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Volumn 42, Issue 9, 2004, Pages 1401-1408

Inhibition of glutathione S-transferases by thonningianin A, isolated from the African medicinal herb, Thonningia sanguinea, in vitro

Author keywords

Antioxidant; Glutathione S transferase; Inhibition; Polyphenol; Thonningia sanguinea; Thonningianin A

Indexed keywords

1 CHLORO 2,4 DINITROBENZENE; 1,2 EPOXY 3 (4 NITROPHENOXY)PROPANE; ALKANE DERIVATIVE; CIBACRON BLUE F3GA; ETACRYNIC ACID; GLUTATHIONE; HEMATIN; PLANT EXTRACT; TANNIN; THONNINGIA SANGUINEA EXTRACT; THONNINGIANIN A; TRANSFERASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 3042747926     PISSN: 02786915     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fct.2004.04.001     Document Type: Article
Times cited : (53)

References (52)
  • 4
    • 0031006947 scopus 로고    scopus 로고
    • Inhibition of human placenta glutathione transferase P1-1 by the antibiotic calvatic acid and its diazocyanide analogue - Evidence for multiple catalytic intermediates
    • Antonini G., Pitari G., Caccuri A.M., Ricci G., Boschi D., Fruttero R., Gasco A., Ascenzi P. Inhibition of human placenta glutathione transferase P1-1 by the antibiotic calvatic acid and its diazocyanide analogue - evidence for multiple catalytic intermediates. European Journal of Biochemistry. 245:1997;663-667
    • (1997) European Journal of Biochemistry , vol.245 , pp. 663-667
    • Antonini, G.1    Pitari, G.2    Caccuri, A.M.3    Ricci, G.4    Boschi, D.5    Fruttero, R.6    Gasco, A.7    Ascenzi, P.8
  • 6
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • Armstrong R.N. Structure, catalytic mechanism, and evolution of the glutathione transferases. Chemical Research in Toxicology. 10:1997;2-18
    • (1997) Chemical Research in Toxicology , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 8
    • 0028078679 scopus 로고
    • Inhibition of rat liver cytosolic glutathione S-transferase by silybin
    • Bartholomaeus A.R., Bolton R., Ahokas J.T. Inhibition of rat liver cytosolic glutathione S-transferase by silybin. Xenobiotica. 24:1994;17-24
    • (1994) Xenobiotica , vol.24 , pp. 17-24
    • Bartholomaeus, A.R.1    Bolton, R.2    Ahokas, J.T.3
  • 9
    • 0029163141 scopus 로고
    • Differential effects of verapamil and quinine on the reversal of doxorubicin resistance in a human leukemia cell line
    • Bennis S., Ichas F., Robert J. Differential effects of verapamil and quinine on the reversal of doxorubicin resistance in a human leukemia cell line. International Journal of Cancer. 62:1995;283-290
    • (1995) International Journal of Cancer , vol.62 , pp. 283-290
    • Bennis, S.1    Ichas, F.2    Robert, J.3
  • 10
    • 0023740342 scopus 로고
    • Formation of toxic metabolites from drugs and other xenobiotics by glutathione conjugation
    • Bladeren van P.J. Formation of toxic metabolites from drugs and other xenobiotics by glutathione conjugation. Trends in Pharmacological Science. 9:1988;295-299
    • (1988) Trends in Pharmacological Science , vol.9 , pp. 295-299
    • Bladeren Van, P.J.1
  • 11
    • 0024561369 scopus 로고
    • The glutathione S-transferase: An update
    • Boyer T.D. The glutathione. S -transferase: an update Hepatology. 9:1989;486-496
    • (1989) Hepatology , vol.9 , pp. 486-496
    • Boyer, T.D.1
  • 13
    • 0036446934 scopus 로고    scopus 로고
    • Glutathione conjugates and their synthetic derivatives as inhibitors of glutathione-dependent enzymes involved in cancer and drug resistance
    • Burg D., Mulder G.J. Glutathione conjugates and their synthetic derivatives as inhibitors of glutathione-dependent enzymes involved in cancer and drug resistance. Drug Metabolism Reviews. 34:2002;821-863
    • (2002) Drug Metabolism Reviews , vol.34 , pp. 821-863
    • Burg, D.1    Mulder, G.J.2
  • 16
    • 0028224013 scopus 로고
    • X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function
