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Volumn 60, Issue 8, 2003, Pages 1760-1763

Green tea epigallocatechin-3-gallate is an inhibitor of mammalian histidine decarboxylase

Author keywords

Epigallocatechin 3 gallate; Green tea; Histamine; Histidine decarboxylase; Pyridoxal 5 phosphate

Indexed keywords

AROMATIC LEVO AMINO ACID DECARBOXYLASE; DOPA DECARBOXYLASE INHIBITOR; ENZYME INHIBITOR; EPIGALLOCATECHIN GALLATE; GREEN TEA EXTRACT; HISTAMINE; HISTIDINE DECARBOXYLASE; HISTIDINE DECARBOXYLASE INHIBITOR; PYRIDOXAL 5 PHOSPHATE; UNCLASSIFIED DRUG;

EID: 0042329688     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-003-3135-3     Document Type: Article
Times cited : (54)

References (22)
  • 1
    • 0022254077 scopus 로고
    • Purification and properties of a pyridoxal 5′-phosphate-dependent histidine decarboxylase from Morganella morganii AM-15
    • Tanase S., Guirard B. M. and Snell E. E. (1985) Purification and properties of a pyridoxal 5′-phosphate-dependent histidine decarboxylase from Morganella morganii AM-15. J. Biol. Chem. 260: 6738-6746
    • (1985) J. Biol. Chem. , vol.260 , pp. 6738-6746
    • Tanase, S.1    Guirard, B.M.2    Snell, E.E.3
  • 2
    • 0021322926 scopus 로고
    • Purification of histidine decarboxylase from the liver of fetal rats and its immunochemical and immunohistochemical characterization
    • Taguchi Y., Watanabe T., Kubota H., Hayashi H. and Wada H. (1984) Purification of histidine decarboxylase from the liver of fetal rats and its immunochemical and immunohistochemical characterization. J. Biol. Chem. 259: 5214-5221
    • (1984) J. Biol. Chem. , vol.259 , pp. 5214-5221
    • Taguchi, Y.1    Watanabe, T.2    Kubota, H.3    Hayashi, H.4    Wada, H.5
  • 5
    • 0036737948 scopus 로고    scopus 로고
    • Spectroscopic analysis of recombinant rat histidine decarboxylase
    • Olmo M. T., Sánchez-Jiménez F., Medina M. A. and Hayashi H. (2002) Spectroscopic analysis of recombinant rat histidine decarboxylase. J. Biochem. 132: 433-439
    • (2002) J. Biochem. , vol.132 , pp. 433-439
    • Olmo, M.T.1    Sánchez-Jiménez, F.2    Medina, M.A.3    Hayashi, H.4
  • 6
    • 0036136731 scopus 로고    scopus 로고
    • 'Angio-prevention': Angiogenesis is a common and key target for cancer chemopreventive agents
    • Tosetti E, Ferrari N., De Flora S. and Albini A. (2002) 'Angio-prevention': angiogenesis is a common and key target for cancer chemopreventive agents. FASEB J. 16: 2-14
    • (2002) FASEB J. , vol.16 , pp. 2-14
    • Tosetti, E.1    Ferrari, N.2    De Flora, S.3    Albini, A.4
  • 7
    • 0034815413 scopus 로고    scopus 로고
    • Green tea polyphenols: Novel irreversible inhibitors of Dopa decarboxylase
    • Bertoldi M., Golsavi M. and Voltattorni C. B. (2001) Green tea polyphenols: novel irreversible inhibitors of Dopa decarboxylase. Biochem. Biophys. Res. Commun. 284: 90-93
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 90-93
    • Bertoldi, M.1    Golsavi, M.2    Voltattorni, C.B.3
  • 8
    • 0036205282 scopus 로고    scopus 로고
    • The specific anti-cancer activity of green tea (-)-epigallocatechin-3-gallate (EGCG)
    • Wang Y. C. and Bachrach U. (2002) The specific anti-cancer activity of green tea (-)-epigallocatechin-3-gallate (EGCG). Amino Acids 22: 131-143
    • (2002) Amino Acids , vol.22 , pp. 131-143
    • Wang, Y.C.1    Bachrach, U.2
  • 9
    • 0029954598 scopus 로고    scopus 로고
    • Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase
    • Engel N., Olmo M. T., Coleman C. S., Medina M. A., Pegg A. E. and Sánchez-Jiménez F. (1996) Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase. Biochem. J. 320: 365-368
    • (1996) Biochem. J. , vol.320 , pp. 365-368
    • Engel, N.1    Olmo, M.T.2    Coleman, C.S.3    Medina, M.A.4    Pegg, A.E.5    Sánchez-Jiménez, F.6
  • 10
    • 0035342272 scopus 로고    scopus 로고
    • Effects of phorbol ester and dexamethasone treatment on histidine decarboxylase and ornithine decarboxylase in basophilic cells
    • Fajardo I., Urdiales J. L., Medina M. A. and Sánchez-Jiménez F (2001) Effects of phorbol ester and dexamethasone treatment on histidine decarboxylase and ornithine decarboxylase in basophilic cells. Biochem. Pharmacol. 61: 1101-1106
