메뉴 건너뛰기




Volumn 462, Issue 2, 2014, Pages 303-314

Potent inhibition of macrophage migration inhibitory factor (MIF) by myeloperoxidase-dependent oxidation of epicatechins

Author keywords

Dopachrome tautomerase; Epicatechin; Inflammation; Macrophage migration inhibitory factor (MIF); Myeloperoxidase (MPO)

Indexed keywords

ANTI-INFLAMMATORY AGENTS; CATECHIN; COMPUTER SIMULATION; HUMANS; HYDROGEN PEROXIDE; ISOMERISM; MACROPHAGE MIGRATION-INHIBITORY FACTORS; MODELS, MOLECULAR; OXIDATION-REDUCTION; PERIODIC ACID; PEROXIDASE; RECOMBINANT PROTEINS;

EID: 84905906541     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20140612     Document Type: Article
Times cited : (26)

References (80)
  • 1
    • 0013923944 scopus 로고
    • Delayed hypersensitivity in vitro: Its mediation by cell-free substances formed by lymphoid cell-antigen interaction
    • David, J. R. (1966) Delayed hypersensitivity in vitro: its mediation by cell-free substances formed by lymphoid cell-antigen interaction. Proc. Natl. Acad. Sci. U.S.A. 56, 72-77
    • (1966) Proc. Natl. Acad. Sci. U.S.A. , vol.56 , pp. 72-77
    • David, J.R.1
  • 2
    • 0013933261 scopus 로고
    • Mechanism of a reaction in vitro associated with delayed-type hypersensitivity
    • Bloom, B. R. and Bennett, B. (1966) Mechanism of a reaction in vitro associated with delayed-type hypersensitivity. Science 153, 80-82
    • (1966) Science , vol.153 , pp. 80-82
    • Bloom, B.R.1    Bennett, B.2
  • 3
    • 0344667547 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor delays apoptosis in neutrophils by inhibiting the mitochondria-dependent death pathway
    • DOI 10.1096/fj.03-0110com
    • Baumann, R., Casaulta, C., Simon, D., Conus, S., Yousefi, S. and Simon, H. U. (2003) Macrophage migration inhibitory factor delays apoptosis in neutrophils by inhibiting the mitochondria-dependent death pathway. FASEB J. 17, 2221-2230 (Pubitemid 37509578)
    • (2003) FASEB Journal , vol.17 , Issue.15 , pp. 2221-2230
    • Baumann, R.1    Casaulta, C.2    Simon, D.3    Conus, S.4    Yousefi, S.5    Simon, H.-U.6
  • 5
    • 33748757667 scopus 로고    scopus 로고
    • Apoptotic neutrophils release macrophage migration inhibitory factor upon stimulation with tumor necrosis factor-α
    • DOI 10.1074/jbc.M604051200
    • Daryadel, A., Grifone, R. F., Simon, H. U. and Yousefi, S. (2006) Apoptotic neutrophils release macrophage migration inhibitory factor upon stimulation with tumor necrosis factor- J. Biol. Chem. 281, 27653-27661 (Pubitemid 44401790)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.37 , pp. 27653-27661
    • Daryadel, A.1    Grifone, R.F.2    Simon, H.-U.3    Yousefi, S.4
  • 7
    • 0028305693 scopus 로고
    • The macrophage is an important and previously unrecognized source of macrophage migration inhibitory factor
    • DOI 10.1084/jem.179.6.1895
    • Calandra, T., Bernhagen, J., Mitchell, R. A. and Bucala, R. (1994) The macrophage is an important and previously unrecognized source of macrophage migration inhibitory factor. J. Exp. Med. 179, 1895-1902 (Pubitemid 24155670)
    • (1994) Journal of Experimental Medicine , vol.179 , Issue.6 , pp. 1895-1902
    • Calandra, T.1    Bernhagen, J.2    Mitchell, R.A.3    Bucala, R.4
  • 8
    • 0142259734 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor: A regulator of innate immunity