    • Dirr H., Reinemer P., Huber R. X-ray crystal structures of cytosolic glutathione. S -transferases. Implications for protein architecture, substrate recognition and catalytic function European Journal of Biochemistry. 220:1994;645-661
    • (1994) European Journal of Biochemistry , vol.220 , pp. 645-661
    • Dirr, H.1    Reinemer, P.2    Huber, R.3
  • 17
    • 0026575011 scopus 로고
    • Insect glutathione S-transferases. Biochemical characteristics of the major forms from houseflies susceptible and resistant to insecticides
    • Fournier D., Bride J.M., Poirie M., Berge J.B., Plapp F.W. Jr. Insect glutathione. S -transferases. Biochemical characteristics of the major forms from houseflies susceptible and resistant to insecticides The Journal Biological Chemistry. 267:1992;1840-1845
    • (1992) The Journal Biological Chemistry , vol.267 , pp. 1840-1845
    • Fournier, D.1    Bride, J.M.2    Poirie, M.3    Berge, J.B.4    Plapp Jr., F.W.5
  • 18
    • 0037652560 scopus 로고    scopus 로고
    • Glutathione S-transferases as emerging therapeutic targets
    • Gate L., Tew K.D. Glutathione S-transferases as emerging therapeutic targets. Expert Opinion on Therapeutic Targets. 5:2001;477-489
    • (2001) Expert Opinion on Therapeutic Targets , vol.5 , pp. 477-489
    • Gate, L.1    Tew, K.D.2
  • 19
    • 0031667813 scopus 로고    scopus 로고
    • Medicinal herb, Thonningia sanguinea protects against aflatoxin B1 acute hepatotoxicity in Fischer 344 rats
    • Gyamfi M.A., Aniya Y. Medicinal herb, Thonningia sanguinea protects against aflatoxin B1 acute hepatotoxicity in Fischer 344 rats. Human and Experimental Toxicology. 17:1998;418-423
    • (1998) Human and Experimental Toxicology , vol.17 , pp. 418-423
    • Gyamfi, M.A.1    Aniya, Y.2
  • 20
    • 0036569892 scopus 로고    scopus 로고
    • Antioxidant properties of Thonningianin A, isolated from the African medicinal herb, Thonningia sanguinea
    • Gyamfi M.A., Aniya Y. Antioxidant properties of Thonningianin A, isolated from the African medicinal herb, Thonningia sanguinea. Biochemical Pharmacology. 63:2002;1725-1737
    • (2002) Biochemical Pharmacology , vol.63 , pp. 1725-1737
    • Gyamfi, M.A.1    Aniya, Y.2
  • 21
    • 20644453312 scopus 로고    scopus 로고
    • Inhibitory effects of the medicinal herb, Thonningia sanguinea, on liver drug metabolizing enzymes of rats
    • Gyamfi M.A., Hokama N., Oppong-Boachie K., Aniya Y. Inhibitory effects of the medicinal herb, Thonningia sanguinea, on liver drug metabolizing enzymes of rats. Human and Experimental Toxicology. 19:2000;623-631
    • (2000) Human and Experimental Toxicology , vol.19 , pp. 623-631
    • Gyamfi, M.A.1    Hokama, N.2    Oppong-Boachie, K.3    Aniya, Y.4
  • 22
    • 0032996245 scopus 로고    scopus 로고
    • Free-radical scavenging action of medicinal herbs from Ghana: Thonningia sanguinea on experimentally-induced liver injuries
    • Gyamfi M.A., Yonamine M., Aniya Y. Free-radical scavenging action of medicinal herbs from Ghana: Thonningia sanguinea on experimentally-induced liver injuries. General Pharmacology. 32:1999;661-667
    • (1999) General Pharmacology , vol.32 , pp. 661-667
    • Gyamfi, M.A.1    Yonamine, M.2    Aniya, Y.3
  • 26
    • 0036701477 scopus 로고    scopus 로고
    • Tocotrienols inhibit human glutathione S-transferase P1-1
    • Haaften van R.I., Haenen G.R., Evelo C.T., Bast A. Tocotrienols inhibit human glutathione. S -transferase P1-1 IUBMB Life. 54:2002;81-84
    • (2002) IUBMB Life , vol.54 , pp. 81-84
    • Haaften Van, R.I.1    Haenen, G.R.2    Evelo, C.T.3    Bast, A.4
  • 27
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig W.H., Pabst M.J., Jakoby W.B. Glutathione. S -transferases. The first enzymatic step in mercapturic acid formation The Journal of Biological Chemistry. 249:1974;7130-7139
    • (1974) The Journal of Biological Chemistry , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 28
    • 0026027666 scopus 로고