    • (2001) Biochem. Pharmacol. , vol.61 , pp. 1101-1106
    • Fajardo, I.1    Urdiales, J.L.2    Medina, M.A.3    Sánchez-Jiménez, F.4
  • 12
    • 0028281750 scopus 로고
    • Multiple evolutionary origins of pyridoxal-5-phosphate-dependent amino acid decarboxylases
    • Sandmeier E., Hale T. I and Christen P. (1994) Multiple evolutionary origins of pyridoxal-5-phosphate-dependent amino acid decarboxylases. Eur. J. Biochem. 221: 997-1002
    • (1994) Eur. J. Biochem. , vol.221 , pp. 997-1002
    • Sandmeier, E.1    Hale, T.I.2    Christen, P.3
  • 13
    • 0025312902 scopus 로고
    • Purification and characterization of L-histidine decarboxylase from mouse mastocytoma P-815 cells
    • Ohmori E., Fukui T., Imanishi N., Yatsunami K. and Ichikawa A. (1990) Purification and characterization of L-histidine decarboxylase from mouse mastocytoma P-815 cells. J. Biochem. 107: 834-839
    • (1990) J. Biochem. , vol.107 , pp. 834-839
    • Ohmori, E.1    Fukui, T.2    Imanishi, N.3    Yatsunami, K.4    Ichikawa, A.5
  • 14
    • 0029090374 scopus 로고
    • Pyridoxal enzymes: Mechanistic diversity and uniformity
    • Hayashi H. (1995) Pyridoxal enzymes: mechanistic diversity and uniformity. J. Biochem. 118: 463-473
    • (1995) J. Biochem. , vol.118 , pp. 463-473
    • Hayashi, H.1
  • 15
    • 0033925366 scopus 로고    scopus 로고
    • Inhibition of xanthine oxidase and suppression of intracellular reactive oxygen species in HL-60 cells by theaflavin-3, 3"-digallate, (-)-epigallocatechin-3-gallate, and propyl gallate
    • Lin J. K., Chen P. C., Ho C. T. and Lin-Shiau S. Y. (2000) Inhibition of xanthine oxidase and suppression of intracellular reactive oxygen species in HL-60 cells by theaflavin-3, 3"-digallate, (-)-epigallocatechin-3-gallate, and propyl gallate. J. Agric. Food. Chem. 48: 2736-2743
    • (2000) J. Agric. Food. Chem. , vol.48 , pp. 2736-2743
    • Lin, J.K.1    Chen, P.C.2    Ho, C.T.3    Lin-Shiau, S.Y.4
  • 16
    • 0034693103 scopus 로고    scopus 로고
    • Antioxidative galloyl esters as enzyme inhibitors of p-hydroxybenzoate hydroxylase
    • Abe I., Kashiwagi K. and Noguchi H. (2000) Antioxidative galloyl esters as enzyme inhibitors of p-hydroxybenzoate hydroxylase. FEBS Lett. 483: 131-134
    • (2000) FEBS Lett. , vol.483 , pp. 131-134
    • Abe, I.1    Kashiwagi, K.2    Noguchi, H.3
  • 19
    • 0025249232 scopus 로고
    • Pyridoxal 5′-phosphate-dependent histidine decarboxylase: Mechanism of inactivation by α-fluoromethylhistidine
    • Bhatacharjee M. E. and Snell E. E. (1990) Pyridoxal 5′-phosphate-dependent histidine decarboxylase: mechanism of inactivation by α-fluoromethylhistidine. J. Biol. Chem. 265: 6664-6668
    • (1990) J. Biol. Chem. , vol.265 , pp. 6664-6668
    • Bhatacharjee, M.E.1    Snell, E.E.2
  • 20
    • 0021166330 scopus 로고
    • Mechanism of inactivation of mammalian L-histidine decarboxylase by (S)-α-fluoromethylhistidine
    • Kubota H., Hayashi H., Watanabe T., Taguchi Y. and Wada H. (1984) Mechanism of inactivation of mammalian L-histidine decarboxylase by (S)-α-fluoromethylhistidine. Biochem. Pharmacol. 33: 983-990
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 983-990
    • Kubota, H.1    Hayashi, H.2    Watanabe, T.3    Taguchi, Y.4    Wada, H.5
  • 21
    • 0037180812 scopus 로고    scopus 로고
    • Points of control in inflammation
    • Nathan C. (2002) Points of control in inflammation. Nature 420: 846-852
    • (2002) Nature , vol.420 , pp. 846-852
    • Nathan, C.1
  • 22
    • 0036779369 scopus 로고    scopus 로고
    • A green tea-derived polyphenol, epigallocatechin-3-gallate, inhibits IkappaB kinase activation and IL-8 gene expression in respiratory epithelium
    • Chen P. C., Wheeler D. S., Malhotra V., Odoms K., Denenberg A. G. and Wong, H. R. (2002) A green tea-derived polyphenol, epigallocatechin-3-gallate, inhibits IkappaB kinase activation and IL-8 gene expression in respiratory epithelium. Inflammation 26: 233-241
    • (2002) Inflammation , vol.26 , pp. 233-241
    • Chen, P.C.1    Wheeler, D.S.2    Malhotra, V.3    Odoms, K.4    Denenberg, A.G.5    Wong, H.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.