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Volumn 137, Issue 18, 2012, Pages 4287-4294

Comparative proteomic analysis of drug sodium iron chlorophyllin addition to Hep 3B cell line

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EID: 84864966846     PISSN: 00032654     EISSN: 13645528     Source Type: Journal    
DOI: 10.1039/c2an35436e     Document Type: Article
Times cited : (12)

References (41)
  • 1
    • 73649086926 scopus 로고    scopus 로고
    • Chinese human liver proteome project: A pathfinder of HUPO human liver proteome project
    • F. He Chinese human liver proteome project: a pathfinder of HUPO human liver proteome project J. Proteome Res. 2010 9 1 2
    • (2010) J. Proteome Res. , vol.9 , pp. 1-2
    • He, F.1
  • 2
    • 0033805542 scopus 로고    scopus 로고
    • Identification and characterization of chlorin e(4) ethyl ester in sera of individuals participating in the chlorophyllin chemoprevention trial
    • P. A. Egner K. H. Stansbury E. P. Snyder M. E. Rogers P. A. Hintz T. W. Kensler Identification and characterization of chlorin e(4) ethyl ester in sera of individuals participating in the chlorophyllin chemoprevention trial Chem. Res. Toxicol. 2000 13 9 900 906
    • (2000) Chem. Res. Toxicol. , vol.13 , Issue.9 , pp. 900-906
    • Egner, P.A.1    Stansbury, K.H.2    Snyder, E.P.3    Rogers, M.E.4    Hintz, P.A.5    Kensler, T.W.6
  • 3
    • 0344033666 scopus 로고    scopus 로고
    • Inhibitory effects of chlorophyllin, hemin and tetrakis(4-benzoic acid)porphyrin on oxidative DNA damage and mouse skin inflammation induced by 12-O-tetradecanoylphorbol-13-acetate as a possible anti-tumor promoting mechanism
    • K. K. Park J. H. Park Y. J. Jung W. Y. Chung Inhibitory effects of chlorophyllin, hemin and tetrakis(4-benzoic acid)porphyrin on oxidative DNA damage and mouse skin inflammation induced by 12-O-tetradecanoylphorbol-13- acetate as a possible anti-tumor promoting mechanism Mutat. Res. 2003 542 1-2 89 97
    • (2003) Mutat. Res. , vol.542 , Issue.12 , pp. 89-97
    • Park, K.K.1    Park, J.H.2    Jung, Y.J.3    Chung, W.Y.4
  • 4
    • 1942510594 scopus 로고    scopus 로고
    • Effect of chlorophyllin against oxidative stress in splenic lymphocytes in vitro and in vivo
    • S. S. Kumar B. Shankar K. B. Sainis Effect of chlorophyllin against oxidative stress in splenic lymphocytes in vitro and in vivo Biochim. Biophys. Acta 2004 1672 2 100 111
    • (2004) Biochim. Biophys. Acta , vol.1672 , Issue.2 , pp. 100-111
    • Kumar, S.S.1    Shankar, B.2    Sainis, K.B.3
  • 5
    • 70249142203 scopus 로고    scopus 로고
    • Et al., E2F4 and ribonucleotide reductase mediate S-phase arrest in colon cancer cells treated with chlorophyllin
    • K. Chimploy G. D. Diaz Q. Li et al., E2F4 and ribonucleotide reductase mediate S-phase arrest in colon cancer cells treated with chlorophyllin Int. J. Cancer 2009 125 9 2086 2094
    • (2009) Int. J. Cancer , vol.125 , Issue.9 , pp. 2086-2094
    • Chimploy, K.1    Diaz, G.D.2    Li, Q.3
  • 6
    • 0028908940 scopus 로고
    • Dietary chlorophyllin is a potent inhibitor of aflatoxin B1 hepatocarcinogenesis in rainbow trout
    • V. Breinholt J. Hendricks C. Pereira D. Arbogast G. Bailey Dietary chlorophyllin is a potent inhibitor of aflatoxin B1 hepatocarcinogenesis in rainbow trout Cancer Res. 1995 55 1 57 62
    • (1995) Cancer Res. , vol.55 , Issue.1 , pp. 57-62
    • Breinholt, V.1    Hendricks, J.2    Pereira, C.3    Arbogast, D.4    Bailey, G.5
  • 7
    • 0020031953 scopus 로고
    • Experimental and clinical studies concerning the influence of natural substances on the crystallization of calcium oxalate