    • Sensitization of human melanoma cells to the cytotoxic effect of melphalan by the glutathione transferase inhibitor ethacrynic acid
    • Hansson J., Berhane K., Castro V.M., Jungnelius U., Mannervik B., Ringborg U. Sensitization of human melanoma cells to the cytotoxic effect of melphalan by the glutathione transferase inhibitor ethacrynic acid. Cancer Research. 51:1991;94-98
    • (1991) Cancer Research , vol.51 , pp. 94-98
    • Hansson, J.1    Berhane, K.2    Castro, V.M.3    Jungnelius, U.4    Mannervik, B.5    Ringborg, U.6
  • 29
    • 0015977769 scopus 로고
    • Polyphenol-protein interactions
    • Haslam E. Polyphenol-protein interactions. The Biochemical Journal. 139:1974;285-288
    • (1974) The Biochemical Journal , vol.139 , pp. 285-288
    • Haslam, E.1
  • 30
    • 0030515619 scopus 로고    scopus 로고
    • Natural polyphenols (vegetable tannins) as drugs: Possible mode of action
    • Haslam E. Natural polyphenols (vegetable tannins) as drugs: possible mode of action. Journal of Natural Products. 59:1996;205-215
    • (1996) Journal of Natural Products , vol.59 , pp. 205-215
    • Haslam, E.1
  • 31
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes J.D., Pulford D.J. The glutathione. S -transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance Critical Reviews in Biochemistry and Molecular Biology. 30:1995;445-600
    • (1995) Critical Reviews in Biochemistry and Molecular Biology , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 33
    • 0034813645 scopus 로고    scopus 로고
    • A highly acidic tyrosine 9 and a normally titrating tyrosine 212 contribute to the catalytic mechanism of human glutathione transferase A4-4
    • Hubatsch I., Mannervik B. A highly acidic tyrosine 9 and a normally titrating tyrosine 212 contribute to the catalytic mechanism of human glutathione transferase A4-4. Biochemical and Biophysical Research Communications. 280:2001;878-882
    • (2001) Biochemical and Biophysical Research Communications , vol.280 , pp. 878-882
    • Hubatsch, I.1    Mannervik, B.2
  • 34
    • 0031574268 scopus 로고    scopus 로고
    • Kinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme
    • Jemth P., Mannervik B. Kinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme. Archives Biochemistry and Biophysics. 348:1997;247-254
    • (1997) Archives Biochemistry and Biophysics , vol.348 , pp. 247-254
    • Jemth, P.1    Mannervik, B.2
  • 35
    • 0037081842 scopus 로고    scopus 로고
    • The polymorphic human glutathione transferase T1-1, the most efficient glutathione transferase in the denitrosation and inactivation of the anticancer drug 1,3-bis (2-chloroethyl)-1-nitrosourea
    • Lien S., Larsson A.-k., Mannervik B. The polymorphic human glutathione transferase T1-1, the most efficient glutathione transferase in the denitrosation and inactivation of the anticancer drug 1, 3-bis (2-chloroethyl)-1-nitrosourea. Biochemical Pharmacology. 63:2002;191-197
    • (2002) Biochemical Pharmacology , vol.63 , pp. 191-197
    • Lien, S.1    Larsson, A.-K.2    Mannervik, B.3
  • 38
    • 8044233719 scopus 로고    scopus 로고
    • Immunohistochemical study of alpha, mu and pi class glutathione S-transferase expression in malignant melanoma. MMM Group. Multidisciplinary Malignant Melanoma Group
    • Moral A., Palou J., Lafuente A., Molina R., Piulachs J., Castel T., Trias M. Immunohistochemical study of alpha, mu and pi class glutathione S-transferase expression in malignant melanoma. MMM Group. Multidisciplinary Malignant Melanoma Group. British Journal of Dermatology. 136:1997;345-350
    • (1997) British Journal of Dermatology , vol.136 , pp. 345-350
    • Moral, A.1    Palou, J.2    Lafuente, A.3    Molina, R.4    Piulachs, J.5    Castel, T.6    Trias, M.7
  • 40
    • 0032493638 scopus 로고    scopus 로고
    • Coordinated action of glutathione S-transferases (GSTs) and multidrug resistance protein 1 (MRP1) in antineoplastic drug detoxification. Mechanism of GST A1-1- and associated resistance to chlorambucil in MCF7 breast carcinoma cells