    • Calandra, T. and Roger, T. (2003) Macrophage migration inhibitory factor: a regulator of innate immunity. Nat. Rev. Immunol. 3, 791-800 (Pubitemid 37328657)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.10 , pp. 791-800
    • Calandra, T.1    Roger, T.2
  • 11
    • 0035650961 scopus 로고    scopus 로고
    • Glucocorticoid counter regulation: Macrophage migration inhibitory factor as a target for drug discovery
    • DOI 10.1016/S1471-4892(01)00112-6, PII S1471489201001126
    • Lolis, E. (2001) Glucocorticoid counter regulation: macrophage migration inhibitory factor as a target for drug discovery. Curr. Opin. Pharmacol. 1, 662-668 (Pubitemid 33586010)
    • (2001) Current Opinion in Pharmacology , vol.1 , Issue.6 , pp. 662-668
    • Lolis, E.1
  • 12
    • 0033580992 scopus 로고    scopus 로고
    • Sustained mitogen-activated protein kinase (MAPK) and cytoplasmic phospholipase A2 activation by macrophage migration inhibitory factor (MIF). Regulatory role in cell proliferation and glucocorticoid action
    • Mitchell, R. A., Metz, C. N., Peng, T. and Bucala, R. (1999) Sustained mitogen-activated protein kinase (MAPK) and cytoplasmic phospholipase A2 activation by macrophage migration inhibitory factor (MIF). Regulatory role in cell proliferation and glucocorticoid action. J. Biol. Chem. 274, 18100-18106
    • (1999) J. Biol. Chem. , vol.274 , pp. 18100-18106
    • Mitchell, R.A.1    Metz, C.N.2    Peng, T.3    Bucala, R.4
  • 13
    • 33745190762 scopus 로고    scopus 로고
    • MIF: A new cytokine link between rheumatoid arthritis and atherosclerosis
    • Morand, E. F., Leech, M. and Bernhagen, J. (2006) MIF: a new cytokine link between rheumatoid arthritis and atherosclerosis. Nat. Rev. Drug Discov. 5, 399-410
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 399-410
    • Morand, E.F.1    Leech, M.2    Bernhagen, J.3
  • 14
    • 0036259530 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor and the discovery of tautomerase inhibitors
    • DOI 10.2174/1381612023394674
    • Orita, M., Yamamoto, S., Katayama, N. and Fujita, S. (2002) Macrophage migration inhibitory factor and the discovery of tautomerase inhibitors. Curr. Pharm. Des. 8, 1297-1317 (Pubitemid 34594254)
    • (2002) Current Pharmaceutical Design , vol.8 , Issue.14 , pp. 1297-1317
    • Orita, M.1    Yamamoto, S.2    Katayama, N.3    Fujita, S.4
  • 16
    • 38749137749 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor stimulates AMP-activated protein kinase in the ischaemic heart
    • DOI 10.1038/nature06504, PII NATURE06504
    • Miller, E. J., Li, J., Leng, L., McDonald, C., Atsumi, T., Bucala, R. and Young, L. H. (2008) Macrophage migration inhibitory factor stimulates AMP-activated protein kinase in the ischaemic heart. Nature 451, 578-582 (Pubitemid 351186266)
    • (2008) Nature , vol.451 , Issue.7178 , pp. 578-582
    • Miller, E.J.1    Li, J.2    Leng, L.3    McDonald, C.4    Atsumi, T.5    Bucala, R.6    Young, L.H.7
  • 19
    • 0033579884 scopus 로고    scopus 로고
    • Targeted disruption of migration inhibitory factor gene reveals its critical role in sepsis
    • DOI 10.1084/jem.189.2.341
    • Bozza, M., Satoskar, A. R., Lin, G., Lu, B., Humbles, A. A., Gerard, C. and David, J. R. (1999) Targeted disruption of migration inhibitory factor gene reveals its critical role in sepsis. J. Exp. Med. 189, 341-346 (Pubitemid 29063255)
    • (1999) Journal of Experimental Medicine , vol.189 , Issue.2 , pp. 341-346