    • W. Berg C. Bother H. J. Schneider Experimental and clinical studies concerning the influence of natural substances on the crystallization of calcium oxalate Urology 1982 21 52 58
    • (1982) Urology , vol.21 , pp. 52-58
    • Berg, W.1    Bother, C.2    Schneider, H.J.3
  • 8
    • 0018921340 scopus 로고
    • Use of chlorophyllin in the care of geriatric patients
    • R. W. Young J. S. Bergei Jr Use of chlorophyllin in the care of geriatric patients J. Am. Geriatr. Soc. 1980 28 46 47
    • (1980) J. Am. Geriatr. Soc. , vol.28 , pp. 46-47
    • Young, R.W.1    Bergei, Jr.J.S.2
  • 9
    • 0026659125 scopus 로고
    • Inhibition of 2-amino-3-methylimidazo4,5-/quinoline (IQ)-DNA binding to chlorophyllin: Studies of enzyme inhibition and molecular complex formation
    • R. H. Dashwood J. Guo Inhibition of 2-amino-3-methylimidazo4,5-/quinoline (IQ)-DNA binding to chlorophyllin: studies of enzyme inhibition and molecular complex formation Carcinogenesis 1992 13 1121 1126
    • (1992) Carcinogenesis , vol.13 , pp. 1121-1126
    • Dashwood, R.H.1    Guo, J.2
  • 10
    • 0028266803 scopus 로고
    • Inhibition of 2-amino-3-methylimidazo4,5-/rquinoline (IQ)-DNA binding in rats given chlorophyllin: Dose-response and time-course studies in the liver and colon
    • D. Guo R. Dashwood Inhibition of 2-amino-3-methylimidazo4,5-/rquinoline (IQ)-DNA binding in rats given chlorophyllin: dose-response and time-course studies in the liver and colon Carcinogenesis 1994 15 763 766
    • (1994) Carcinogenesis , vol.15 , pp. 763-766
    • Guo, D.1    Dashwood, R.2
  • 11
    • 0029064349 scopus 로고
    • Non-specific inhibition of cytochrome P450 activities by chlorophyllin in human and rat liver microsomes
    • C. H. Yun H. G. Jeong J. W. Jhoun F. P. Guengerich Non-specific inhibition of cytochrome P450 activities by chlorophyllin in human and rat liver microsomes Carcinogenesis 1995 16 1437 1440
    • (1995) Carcinogenesis , vol.16 , pp. 1437-1440
    • Yun, C.H.1    Jeong, H.G.2    Jhoun, J.W.3    Guengerich, F.P.4
  • 12
    • 0034868043 scopus 로고    scopus 로고
    • Selective analysis of phosphopeptide within a protein mixture by chemical modification, reversible biotinylation and mass spectrometry
    • M. Adamczyk J. C. Gebler J. Wu Selective analysis of phosphopeptide within a protein mixture by chemical modification, reversible biotinylation and mass spectrometry Rapid Commun. Mass Spectrom. 2001 15 1481
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 1481
    • Adamczyk, M.1    Gebler, J.C.2    Wu, J.3
  • 14
    • 0037387175 scopus 로고    scopus 로고
    • Multi-component immunoaffinity subtraction chromatography: An innovative step towards a comprehensive survey of the human plasma proteome
    • R. Pieper Q. Su C. L. Gatlin S. T. Huang N. L. Anderson S. Steiner Multi-component immunoaffinity subtraction chromatography: an innovative step towards a comprehensive survey of the human plasma proteome Proteomics 2003 3 422 432
    • (2003) Proteomics , vol.3 , pp. 422-432
    • Pieper, R.1    Su, Q.2    Gatlin, C.L.3    Huang, S.T.4    Anderson, N.L.5    Steiner, S.6
  • 17
    • 0034855204 scopus 로고    scopus 로고
    • Prefractionation of protein samples for proteome analysis using reversed-phase high-performance liquid chromatography
    • V. Badock U. Steinhusen K. Bommert A. Otto Prefractionation of protein samples for proteome analysis using reversed-phase high-performance liquid chromatography Electrophoresis 2001 22 2856
    • (2001) Electrophoresis , vol.22 , pp. 2856
    • Badock, V.1    Steinhusen, U.2    Bommert, K.3    Otto, A.4
  • 18
    • 0347134696 scopus 로고    scopus 로고
