메뉴 건너뛰기




Volumn 93, Issue 2, 2011, Pages 217-226

Oxidative metabolism of the anti-cancer agent mitoxantrone by horseradish, lacto-and lignin peroxidase

Author keywords

Cancer; Mitoxantrone drug metabolism; Novel enzymatic oxidation cascade

Indexed keywords

ANTHRAQUINONE; CARBOXYLIC ACID; DICARBOXYLIC ACID DERIVATIVE; DRUG METABOLITE; HEXAHYDRONAPHTHO [2,3 F] QUINOXALINE 7,12 DIONE; HORSERADISH PEROXIDASE; HYDROGEN PEROXIDE; LACTO PEROXIDASE; LIGNIN PEROXIDASE; LIPID PEROXIDASE; MITOXANTRONE; UNCLASSIFIED DRUG;

EID: 78651338653     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.09.015     Document Type: Article
Times cited : (20)

References (47)
  • 2
  • 3
    • 0031586756 scopus 로고    scopus 로고
    • Neutrophil-mediated activation of mitoxantrone to metabolites which form adducts with DNA
    • C. Panousis, A.J. Kettle, and D.R. Phillips Neutrophil-mediated activation of mitoxantrone to metabolites which form adducts with DNA Cancer Lett. 113 1997 173 178
    • (1997) Cancer Lett. , vol.113 , pp. 173-178
    • Panousis, C.1    Kettle, A.J.2    Phillips, D.R.3
  • 4
    • 0026018422 scopus 로고
    • DNA strand breakage by peroxidase-activated mitoxantrone
    • G. Fisher, and L.H. Patterson DNA strand breakage by peroxidase-activated mitoxantrone J. Pharm. Pharmacol. 43 1991 65 68
    • (1991) J. Pharm. Pharmacol. , vol.43 , pp. 65-68
    • Fisher, G.1    Patterson, L.H.2
  • 7
    • 0023028913 scopus 로고
    • Redox cycling of anthracyclines by cardiac mitochondria
    • J.H. Doroshow, and K.J.A. Davies Redox cycling of anthracyclines by cardiac mitochondria J. Biol. Chem. 261 1986 3066 3074
    • (1986) J. Biol. Chem. , vol.261 , pp. 3066-3074
    • Doroshow, J.H.1    Davies, K.J.A.2
  • 8
    • 0024424289 scopus 로고
    • The role of reductive and oxidative metabolism in the toxicity of mitoxantrone, adriamycin and menadione in human liver-derived HEPG2 hepatoma cells
    • S.J. Duthie, and M.H. Grant The role of reductive and oxidative metabolism in the toxicity of mitoxantrone, adriamycin and menadione in human liver-derived HEPG2 hepatoma cells Br. J. Can. 60 1989 566 571
    • (1989) Br. J. Can. , vol.60 , pp. 566-571
    • Duthie, S.J.1    Grant, M.H.2
  • 9
    • 0028261718 scopus 로고
    • Synthesis and structural elucidation of biliary excreted thioether derivatives of mitoxantrone
    • K. Mewes, J. Blanz, S. Freund, G. Ehninger, and K.P. Zeller Synthesis and structural elucidation of biliary excreted thioether derivatives of mitoxantrone Xenobiotica 24 1994 199 213
    • (1994) Xenobiotica , vol.24 , pp. 199-213
    • Mewes, K.1    Blanz, J.2    Freund, S.3    Ehninger, G.4    Zeller, K.P.5
  • 10
    • 0025261039 scopus 로고
    • Mechanism(s) for the metabolism of mitoxantrone: Electron-spin resonance and electrochemical studies
    • B. Nguyen, and P.L. Gutierrez Mechanism(s) for the metabolism of mitoxantrone: electron-spin resonance and electrochemical studies Chem. Biol. Interactions 74 1990 139 162
    • (1990) Chem. Biol. Interactions , vol.74 , pp. 139-162
    • Nguyen, B.1    Gutierrez, P.L.2
  • 12
    • 0028043893 scopus 로고
    • Oxidative metabolism of mitoxantrone by the human neutrophil enzyme myeloperoxidase
    • C. Panousis, A.J. Kettle, and D.R. Phillips Oxidative metabolism of mitoxantrone by the human neutrophil enzyme myeloperoxidase Biochem. Pharmacol. 48 1994 223 2230
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 223-2230
    • Panousis, C.1    Kettle, A.J.2    Phillips, D.R.3
  • 13
    • 0029557575 scopus 로고