    • Bozza, M.1    Satoskar, A.R.2    Lin, G.3    Lu, B.4    Humbles, A.A.5    Gerard, C.6    David, J.R.7
  • 22
    • 54749101549 scopus 로고    scopus 로고
    • A novel, macrophage migration inhibitory factor suicide substrate inhibits motility and growth of lung cancer cells
    • Winner, M., Meier, J., Zierow, S., Rendon, B. E., Crichlow, G. V., Riggs, R., Bucala, R., Leng, L., Smith, N., Lolis, E. et al. (2008) A novel, macrophage migration inhibitory factor suicide substrate inhibits motility and growth of lung cancer cells. Cancer Res. 68, 7253-7257
    • (2008) Cancer Res. , vol.68 , pp. 7253-7257
    • Winner, M.1    Meier, J.2    Zierow, S.3    Rendon, B.E.4    Crichlow, G.V.5    Riggs, R.6    Bucala, R.7    Leng, L.8    Smith, N.9    Lolis, E.10
  • 25
  • 26
    • 0343580469 scopus 로고    scopus 로고
    • The macrophage migration inhibitory factor MIF is a phenylpyruvate tautomerase
    • DOI 10.1016/S0014-5793(97)01261-1, PII S0014579397012611
    • Rosengren, E., Aman, P., Thelin, S., Hansson, C., Ahlfors, S., Bjork, P., Jacobsson, L. and Rorsman, H. (1997) The macrophage migration inhibitory factor MIF is a phenylpyruvate tautomerase. FEBS Lett. 417, 85-88 (Pubitemid 27490478)
    • (1997) FEBS Letters , vol.417 , Issue.1 , pp. 85-88
    • Rosengren, E.1    Aman, P.2    Thelin, S.3    Hansson, C.4    Ahlfors, S.5    Bjork, P.6    Jacobsson, L.7    Rorsman, H.8
  • 27
    • 0030663805 scopus 로고    scopus 로고
    • Biochemical and mutational investigations of the enzymatic activity of macrophage migration inhibitory factor
    • DOI 10.1021/bi971153a
    • Bendrat, K., Al-Abed, Y., Callaway, D. J., Peng, T., Calandra, T., Metz, C. N. and Bucala, R. (1997) Biochemical and mutational investigations of the enzymatic activity of macrophage migration inhibitory factor. Biochemistry 36, 15356-15362 (Pubitemid 27528002)
    • (1997) Biochemistry , vol.36 , Issue.49 , pp. 15356-15362
    • Bendrat, K.1    Al-Abed, Y.2    Callaway, D.J.E.3    Peng, T.4    Calandra, T.5    Metz, C.N.6    Bucala, R.7
  • 28
    • 0032127485 scopus 로고    scopus 로고
    • Direct link between cytokine activity and a catalytic site for macrophage migration inhibitory factor
    • DOI 10.1093/emboj/17.13.3534
    • Swope, M., Sun, H. W., Blake, P. R. and Lolis, E. (1998) Direct link between cytokine activity and a catalytic site for macrophage migration inhibitory factor. EMBO J. 17, 3534-3541 (Pubitemid 28327372)
    • (1998) EMBO Journal , vol.17 , Issue.13 , pp. 3534-3541
    • Swope, M.1    Sun, H.-W.2    Blake, P.R.3    Lolis, E.4
  • 31
    • 63049135766 scopus 로고    scopus 로고
    • A tautomerase-null macrophage migration-inhibitory factor (MIF) gene knock-in mouse model reveals that protein interactions and not enzymatic activity mediate MIF-dependent growth regulation
    • Fingerle-Rowson, G., Kaleswarapu, D. R., Schlander, C., Kabgani, N., Brocks, T., Reinart, N., Busch, R., Schutz, A., Lue, H., Du, X. et al. (2009) A tautomerase-null macrophage migration-inhibitory factor (MIF) gene knock-in mouse model reveals that protein interactions and not enzymatic activity mediate MIF-dependent growth regulation. Mol. Cell. Biol. 29, 1922-1932
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1922-1932
    • Fingerle-Rowson, G.1    Kaleswarapu, D.R.2    Schlander, C.3    Kabgani, N.4    Brocks, T.5    Reinart, N.6    Busch, R.7    Schutz, A.8    Lue, H.9    Du, X.10
  • 32