    • Fluorescent two-dimensional difference gel electrophoresis and mass spectrometry identify age-related protein expression differences for the primary visual cortex of kitten and adult cat
    • G. V. Bergh S. Clerens F. Vandesande L. Arckens Fluorescent two-dimensional difference gel electrophoresis and mass spectrometry identify age-related protein expression differences for the primary visual cortex of kitten and adult cat Electrophoresis 2003 24 1471
    • (2003) Electrophoresis , vol.24 , pp. 1471
    • Bergh, G.V.1    Clerens, S.2    Vandesande, F.3    Arckens, L.4
  • 20
    • 0026786238 scopus 로고
    • The human hepatoma Hep 3B cell line as an experimental model in the study of the long-term regulation of acute-phase proteins by cytokines
    • M. Hiron M. Daveau P. Arnaud J. Bauer J. P. Lebreton The human hepatoma Hep 3B cell line as an experimental model in the study of the long-term regulation of acute-phase proteins by cytokines J. Biochem. 1992 287 255 259
    • (1992) J. Biochem. , vol.287 , pp. 255-259
    • Hiron, M.1    Daveau, M.2    Arnaud, P.3    Bauer, J.4    Lebreton, J.P.5
  • 21
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • T. Mosmann Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays J. Immunol. Methods 1983 65 55 63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 22
    • 0022445670 scopus 로고
    • Rapid colorimetric assay for cell growth and survival
    • F. Denizot R. Lang Rapid colorimetric assay for cell growth and survival J. Immunol. Methods 1986 89 271 277
    • (1986) J. Immunol. Methods , vol.89 , pp. 271-277
    • Denizot, F.1    Lang, R.2
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M. Bradford 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.1
  • 24
    • 0028219162 scopus 로고
    • A simple modification of Blum's silver stain method allows for 30 minute detection of proteins in polyacrylamide gels
    • M. V. Nesterenko M. Tilley S. J. Upton A simple modification of Blum's silver stain method allows for 30 minute detection of proteins in polyacrylamide gels J. Biochem. Biophys. Methods 1994 28 239 242
    • (1994) J. Biochem. Biophys. Methods , vol.28 , pp. 239-242
    • Nesterenko, M.V.1    Tilley, M.2    Upton, S.J.3
  • 26
    • 79251629982 scopus 로고    scopus 로고
    • The antioxidant protein peroxiredoxin 4 is epigenetically down-regulated in acute promyelocytic leukemia
    • 10.1371/journal.pone.0016340
    • K. K. Palande R. Beekman L. E. van der Meeren1 H. B. Beverloo P. Valk I. P. Touw The antioxidant protein peroxiredoxin 4 is epigenetically down-regulated in acute promyelocytic leukemia PLoS One 2011 6 1 e16340 10.1371/journal.pone. 0016340
    • (2011) PLoS One , vol.6 , Issue.1 , pp. 16340
    • Palande, K.K.1    Beekman, R.2    Van Der Meeren, L.E.3    Beverloo, H.B.4    Valk, P.5    Touw, I.P.6
  • 28
    • 0023301988 scopus 로고
    • Molecular cloning of cDNA coding for rat proliferating cell nuclear antigen (PCNA)/cyclin
    • K. Matsumoto T. Moriuchi T. Koji P. K. Nakane Molecular cloning of cDNA coding for rat proliferating cell nuclear antigen (PCNA)/cyclin EMBO J. 1987 6 3 637 642
    • (1987) EMBO J. , vol.6 , Issue.3 , pp. 637-642
    • Matsumoto, K.1    Moriuchi, T.2    Koji, T.3    Nakane, P.K.4
  • 29
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • G. D. Bowman M. O'Donnell J. Kuriyan Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex Nature 2004 429 6993 724 730
    • (2004) Nature , vol.429 , Issue.6993 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 30
    • 0026072875 scopus 로고
    • Regulation of expression and intracellular distribution of calreticulin: A major calcium binding protein of nonmuscle cells