    • Myeloperoxidase oxidises mitoxantrone to metabolites which bind covalently to DNA and RNA
    • C. Panousis, A.J. Kettle, and D.R. Phillips Myeloperoxidase oxidises mitoxantrone to metabolites which bind covalently to DNA and RNA Anti-cancer Drug Des. 10 1995 593 605
    • (1995) Anti-cancer Drug Des. , vol.10 , pp. 593-605
    • Panousis, C.1    Kettle, A.J.2    Phillips, D.R.3
  • 14
    • 0030467995 scopus 로고    scopus 로고
    • Acid-catalyzed oxidation of the anticancer agent mitoxantrone by nitrite ions
    • K.J. Reszka, and C.F. Chignell Acid-catalyzed oxidation of the anticancer agent mitoxantrone by nitrite ions Mol. Pharmacol. 50 1996 1612 1618
    • (1996) Mol. Pharmacol. , vol.50 , pp. 1612-1618
    • Reszka, K.J.1    Chignell, C.F.2
  • 15
    • 0028230140 scopus 로고
    • New aspects on the pharmacokinetics of mitoxantrone and its two major metabolites
    • E. Schleyer, A. Kamischke, C.C. Kaufmann, M. Unterhalt, and W. Hiddemann New aspects on the pharmacokinetics of mitoxantrone and its two major metabolites Leukemia 8 1994 435 440
    • (1994) Leukemia , vol.8 , pp. 435-440
    • Schleyer, E.1    Kamischke, A.2    Kaufmann, C.C.3    Unterhalt, M.4    Hiddemann, W.5
  • 16
    • 0030991136 scopus 로고    scopus 로고
    • Redox pathway leading to the alkylation of DNA by the anthracycline, antitumor drugs adriamycin and daunomycin
    • D.J. Taatjes, G. Gaudiano, K. Resing, and T.H. Koch Redox pathway leading to the alkylation of DNA by the anthracycline, antitumor drugs adriamycin and daunomycin J. Med. Chem. 40 1997 1276 1286
    • (1997) J. Med. Chem. , vol.40 , pp. 1276-1286
    • Taatjes, D.J.1    Gaudiano, G.2    Resing, K.3    Koch, T.H.4
  • 17
    • 21244432233 scopus 로고    scopus 로고
    • Effects of peroxidase substrates on the Amplex red/peroxidase assay: Antioxidant properties of anthracyclines
    • K.J. Reszka, B.A. Wagner, and B.E. Burns Effects of peroxidase substrates on the Amplex red/peroxidase assay: antioxidant properties of anthracyclines Anal. Biochem. 15 2005 327 337
    • (2005) Anal. Biochem. , vol.15 , pp. 327-337
    • Reszka, K.J.1    Wagner, B.A.2    Burns, B.E.3
  • 18
    • 0142152337 scopus 로고    scopus 로고
    • Oxidation of mitoxantrone by lactoperoxidase
    • T.B. Brück, and P.J. Harvey Oxidation of mitoxantrone by lactoperoxidase Biochim. Biophys. Acta 1649 2 2003 154 163
    • (2003) Biochim. Biophys. Acta , vol.1649 , Issue.2 , pp. 154-163
    • Brück, T.B.1    Harvey, P.J.2
  • 19
    • 51849113762 scopus 로고    scopus 로고
    • Intramolecular electron transfer versus substrate oxidation in lactoperoxidase: Investigation of radical intermediates by stopped-flow absorption spectrophotometry and (9-285 GHz) electron paramagnetic resonance spectroscopy
    • A.J. Fielding, R. Singh, B. Boscolo, P.C. Loewen, E.M. Ghibaudi, and A. Ivancich Intramolecular electron transfer versus substrate oxidation in lactoperoxidase: investigation of radical intermediates by stopped-flow absorption spectrophotometry and (9-285 GHz) electron paramagnetic resonance spectroscopy Biochem 47 2008 9781 9792
    • (2008) Biochem , vol.47 , pp. 9781-9792
    • Fielding, A.J.1    Singh, R.2    Boscolo, B.3    Loewen, P.C.4    Ghibaudi, E.M.5    Ivancich, A.6
  • 20
    • 34548577031 scopus 로고    scopus 로고
    • Generation and identification of reactive metabolites by electrochemistry and immobilized enzymes coupled on-line to liquid chromatography/mass spectrometry