    • 0037067777 scopus 로고    scopus 로고
    • The tautomerase active site of macrophage migration inhibitory factor is a potential target for discovery of novel anti-inflammatory agents
    • DOI 10.1074/jbc.M203220200
    • Lubetsky, J. B., Dios, A., Han, J., Aljabari, B., Ruzsicska, B., Mitchell, R., Lolis, E. and Al-Abed, Y. (2002) The tautomerase active site of macrophage migration inhibitory factor is a potential target for discovery of novel anti-inflammatory agents. J. Biol. Chem. 277, 24976-24982 (Pubitemid 34951799)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 24976-24982
    • Lubetsky, J.B.1    Dios, A.2    Han, J.3    Aljabari, B.4    Ruzsicska, B.5    Mitchell, R.6    Lolis, E.7    Al-Abed, Y.8
  • 35
    • 70450248452 scopus 로고    scopus 로고
    • Direct modification of the proinflammatory cytokine macrophage migration inhibitory factor by dietary isothiocyanates
    • Brown, K. K., Blaikie, F. H., Smith, R. A., Tyndall, J. D., Lue, H., Bernhagen, J., Winterbourn, C. C. and Hampton, M. B. (2009) Direct modification of the proinflammatory cytokine macrophage migration inhibitory factor by dietary isothiocyanates. J. Biol. Chem. 284, 32425-32433
    • (2009) J. Biol. Chem. , vol.284 , pp. 32425-32433
    • Brown, K.K.1    Blaikie, F.H.2    Smith, R.A.3    Tyndall, J.D.4    Lue, H.5    Bernhagen, J.6    Winterbourn, C.C.7    Hampton, M.B.8
  • 36
    • 38949131470 scopus 로고    scopus 로고
    • Flavan-3-ols: Nature, occurrence and biological activity
    • DOI 10.1002/mnfr.200700137
    • Aron, P. M. and Kennedy, J. A. (2008) Flavan-3-ols: nature, occurrence and biological activity. Mol. Nutr. Food. Res. 52, 79-104 (Pubitemid 351211804)
    • (2008) Molecular Nutrition and Food Research , vol.52 , Issue.1 , pp. 79-104
    • Aron, P.M.1    Kennedy, J.A.2
  • 38
    • 37049042562 scopus 로고
    • Periodate oxidation of 1,2-diols, diketones, and hydroxy-ketones: The use of oxygen-18 as a tracer
    • Bunton, C. A. and Shiner, V. J. (1960) Periodate oxidation of 1,2-diols, diketones, and hydroxy-ketones: the use of oxygen-18 as a tracer. J. Chem. Soc. 1593-1598
    • (1960) J. Chem. Soc. , pp. 1593-1598
    • Bunton, C.A.1    Shiner, V.J.2
  • 40
    • 0026701776 scopus 로고
    • Oxidation of hydroquinone by myeloperoxidase. Mechanism of stimulation by benzoquinone
    • Kettle, A. J. and Winterbourn, C. C. (1992) Oxidation of hydroquinone by myeloperoxidase. Mechanism of stimulation by benzoquinone. J. Biol. Chem. 267, 8319-8324
    • (1992) J. Biol. Chem. , vol.267 , pp. 8319-8324
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 41
    • 36248932605 scopus 로고    scopus 로고
    • Myricitrin as a substrate and inhibitor of myeloperoxidase: Implications for the pharmacological effects of flavonoids
    • DOI 10.1016/j.freeradbiomed.2007.09.017, PII S0891584907006521
    • Meotti, F. C., Senthilmohan, R., Harwood, D. T., Missau, F. C., Pizzolatti, M. G. and Kettle, A. J. (2008) Myricitrin as a substrate and inhibitor of myeloperoxidase: implications for the pharmacological effects of flavonoids. Free Radic. Biol. Med. 44, 109-120 (Pubitemid 350138636)
    • (2008) Free Radical Biology and Medicine , vol.44 , Issue.1 , pp. 109-120
    • Meotti, F.C.1    Senthilmohan, R.2    Harwood, D.T.3    Missau, F.C.4    Pizzolatti, M.G.5    Kettle, A.J.6
  • 45
    • 0030915481 scopus 로고    scopus 로고
    • Myeloperoxidase: A key regulator of neutrophil oxidant product
