메뉴 건너뛰기




Volumn 16, Issue 11, 2015, Pages 27561-27575

A mechanism of O-demethylation of aristolochic acid I by cytochromes P450 and their contributions to this reaction in human and rat livers: Experimental and theoretical approaches

Author keywords

Contribution of cytochromes P450 in detoxification of aristolochic acid I in human and rat livers; Cytochrome P450 mediated detoxification of aristolochic acid I; Molecular modeling; Plant nephrotoxin and carcinogen aristolochic acid I

Indexed keywords

ALPHA NAPHTHOFLAVONE; AMANTADINE; ARISTOLOCHIC ACID; CYTOCHROME B5; CYTOCHROME P450; DIETHYLDITHIOCARBAMIC ACID; FURAFYLLINE; KETOCONAZOLE; O DEMETHYLASE; QUINIDINE; SULFAPHENAZOLE; ARISTOLOCHIC ACID I; CYTOCHROME P450 INHIBITOR; PROTEIN BINDING;

EID: 84947564784     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms161126047     Document Type: Article
Times cited : (31)

References (91)
  • 1
    • 0036020624 scopus 로고    scopus 로고
    • Aristolochic acid as a probable human cancer hazard in herbal remedies
    • Arlt, V.M.; Stiborova, M.; Schmeiser, H.H. Aristolochic acid as a probable human cancer hazard in herbal remedies: A review. Mutagenesis 2002, 17, 265–277.
    • (2002) A Review. Mutagenesis , vol.17 , pp. 265-277
    • Arlt, V.M.1    Stiborova, M.2    Schmeiser, H.H.3
  • 2
    • 58449131001 scopus 로고    scopus 로고
    • Chemical and molecular basis of the carcinogenicity of Aristolochia plants
    • Schmeiser, H.H.; Stiborová, M.; Arlt, V.M. Chemical and molecular basis of the carcinogenicity of Aristolochia plants. Curr. Opin. Drug Discov. Dev. 2009, 12, 141–148.
    • (2009) Curr. Opin. Drug Discov. Dev , vol.12 , pp. 141-148
    • Schmeiser, H.H.1    Stiborová, M.2    Arlt, V.M.3
  • 7
    • 84947559971 scopus 로고    scopus 로고
    • A review of human CARCINOGENS: Pharmaceuticals
    • World Health Organization: Geneva, Switzerland
    • International Agency for Research on Cancer (IARC). A review of human CARCINOGENS: Pharmaceuticals. In Environ. Health Criteria Monographs;World Health Organization: Geneva, Switzerland, 2012; Volume 100A.
    • (2012) Environ. Health Criteria Monographs , vol.100A
  • 12
    • 38649109829 scopus 로고    scopus 로고
    • Metabolic activation of carcinogenic aristolochic acid, a risk factor for Balkan endemic nephropathy
    • Stiborová, M.; Frei, E.; Arlt, V.M.; Schmeiser, H.H. Metabolic activation of carcinogenic aristolochic acid, a risk factor for Balkan endemic nephropathy. Mutat. Res. Rev. Mutat. Res. 2008, 658, 55–67.
    • (2008) Mutat. Res. Rev. Mutat. Res , vol.658 , pp. 55-67
    • Stiborová, M.1    Frei, E.2    Arlt, V.M.3    Schmeiser, H.H.4
  • 13
    • 43749112968 scopus 로고    scopus 로고
    • Biotransformation enzymes in development of renal injury and urothelial cancer caused by aristolochic acid
    • Stiborová, M.; Frei, E.; Schmeiser, H.H. Biotransformation enzymes in development of renal injury and urothelial cancer caused by aristolochic acid. Kidney Int. 2008, 73, 1209–1211.
    • (2008) Kidney Int , vol.73 , pp. 1209-1211
    • Stiborová, M.1    Frei, E.2    Schmeiser, H.H.3
  • 14
    • 84882303544 scopus 로고    scopus 로고
    • Enzymes metabolizing aristolochic acid and their contribution to the development of Aristolochic acid nephropathy and urothelial cancer
    • Stiborová, M.; Martínek, V.; Frei, E.; Arlt, V.M.; Schmeiser, H.H. Enzymes metabolizing aristolochic acid and their contribution to the development of Aristolochic acid nephropathy and urothelial cancer. Curr. Drug Metab. 2013, 14, 695–705.
    • (2013) Curr. Drug Metab , vol.14 , pp. 695-705
    • Stiborová, M.1    Martínek, V.2    Frei, E.3    Arlt, V.M.4    Schmeiser, H.H.5
  • 15
    • 84893070184 scopus 로고    scopus 로고
    • Knock-out and humanized mice as suitable tools to identify enzymes metabolizing the human carcinogen aristolochic acid
    • Stiborová, M.; Frei, E.; Arlt, V.M.; Schmeiser, H.H. Knock-out and humanized mice as suitable tools to identify enzymes metabolizing the human carcinogen aristolochic acid. Xenobiotica 2014, 44, 135–145.
    • (2014) Xenobiotica , vol.44 , pp. 135-145