    • Morrow C.S., Smitherman P.K., Diah S.K., Schneider E., Townsend A.J. Coordinated action of glutathione S-transferases (GSTs) and multidrug resistance protein 1 (MRP1) in antineoplastic drug detoxification. Mechanism of GST A1-1- and associated resistance to chlorambucil in MCF7 breast carcinoma cells. The Journal of Biological Chemistry. 273:1998;20114-20120
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 20114-20120
    • Morrow, C.S.1    Smitherman, P.K.2    Diah, S.K.3    Schneider, E.4    Townsend, A.J.5
  • 41
    • 0037050733 scopus 로고    scopus 로고
    • Inhibition of glutathione S-transferases by antimalarial drugs possible implications for circumventing anticancer drug resistance
    • Mukanganyama S., Widersten M., Naik Y.S., Mannervik B., Hasler J.A. Inhibition of glutathione S-transferases by antimalarial drugs possible implications for circumventing anticancer drug resistance. International Journal of Cancer. 97:2002;700-705
    • (2002) International Journal of Cancer , vol.97 , pp. 700-705
    • Mukanganyama, S.1    Widersten, M.2    Naik, Y.S.3    Mannervik, B.4    Hasler, J.A.5
  • 44
  • 45
    • 0024490605 scopus 로고
    • Glutathione S-transferases as markers of preneoplasia and neoplasia
    • Sato K. Glutathione. S -transferases as markers of preneoplasia and neoplasia Advances in Cancer Research. 52:1989;205-247
    • (1989) Advances in Cancer Research , vol.52 , pp. 205-247
    • Sato, K.1
  • 46
    • 0030778937 scopus 로고    scopus 로고
    • Evidence that human class theta glutathione S-transferase T1-1 can catalyse the activation of dichloromethane, a liver and lung carcinogen in the mouse. Comparison of the tissue distribution of GSTT1-1 with that of classes alpha, mu and pi GST in human
    • Sherratt P.J., Pulford D.J., Harrison D.J., Green T., Hayes J.D. Evidence that human class theta glutathione S-transferase T1-1 can catalyse the activation of dichloromethane, a liver and lung carcinogen in the mouse. Comparison of the tissue distribution of GSTT1-1 with that of classes alpha, mu and pi GST in human. The Biochemical Journal. 326:1997;837-846
    • (1997) The Biochemical Journal , vol.326 , pp. 837-846
    • Sherratt, P.J.1    Pulford, D.J.2    Harrison, D.J.3    Green, T.4    Hayes, J.D.5
  • 47
    • 0028106016 scopus 로고
    • Glutathione-associated enzymes in anticancer drug resistance
    • Tew K.D. Glutathione-associated enzymes in anticancer drug resistance. Cancer Research. 54:1994;4313-4320
    • (1994) Cancer Research , vol.54 , pp. 4313-4320
    • Tew, K.D.1
  • 48
    • 0032579563 scopus 로고    scopus 로고
    • The three-dimensional structure of Cys-47-modified mouse liver glutathione S-transferase P1-1. Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the alphaB-310B region
    • Vega M.C., Walsh S.B., Mantle T.J., Coll M. The three-dimensional structure of Cys-47-modified mouse liver glutathione. S -transferase P1-1. Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the alphaB-310B region The Journal of Biological Chemistry. 273:1998;2844-2850
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 2844-2850
    • Vega, M.C.1    Walsh, S.B.2    Mantle, T.J.3    Coll, M.4
  • 49
    • 0028263070 scopus 로고
    • Structure and function of glutathione S-transferases
    • Wilce M.C., Parker M.W. Structure and function of glutathione S-transferases. Biochimica et Biophysical Acta. 1205:1994;1-18
    • (1994) Biochimica et Biophysical Acta , vol.1205 , pp. 1-18
    • Wilce, M.C.1    Parker, M.W.2
  • 52
    • 0028303457 scopus 로고
    • Inhibitory effects of plant polyphenols on rat liver glutathione S-transferases
    • Zhang K., Das N.P. Inhibitory effects of plant polyphenols on rat liver glutathione. S -transferases Biochemical Pharmacology. 47:1994;2063-2068
    • (1994) Biochemical Pharmacology , vol.47 , pp. 2063-2068
    • Zhang, K.1    Das, N.P.2


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