    • Kettle, A. J. and Winterbourn, C. C. (1997) Myeloperoxidase: a key regulator of neutrophil oxidant production. Redox Rep. 3, 3-15 (Pubitemid 27199160)
    • (1997) Redox Report , vol.3 , Issue.1 , pp. 3-15
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 46
    • 0030660227 scopus 로고    scopus 로고
    • Thiocyanate and chloride as competing substrates for myeloperoxidase
    • van Dalen, C. J., Whitehouse, M. W., Winterbourn, C. C. and Kettle, A. J. (1997) Thiocyanate and chloride as competing substrates for myeloperoxidase. Biochem. J. 327, 487-492 (Pubitemid 27477827)
    • (1997) Biochemical Journal , vol.327 , Issue.2 , pp. 487-492
    • Van Dalen, C.J.1    Whitehouse, M.W.2    Winterbourn, C.C.3    Kettle, A.J.4
  • 48
    • 0029557684 scopus 로고
    • Kinetics of oxidation of tyrosine and dityrosine by myeloperoxidase compounds i and II. Implications for lipoprotein peroxidation studies
    • Marquez, L. A. and Dunford, H. B. (1995) Kinetics of oxidation of tyrosine and dityrosine by myeloperoxidase compounds I and II. Implications for lipoprotein peroxidation studies. J. Biol. Chem. 270, 30434-30440
    • (1995) J. Biol. Chem. , vol.270 , pp. 30434-30440
    • Marquez, L.A.1    Dunford, H.B.2
  • 49
    • 0033030493 scopus 로고    scopus 로고
    • Kinetics of oxidation of aliphatic and aromatic thiols by myeloperoxidase compounds I and II
    • DOI 10.1016/S0014-5793(98)01727-X, PII S001457939801727X
    • Burner, U., Jantschko, W. and Obinger, C. (1999) Kinetics of oxidation of aliphatic and aromatic thiols by myeloperoxidase compounds I and II. FEBS Lett. 443, 290-296 (Pubitemid 29080813)
    • (1999) FEBS Letters , vol.443 , Issue.3 , pp. 290-296
    • Burner, U.1    Jantschko, W.2    Obinger, C.3
  • 51
    • 0036478818 scopus 로고    scopus 로고
    • Redox intermediates of plant and mammalian peroxidases: A comparative transient-kinetic study of their reactivity toward indole derivatives
    • DOI 10.1006/abbi.2001.2674
    • Jantschko, W., Furtmuller, P. G., Allegra, M., Livrea, M. A., Jakopitsch, C., Regelsberger, G. and Obinger, C. (2002) Redox intermediates of plant and mammalian peroxidases: a comparative transient-kinetic study of their reactivity toward indole derivatives. Arch. Biochem. Biophys. 398, 12-22 (Pubitemid 34848320)
    • (2002) Archives of Biochemistry and Biophysics , vol.398 , Issue.1 , pp. 12-22
    • Jantschko, W.1    Furtmuller, P.G.2    Allegra, M.3    Livrea, M.A.4    Jakopitsch, C.5    Regelsberger, G.6    Obinger, C.7
  • 53
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • Beers, Jr, R. F. and Sizer, I. W. (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195, 133-140
    • (1952) J. Biol. Chem. , vol.195 , pp. 133-140
    • Beers Jr., R.F.1    Sizer, I.W.2
  • 54
    • 0014958437 scopus 로고
    • Myeloperoxidase of leukocyte of normal blood. 1. Reaction of myeloperoxidase with hydrogen peroxide
    • Odajima, T. and Yamazaki, I. (1970) Myeloperoxidase of leukocyte of normal blood. 1. Reaction of myeloperoxidase with hydrogen peroxide. Biochim. Biophys. Acta 206, 71-77
    • (1970) Biochim. Biophys. Acta , vol.206 , pp. 71-77
    • Odajima, T.1    Yamazaki, I.2
  • 55
    • 0025833659 scopus 로고
    • Specificity of dopachrome tautomerase and inhibition by carboxylated indoles. Considerations on the enzyme active site