    • W. Lohmann, and U. Karst Generation and identification of reactive metabolites by electrochemistry and immobilized enzymes coupled on-line to liquid chromatography/mass spectrometry Anal. Chem. 79 2007 6831 6839
    • (2007) Anal. Chem. , vol.79 , pp. 6831-6839
    • Lohmann, W.1    Karst, U.2
  • 21
    • 0000805517 scopus 로고
    • On the function and mechanism of action of peroxidases
    • H.B. Dunford, and J.S. Stillman On the function and mechanism of action of peroxidases Coord. Chem. Rev. 19 1976 187 251
    • (1976) Coord. Chem. Rev. , vol.19 , pp. 187-251
    • Dunford, H.B.1    Stillman, J.S.2
  • 22
    • 0023775004 scopus 로고
    • Enzymatic oxidative activation and transformation of the antitumor agent mitoxantrone
    • P. Kolodziejczyk, K. Reszka, and J.W. Lown Enzymatic oxidative activation and transformation of the antitumor agent mitoxantrone Free Radical Biol. Med. 5 1988 13 25
    • (1988) Free Radical Biol. Med. , vol.5 , pp. 13-25
    • Kolodziejczyk, P.1    Reszka, K.2    Lown, J.W.3
  • 23
    • 0023038168 scopus 로고
    • Horseradish peroxidase-catalyzed oxidation of mitoxantrone: Spectrophotometric and electron paramagnetic resonance studies
    • K.J. Reszka, P. Kolodziejczyk, and J.W. Lown Horseradish peroxidase-catalyzed oxidation of mitoxantrone: spectrophotometric and electron paramagnetic resonance studies J. Free Rad. Biol. Med. 2 1986 25 32
    • (1986) J. Free Rad. Biol. Med. , vol.2 , pp. 25-32
    • Reszka, K.J.1    Kolodziejczyk, P.2    Lown, J.W.3
  • 24
    • 0024340588 scopus 로고
    • The reaction of horseradish peroxidase, lactoperoxidase and myeloperoxidase with enzymatically generated superoxide
    • D. Metodiwa, and H.B. Dunford The reaction of horseradish peroxidase, lactoperoxidase and myeloperoxidase with enzymatically generated superoxide Arch. Biochem. Biopys 272 1989 245 253
    • (1989) Arch. Biochem. Biopys , vol.272 , pp. 245-253
    • Metodiwa, D.1    Dunford, H.B.2
  • 25
    • 0023759565 scopus 로고
    • The potential diagram for oxygen at pH 7
    • P.M. Wood The potential diagram for oxygen at pH 7 Biochem. J. 235 1988 287 289
    • (1988) Biochem. J. , vol.235 , pp. 287-289
    • Wood, P.M.1
  • 26
    • 0019349401 scopus 로고
    • Interactions of the new antitumor agent 1,4-dihydroxy-5,8-bis[[2-[(2- hydroxyethyl)amino]-ethyl]amino]-9,10-anthracenedione, with nucleic acids
    • J. Kapuscinski, Z. Darzynkiewicz, F. Traganos, and M.R. Melamed Interactions of the new antitumor agent 1,4-dihydroxy-5,8-bis[[2-[(2- hydroxyethyl)amino]-ethyl]amino]-9,10-anthracenedione, with nucleic acids Biochem. Pharm. 30 1981 231 240
    • (1981) Biochem. Pharm. , vol.30 , pp. 231-240
    • Kapuscinski, J.1    Darzynkiewicz, Z.2    Traganos, F.3    Melamed, M.R.4
  • 27
    • 0001624554 scopus 로고
    • Optical spectroscopic studies of the antitumor drug 1,4-dihydroxy-5,8- bis[[2-[(2-hydroxyethyl)amino]ethyl]amino]-9,10-anthracenedione (mitoxantrone)
    • B.S. Lee, and P.K. Dutta Optical spectroscopic studies of the antitumor drug 1,4-dihydroxy-5,8-bis[[2-[(2-hydroxyethyl)amino]ethyl]amino]-9,10- anthracenedione (mitoxantrone) J. Phys. Chem. 93 1989 5665 5672
    • (1989) J. Phys. Chem. , vol.93 , pp. 5665-5672
    • Lee, B.S.1    Dutta, P.K.2
  • 28
    • 0141679063 scopus 로고    scopus 로고
    • Oxidation of thioanisole and p-methoxythioanisole by lignin peroxidase: Kinetic evidence of a direct reaction between Compound II and a radical cation
    • T.B. Brück, M.F. Gerini, E. Baciocchi, and P.J. Harvey Oxidation of thioanisole and p-methoxythioanisole by lignin peroxidase: kinetic evidence of a direct reaction between Compound II and a radical cation Biochem. J. 374 Pt 3 2003 761 766