    • M. Opas E. Dziak L. Fliegel M. Michalak Regulation of expression and intracellular distribution of calreticulin: a major calcium binding protein of nonmuscle cells J. Cell. Physiol. 1991 149 160 171
    • (1991) J. Cell. Physiol. , vol.149 , pp. 160-171
    • Opas, M.1    Dziak, E.2    Fliegel, L.3    Michalak, M.4
  • 31
    • 0030783012 scopus 로고    scopus 로고
    • Stathmin: A tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules
    • L. Jourdain P. Curmi A. Sobel D. Pantaloni M. F. Carlier Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules Biochemistry 1997 36 10817 10821
    • (1997) Biochemistry , vol.36 , pp. 10817-10821
    • Jourdain, L.1    Curmi, P.2    Sobel, A.3    Pantaloni, D.4    Carlier, M.F.5
  • 32
    • 0036468982 scopus 로고    scopus 로고
    • The oncoprotein 18/stathmin family of microtubule destabilizers
    • L. Cassimeris The oncoprotein 18/stathmin family of microtubule destabilizers Curr. Opin. Cell Biol. 2002 14 1 18 24
    • (2002) Curr. Opin. Cell Biol. , vol.14 , Issue.1 , pp. 18-24
    • Cassimeris, L.1
  • 33
    • 0033514354 scopus 로고    scopus 로고
    • Conformational flexibility of a ubiquitin conjugation enzyme (E2)
    • Q. Liu Y. C. Yuan B. Shen D. J. Chen Y. Chen Conformational flexibility of a ubiquitin conjugation enzyme (E2) Biochemistry 1999 38 5 1415 1425
    • (1999) Biochemistry , vol.38 , Issue.5 , pp. 1415-1425
    • Liu, Q.1    Yuan, Y.C.2    Shen, B.3    Chen, D.J.4    Chen, Y.5
  • 34
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • M. H. Glickman A. Ciechanover The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction Physiol. Rev. 2002 82 2373 2428
    • (2002) Physiol. Rev. , vol.82 , pp. 2373-2428
    • Glickman, M.H.1    Ciechanover, A.2
  • 35
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • A. M. Weissman Themes and variations on ubiquitylation Nat. Rev. Mol. Cell Biol. 2001 2 169 178
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 37
    • 8544232810 scopus 로고    scopus 로고
    • TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway
    • N. Amzallag B. J. Passer D. Allanic E. Segura C. Théry B. Goud R. Amson A. Telerman TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway J. Biochem. 2004 279 46104 46112
    • (2004) J. Biochem. , vol.279 , pp. 46104-46112
    • Amzallag, N.1    Passer, B.J.2    Allanic, D.3    Segura, E.4    Théry, C.5    Goud, B.6    Amson, R.7    Telerman, A.8
  • 38
    • 4544255170 scopus 로고    scopus 로고
    • Cell surface expression of the stress response chaperone GRP78 enables tumor targeting by circulating ligands
    • M. A. Arap J. Lahdenranta P. J. Mintz A. Hajitou1 Á. S. Sarkis W. Arap R. Pasqualini Cell surface expression of the stress response chaperone GRP78 enables tumor targeting by circulating ligands Cancer Cell 2004 6 3 275 284
    • (2004) Cancer Cell , vol.6 , Issue.3 , pp. 275-284
    • Arap, M.A.1    Lahdenranta, J.2    Mintz, P.J.3    Hajitou, A.4    Sarkis, Á.S.5    Arap, W.6    Pasqualini, R.7
  • 39
    • 2942755868 scopus 로고    scopus 로고
    • Signaling the unfolded protein response from the endoplasmic reticulum
    • K. Zhang R. J. Kaufman Signaling the unfolded protein response from the endoplasmic reticulum J. Biol. Chem. 2004 279 25 25935 25938
    • (2004) J. Biol. Chem. , vol.279 , Issue.25 , pp. 25935-25938
    • Zhang, K.1    Kaufman, R.J.2
  • 40
    • 34447558236 scopus 로고    scopus 로고
    • ER chaperones in mammalian development and human diseases
    • M. Ni A. S. Lee ER chaperones in mammalian development and human diseases FEBS Lett. 2007 581 19 3641 3651
    • (2007) FEBS Lett. , vol.581 , Issue.19 , pp. 3641-3651
    • Ni, M.1    Lee, A.S.2


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