    • Aroca, P., Solano, F., Garcia-Borron, J. C. and Lozano, J. A. (1991) Specificity of dopachrome tautomerase and inhibition by carboxylated indoles. Considerations on the enzyme active site. Biochem. J. 277, 393-397
    • (1991) Biochem. J. , vol.277 , pp. 393-397
    • Aroca, P.1    Solano, F.2    Garcia-Borron, J.C.3    Lozano, J.A.4
  • 56
    • 0017240322 scopus 로고
    • Studies on the chlorinating activity of myeloperoxidase
    • Harrison, J. E. and Schultz, J. (1976) Studies on the chlorinating activity of myeloperoxidase. J. Biol. Chem. 251, 1371-1374
    • (1976) J. Biol. Chem. , vol.251 , pp. 1371-1374
    • Harrison, J.E.1    Schultz, J.2
  • 57
    • 0033652986 scopus 로고    scopus 로고
    • Characterization of methylation site of monomethylflavan-3-ols by liquid chromatography/electrospray ionization tandem mass spectrometry
    • Cren-Olive, C., Deprez, S., Lebrun, S., Coddeville, B. and Rolando, C. (2000) Characterization of methylation site of monomethylflavan-3-ols by liquid chromatography/electrospray ionization tandem mass spectrometry. Rapid Commun. Mass Spectrom. 14, 2312-2319
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 2312-2319
    • Cren-Olive, C.1    Deprez, S.2    Lebrun, S.3    Coddeville, B.4    Rolando, C.5
  • 60
    • 72449125795 scopus 로고    scopus 로고
    • Serotonin as a physiological substrate for myeloperoxidase and its superoxide-dependent oxidation to cytotoxic tryptamine-4,5-dione
    • Ximenes, V. F., Maghzal, G. J., Turner, R., Kato, Y., Winterbourn, C. C. and Kettle, A. J. (2010) Serotonin as a physiological substrate for myeloperoxidase and its superoxide-dependent oxidation to cytotoxic tryptamine-4,5-dione. Biochem. J. 425, 285-293
    • (2010) Biochem. J. , vol.425 , pp. 285-293
    • Ximenes, V.F.1    Maghzal, G.J.2    Turner, R.3    Kato, Y.4    Winterbourn, C.C.5    Kettle, A.J.6
  • 61
    • 0025240884 scopus 로고
    • Kinetic studies on the reaction of compound II of myeloperoxidase with ascorbic acid. Role of ascorbic acid in myeloperoxidase function
    • Marquez, L. A., Dunford, H. B. and Van Wart, H. (1990) Kinetic studies on the reaction of compound II of myeloperoxidase with ascorbic acid. Role of ascorbic acid in myeloperoxidase function. J. Biol. Chem. 265, 5666-5670
    • (1990) J. Biol. Chem. , vol.265 , pp. 5666-5670
    • Marquez, L.A.1    Dunford, H.B.2    Van Wart, H.3
  • 63
    • 84859010162 scopus 로고    scopus 로고
    • Structurally related (-)-epicatechin metabolites in humans: Assessment using de novo chemically synthesized authentic standards
    • Ottaviani, J. I., Momma, T. Y., Kuhnle, G. K., Keen, C. L. and Schroeter, H. (2012) Structurally related (-)-epicatechin metabolites in humans: assessment using de novo chemically synthesized authentic standards. Free Radic. Biol. Med. 52, 1403-1412
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 1403-1412
    • Ottaviani, J.I.1    Momma, T.Y.2    Kuhnle, G.K.3    Keen, C.L.4    Schroeter, H.5
  • 64
    • 0033867415 scopus 로고    scopus 로고
    • Epicatechin in human plasma: In vivo determination and effect of chocolate consumption on plasma oxidation status
    • Rein, D., Lotito, S., Holt, R. R., Keen, C. L., Schmitz, H. H. and Fraga, C. G. (2000) Epicatechin in human plasma: in vivo determination and effect of chocolate consumption on plasma oxidation status. J. Nutr. 130, 2109S-2114S (Pubitemid 30619391)
    • (2000) Journal of Nutrition , vol.130 , Issue.8 SUPPL.