    • (2003) Biochem. J. , vol.374 , Issue.PART 3 , pp. 761-766
    • Brück, T.B.1    Gerini, M.F.2    Baciocchi, E.3    Harvey, P.J.4
  • 29
    • 0023742760 scopus 로고
    • Spectral studies with lactoperoxidase and thyroid peroxidase: Interconversions between native enzyme, Compound II and Compound III
    • H. Kohler, A. Taurog, and H.B. Dunford Spectral studies with lactoperoxidase and thyroid peroxidase: interconversions between native enzyme, Compound II and Compound III Arch. Biochem. Biophys. 264 1988 438 444
    • (1988) Arch. Biochem. Biophys. , vol.264 , pp. 438-444
    • Kohler, H.1    Taurog, A.2    Dunford, H.B.3
  • 30
    • 0018070937 scopus 로고
    • Isolation and purification of rat mammary tumour peroxidase
    • E.R. DeSombre, and C.R. Lyttle Isolation and purification of rat mammary tumour peroxidase Cancer Res. 38 1978 4086 4090
    • (1978) Cancer Res. , vol.38 , pp. 4086-4090
    • Desombre, E.R.1    Lyttle, C.R.2
  • 31
    • 0034629002 scopus 로고    scopus 로고
    • Metabolism of cellulose by Phanerochaete chrysosporium in continuously agitated culture is associated with enhanced production of lignin peroxidase
    • L. Zacchi, G. Burla, D. Zuolong, and P.J. Harvey Metabolism of cellulose by Phanerochaete chrysosporium in continuously agitated culture is associated with enhanced production of lignin peroxidase J. Biotechnol. 78 2000 185 192
    • (2000) J. Biotechnol. , vol.78 , pp. 185-192
    • Zacchi, L.1    Burla, G.2    Zuolong, D.3    Harvey, P.J.4
  • 32
    • 0027114926 scopus 로고
    • Purification and characterization of a soluble peroxidase of rat preputial gland: Comparison with lactoperoxidase
    • P.K. De, and R.K. Banerjee Purification and characterization of a soluble peroxidase of rat preputial gland: comparison with lactoperoxidase Biochim. Biophys. Acta 1120 1992 167 172
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 167-172
    • De, P.K.1    Banerjee, R.K.2
  • 33
    • 0016659527 scopus 로고
    • Fractionation of horseradish peroxidase by preparative isoelectric focusing, gel chromatography and ion-exchange chromatography
    • H. Delincee, and B. Radola Fractionation of horseradish peroxidase by preparative isoelectric focusing, gel chromatography and ion-exchange chromatography Eur. J. Biochem. 52 1975 321 330
    • (1975) Eur. J. Biochem. , vol.52 , pp. 321-330
    • Delincee, H.1    Radola, B.2
  • 34
    • 0041096260 scopus 로고
    • Calculation of equilibrium constants from multiwavelength spectroscopic data-IV
    • H. Gampp, M. Maeder, C.H.J. Meyer, and A.D. Zuberbühler Calculation of equilibrium constants from multiwavelength spectroscopic data-IV Talanta 33 1986 943 951
    • (1986) Talanta , vol.33 , pp. 943-951
    • Gampp, H.1    Maeder, M.2    Meyer, C.H.J.3    Zuberbühler, A.D.4
  • 35
    • 0000685339 scopus 로고
    • The spectra of the enzyme-substrate complexes of catalase and peroxidase
    • B. Chance The spectra of the enzyme-substrate complexes of catalase and peroxidase Arch.Biochem.Biophys. 41 1952 404 415
    • (1952) Arch.Biochem.Biophys. , vol.41 , pp. 404-415
    • Chance, B.1
  • 37
    • 0027420344 scopus 로고
    • Cytochrome P-450-induced cytotoxicity of mitoxatrone by formation of electrophilic intermediates
    • K. Mewes, J. Blanz, G. Ehninger, R. Gebhardt, and K.-P. Zeller Cytochrome P-450-induced cytotoxicity of mitoxatrone by formation of electrophilic intermediates Cancer Res. 53 1993 5135 5142
