • 27
    • 1542359582 scopus 로고    scopus 로고
    • Carbonylation of glycolytic proteins is a key response to drug-induced oxidative stress and apoptosis
    • England, K.; O'Driscoll, C.; Cotter, T. Carbonylation of glycolytic proteins is a key response to drug-induced oxidative stress and apoptosis. Cell Death Differ. 2004, 11, 252-260.
    • (2004) Cell Death Differ , vol.11 , pp. 252-260
    • England, K.1    O'Driscoll, C.2    Cotter, T.3
  • 28
    • 20544459926 scopus 로고    scopus 로고
    • Proteomic detection of hydrogen peroxide-sensitive thiol proteins in Jurkat cells
    • Baty, J.; Hampton, M.; Winterbourn, C. Proteomic detection of hydrogen peroxide-sensitive thiol proteins in Jurkat cells. Biochem. J. 2005, 389, 785-795.
    • (2005) Biochem. J , vol.389 , pp. 785-795
    • Baty, J.1    Hampton, M.2    Winterbourn, C.3
  • 29
    • 11144221439 scopus 로고    scopus 로고
    • Widespread sulfenic acid formation in tissues in response to hydrogen peroxide
    • Saurin, A.; Neubert, H.; Brennan, J.; Eaton, P. Widespread sulfenic acid formation in tissues in response to hydrogen peroxide. Proc. Natl. Acad. Sci. U.S.A 2004, 101, 17982-17987.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 17982-17987
    • Saurin, A.1    Neubert, H.2    Brennan, J.3    Eaton, P.4
  • 30
    • 12344291243 scopus 로고    scopus 로고
    • Hsp90 and Cdc37 - a chaperone cancer conspiracy
    • Pearl, L. Hsp90 and Cdc37 - a chaperone cancer conspiracy. Curr. Opin. Genet. Dev. 2005, 15, 55-61.
    • (2005) Curr. Opin. Genet. Dev , vol.15 , pp. 55-61
    • Pearl, L.1
  • 32
    • 0035953399 scopus 로고    scopus 로고
    • In vitro and in vivo inhibition of epidermal growth factor receptor-tyrosine kinase pathway by photodynamic therapy
    • Ahmad, N.; Kalka, K.; Mukhtar, H. In vitro and in vivo inhibition of epidermal growth factor receptor-tyrosine kinase pathway by photodynamic therapy. Oncogene 2001, 20, 2314-2317.
    • (2001) Oncogene , vol.20 , pp. 2314-2317
    • Ahmad, N.1    Kalka, K.2    Mukhtar, H.3
  • 33
    • 33646777450 scopus 로고    scopus 로고
    • Identification of Ebpl as a component of cytoplasmic bcl-2 mRNP (messenger ribonucleoprotein particle) complexes
    • Bose, S.; Sengupta, T.; Bandyopadhyay, S.; Spicer, E. Identification of Ebpl as a component of cytoplasmic bcl-2 mRNP (messenger ribonucleoprotein particle) complexes. Biochem. J. 2006, 396, 99-107.
    • (2006) Biochem. J , vol.396 , pp. 99-107
    • Bose, S.1    Sengupta, T.2    Bandyopadhyay, S.3    Spicer, E.4
  • 34
    • 33846995658 scopus 로고    scopus 로고
    • Protein kinase C-δ phosphorylates Ebpl and prevents its proteolytic degradation, enhancing cell survival
    • Liu, Z.; Liu, X.; Nakayama, K.; Nakayama, K.; Ye, K. Protein kinase C-δ phosphorylates Ebpl and prevents its proteolytic degradation, enhancing cell survival. J. Neurochem. 2007, 100, 1278-1288.
    • (2007) J. Neurochem , vol.100 , pp. 1278-1288
    • Liu, Z.1    Liu, X.2    Nakayama, K.3    Nakayama, K.4    Ye, K.5
  • 35
    • 4344686072 scopus 로고    scopus 로고
    • Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP binding domain
    • Cross, J.; Templeton, D. Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP binding domain. Biochem. J. 2004, 381, 697-707.
    • (2004) Biochem. J , vol.381 , pp. 697-707
    • Cross, J.1    Templeton, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.