    • Rein, D.1    Lotito, S.2    Holt, R.R.3    Keen, C.L.4    Schmitz, H.H.5    Fraga, C.G.6
  • 65
  • 67
    • 68449098789 scopus 로고    scopus 로고
    • Overview of the role of macrophage migration inhibitory factor (MIF) in inflammatory bowel disease
    • Nishihira, J. and Mitsuyama, K. (2009) Overview of the role of macrophage migration inhibitory factor (MIF) in inflammatory bowel disease. Curr. Pharm. Des. 15, 2104-2109
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 2104-2109
    • Nishihira, J.1    Mitsuyama, K.2
  • 68
    • 37049077367 scopus 로고
    • Synthesis of condensed tannins. 19. Phenol oxidative coupling of (+)-catechin and (+)-mesquitol: Conformation of Bis-(+)-catechins
    • Young, D. A., Young, E., Roux, D. G., Brandt, E. V. and Ferreira, D. (1987) Synthesis of condensed tannins. 19. Phenol oxidative coupling of (+)-catechin and (+)-mesquitol: conformation of Bis-(+)-catechins. J. Chem. Soc. Perk. T. 1, 2345-2351
    • (1987) J. Chem. Soc. Perk. T. , vol.1 , pp. 2345-2351
    • Young, D.A.1    Young, E.2    Roux, D.G.3    Brandt, E.V.4    Ferreira, D.5
  • 69
    • 0000513299 scopus 로고
    • Influence of Ph on the enzymatic oxidation of (+)-catechin in model systems
    • Guyot, S., Cheynier, V., Souquet, J. M. and Moutounet, M. (1995) Influence of Ph on the enzymatic oxidation of (+)-catechin in model systems. J. Agric. Food Chem. 43, 2458-2462
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 2458-2462
    • Guyot, S.1    Cheynier, V.2    Souquet, J.M.3    Moutounet, M.4
  • 70
    • 10044220649 scopus 로고    scopus 로고
    • Mechanism-based inactivation of COX-1 by red wine m-hydroquinones: A structure-activity relationship study
    • DOI 10.1021/np0498410
    • Szewczuk, L. M. and Penning, T. M. (2004) Mechanism-based inactivation of COX-1 by red wine m-hydroquinones: a structure-activity relationship study. J. Nat. Prod. 67, 1777-1782 (Pubitemid 39602350)
    • (2004) Journal of Natural Products , vol.67 , Issue.11 , pp. 1777-1782
    • Szewczuk, L.M.1    Penning, T.M.2
  • 72
    • 78650667117 scopus 로고    scopus 로고
    • Covalent binding of tea catechins to protein thiols: The relationship between stability and electrophilic reactivity
    • Mori, T., Ishii, T., Akagawa, M., Nakamura, Y. and Nakayama, T. (2010) Covalent binding of tea catechins to protein thiols: the relationship between stability and electrophilic reactivity. Biosci. Biotechnol. Biochem. 74, 2451-2456
    • (2010) Biosci. Biotechnol. Biochem. , vol.74 , pp. 2451-2456
    • Mori, T.1    Ishii, T.2    Akagawa, M.3    Nakamura, Y.4    Nakayama, T.5
  • 74
    • 78951472957 scopus 로고    scopus 로고
    • Human serum albumin as an antioxidant in the oxidation of (-)-epigallocatechin gallate: Participation of reversible covalent binding for interaction and stabilization