    • (1993) Cancer Res. , vol.53 , pp. 5135-5142
    • Mewes, K.1    Blanz, J.2    Ehninger, G.3    Gebhardt, R.4    Zeller, K.-P.5
  • 38
    • 0033637505 scopus 로고    scopus 로고
    • Selective oxygen transfer catalyzed by the heme peroxidases: Synthetic and mechanistic aspects
    • F. van Rantwijk, and R.A. Sheldon Selective oxygen transfer catalyzed by the heme peroxidases: synthetic and mechanistic aspects Curr.Opin.Biotechnol. 11 2000 554 564
    • (2000) Curr.Opin.Biotechnol. , vol.11 , pp. 554-564
    • Van Rantwijk, F.1    Sheldon, R.A.2
  • 39
    • 0026021362 scopus 로고
    • Production of large amounts of hydrogen peroxide by human tumor cells
    • T.P. Szatrowski, and C.F. Nathan Production of large amounts of hydrogen peroxide by human tumor cells Cancer Res. 51 1991 794 798
    • (1991) Cancer Res. , vol.51 , pp. 794-798
    • Szatrowski, T.P.1    Nathan, C.F.2
  • 40
    • 34248396033 scopus 로고    scopus 로고
    • Dual role of hydrogen peroxide in cancer: Possible relevance to cancer chemoprevention and therapy
    • M. Lopez-Lazaro Dual role of hydrogen peroxide in cancer: possible relevance to cancer chemoprevention and therapy Cancer Lett. 252 2007 1 8
    • (2007) Cancer Lett. , vol.252 , pp. 1-8
    • Lopez-Lazaro, M.1
  • 43
    • 0031981322 scopus 로고    scopus 로고
    • Cytotoxicity of weak electrolytes after adaptation of cells to low pH: Role of transmembrane pH gradient
    • S.V. Kozin, and L.E. Gerweck Cytotoxicity of weak electrolytes after adaptation of cells to low pH: role of transmembrane pH gradient Brit.J.Cancer. 77 1998 1580 1585
    • (1998) Brit.J.Cancer. , vol.77 , pp. 1580-1585
    • Kozin, S.V.1    Gerweck, L.E.2
  • 44
    • 0141786825 scopus 로고    scopus 로고
    • Tumour acidity, ion trapping and chemotherapeutics. I. Acid pH affects the distribution of chemotherapeutic agents in vitro
    • B.P. Mahoney, N. Raghunand, B. Bagget, and R.J. Gillies Tumour acidity, ion trapping and chemotherapeutics. I. Acid pH affects the distribution of chemotherapeutic agents in vitro Biochem. Pharmacol. 66 2003 1207 1218
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1207-1218
    • Mahoney, B.P.1    Raghunand, N.2    Bagget, B.3    Gillies, R.J.4
  • 45
    • 70349479241 scopus 로고    scopus 로고
    • Prx1 enhances androgen receptor function in prostate cancer cells by increasing receptor affinity to dihydrotestosterone
    • R.R. Chhipa, K.S. Lee, S. Onate, Y. Wu, and C. Ip Prx1 enhances androgen receptor function in prostate cancer cells by increasing receptor affinity to dihydrotestosterone Mol. Cancer Res. 7 2009 1543 1552
    • (2009) Mol. Cancer Res. , vol.7 , pp. 1543-1552
    • Chhipa, R.R.1    Lee, K.S.2    Onate, S.3    Wu, Y.4    Ip, C.5
  • 46
    • 34047140371 scopus 로고    scopus 로고
    • The role of antioxidant enzymes in the growth of pancreatic carcinoma
    • N. Jabbari, and J.J. Cullen The role of antioxidant enzymes in the growth of pancreatic carcinoma Curr. Canc. Ther. Rev. 3 2007 61 65
    • (2007) Curr. Canc. Ther. Rev. , vol.3 , pp. 61-65
    • Jabbari, N.1    Cullen, J.J.2
  • 47
    • 0030915947 scopus 로고    scopus 로고
    • Hydrogen peroxidase is involved in lymphocyte activation mechanisms to induce angiogenesis
    • M. Monte, L.E. Davel, and E. Sacerdote de Lustig Hydrogen peroxidase is involved in lymphocyte activation mechanisms to induce angiogenesis Eur.J.Canc. 33 1997 676 682
    • (1997) Eur.J.Canc. , vol.33 , pp. 676-682
    • Monte, M.1    Davel, L.E.2    Sacerdote De Lustig, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.