    • Ishii, T., Ichikawa, T., Minoda, K., Kusaka, K., Ito, S., Suzuki, Y., Akagawa, M., Mochizuki, K., Goda, T. and Nakayama, T. (2011) Human serum albumin as an antioxidant in the oxidation of (-)-epigallocatechin gallate: participation of reversible covalent binding for interaction and stabilization. Biosci. Biotechnol. Biochem. 75, 100-106
    • (2011) Biosci. Biotechnol. Biochem. , vol.75 , pp. 100-106
    • Ishii, T.1    Ichikawa, T.2    Minoda, K.3    Kusaka, K.4    Ito, S.5    Suzuki, Y.6    Akagawa, M.7    Mochizuki, K.8    Goda, T.9    Nakayama, T.10
  • 75
    • 52049116999 scopus 로고    scopus 로고
    • Green tea catechins and cardiovascular health: An update
    • Babu, P. V. and Liu, D. (2008) Green tea catechins and cardiovascular health: an update. Curr. Med. Chem. 15, 1840-1850
    • (2008) Curr. Med. Chem. , vol.15 , pp. 1840-1850
    • Babu, P.V.1    Liu, D.2
  • 76
    • 0038121053 scopus 로고    scopus 로고
    • Tea catechins and polyphenols: Health effects, metabolism, and antioxidant functions
    • DOI 10.1080/10408690390826464
    • Higdon, J. V. and Frei, B. (2003) Tea catechins and polyphenols: health effects, metabolism, and antioxidant functions. Crit. Rev. Food Sci. Nutr. 43, 89-143 (Pubitemid 38552312)
    • (2003) Critical Reviews in Food Science and Nutrition , vol.43 , Issue.1 , pp. 89-143
    • Higdon, J.V.1    Frei, B.2
  • 77
    • 34547679576 scopus 로고    scopus 로고
    • Tea polyphenols for health promotion
    • DOI 10.1016/j.lfs.2007.06.011, PII S0024320507004717
    • Khan, N. and Mukhtar, H. (2007) Tea polyphenols for health promotion. Life Sci. 81, 519-533 (Pubitemid 47212236)
    • (2007) Life Sciences , vol.81 , Issue.7 , pp. 519-533
    • Khan, N.1    Mukhtar, H.2
  • 78
    • 84883217899 scopus 로고    scopus 로고
    • Potential benefits of green tea polyphenol EGCG in the prevention and treatment of vascular inflammation in rheumatoid arthritis
    • Riegsecker, S., Wiczynski, D., Kaplan, M. J. and Ahmed, S. (2013) Potential benefits of green tea polyphenol EGCG in the prevention and treatment of vascular inflammation in rheumatoid arthritis. Life Sci. 93, 307-312
    • (2013) Life Sci. , vol.93 , pp. 307-312
    • Riegsecker, S.1    Wiczynski, D.2    Kaplan, M.J.3    Ahmed, S.4
  • 79
    • 24744471877 scopus 로고    scopus 로고
    • Mechanism of action of (-)-epigallocatechin-3-gallate: Auto-oxidation- dependent inactivation of epidermal growth factor receptor and direct effects on growth inhibition in human esophageal cancer KYSE 150 cells
    • DOI 10.1158/0008-5472.CAN-05-0480
    • Hou, Z., Sang, S. M., You, H., Lee, M. J., Hong, J., Chin, K. V. and Yang, C. S. (2005) Mechanism of action of (-)-epigallocatechin-3-gallate: auto-oxidation-dependent inactivation of epidermal growth factor receptor and direct effects on growth inhibition in human esophageal cancer KYSE 150 cells. Cancer Res. 65, 8049-8056 (Pubitemid 41297287)
    • (2005) Cancer Research , vol.65 , Issue.17 , pp. 8049-8056
    • Hou, Z.1    Sang, S.2    You, H.3    Lee, M.-J.4    Hong, J.5    Chin, K.-V.6    Yang, C.S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.