    • Stiborová, M.1    Frei, E.2    Arlt, V.M.3    Schmeiser, H.H.4
  • 16
    • 0029983768 scopus 로고    scopus 로고
    • Detection of DNA adducts formed by aristolochic acid in renal tissue from patients with Chinese herbs nephropathy
    • Schmeiser, H.H.; Bieler, C.A.; Wiessler, M.; van Ypersele de Strihou, C.; Cosyns, J.P. Detection of DNA adducts formed by aristolochic acid in renal tissue from patients with Chinese herbs nephropathy. Cancer Res. 1996, 56, 2025–2028.
    • (1996) Cancer Res , vol.56 , pp. 2025-2028
    • Schmeiser, H.H.1    Bieler, C.A.2    Wiessler, M.3    Van Ypersele De Strihou, C.4    Cosyns, J.P.5
  • 17
    • 0031408650 scopus 로고    scopus 로고
    • Comparison of DNA adduct formation by aristolochic acids in various in vitro activation systems by 32P-post-labelling: Evidence for reductive activation by peroxidases
    • Schmeiser, H.H.; Frei, E.; Wiessler, M.; Stiborová, M. Comparison of DNA adduct formation by aristolochic acids in various in vitro activation systems by 32P-post-labelling: Evidence for reductive activation by peroxidases. Carcinogenesis 1996, 18, 1055–1062.
    • (1996) Carcinogenesis , vol.18 , pp. 1055-1062
    • Schmeiser, H.H.1    Frei, E.2    Wiessler, M.3    Stiborová, M.4
  • 21
    • 58149459327 scopus 로고    scopus 로고
    • TP53 mutation signature supports involvement of aristolochic acid in the aetiology of endemic nephropathy-associated tumours
    • Nedelko, T.; Arlt, V.M.; Phillips, D.H.; Hollstein, M. TP53 mutation signature supports involvement of aristolochic acid in the aetiology of endemic nephropathy-associated tumours. Int. J. Cancer 2009, 124, 987–990.
    • (2009) Int. J. Cancer , vol.124 , pp. 987-990
    • Nedelko, T.1    Arlt, V.M.2    Phillips, D.H.3    Hollstein, M.4
  • 22
    • 77953219808 scopus 로고    scopus 로고
    • Linking environmental carcinogen exposure to TP53 mutations in human tumours using the human TP53 knock-in (Hupki) mouse model
    • Kucab, J.E.; Phillips, D.H.; Arlt, V.M. Linking environmental carcinogen exposure to TP53 mutations in human tumours using the human TP53 knock-in (Hupki) mouse model. FEBS J. 2010, 277, 2567–2583.
    • (2010) FEBS J , vol.277 , pp. 2567-2583
    • Kucab, J.E.1    Phillips, D.H.2    Arlt, V.M.3
  • 27
    • 33646948289 scopus 로고    scopus 로고
    • Study of the phase I and phase II metabolism of nephrotoxin aristolochic acid by liquid chromatography/tandem mass spectrometry
    • Chan, W.; Cu, L.; Xu, G.; Cai, Z. Study of the phase I and phase II metabolism of nephrotoxin aristolochic acid by liquid chromatography/tandem mass spectrometry. Rapid. Commun. Mass Spectrom. 2006, 20, 1755–1760.
    • (2006) Rapid. Commun. Mass Spectrom. , vol.20 , pp. 1755-1760
    • Chan, W.1    Cu, L.2    Xu, G.3    Cai, Z.4
  • 28
    • 77955477610 scopus 로고    scopus 로고
    • Detoxification of aristolochic acid I by O-demethylation: Less nephrotoxicity and genotoxicity of aristolochic acid Ia in rodents
    • Shibutani, S.; Bonala, R.R.; Rosenquist, T.; Rieger, R.; Suzuki, N.; Johnson, F.; Miller, F.; Grollman, A.P. Detoxification of aristolochic acid I by O-demethylation: Less nephrotoxicity and genotoxicity of aristolochic acid Ia in rodents. Int. J. Cancer 2010, 127, 1021–1027.
    • (2010) Int. J. Cancer , vol.127 , pp. 1021-1027
    • Shibutani, S.1    Bonala, R.R.2    Rosenquist, T.3    Rieger, R.4    Suzuki, N.5    Johnson, F.6    Miller, F.7    Grollman, A.P.8
  • 29
    • 80054742122 scopus 로고    scopus 로고
    • Role of P450 1A1 and P450 1A2 in bioactivation versus detoxication of the renal carcinogen aristolochic acid I: Studies in Cyp1a1-/-, Cyp1a2-/-, and Cyp1a1/1a2-/- mice
    • Arlt, V.M.; Levova, K.; Barta, F.; Shi, Z.; Evans, J.D.; Frei, E.; Schmeiser, H.H.; Nebert, D.W.; Phillips, D.H.; Stiborova, M. Role of P450 1A1 and P450 1A2 in bioactivation versus detoxication of the renal carcinogen aristolochic acid I: Studies in Cyp1a1-/-, Cyp1a2-/-, and Cyp1a1/1a2-/- mice. Chem. Res. Toxicol. 2011, 24, 1710–1719.
    • (2011) Chem. Res. Toxicol. , vol.24 , pp. 1710-1719
    • Arlt, V.M.1    Levova, K.2    Barta, F.3    Shi, Z.4    Evans, J.D.5    Frei, E.6    Schmeiser, H.H.7    Nebert, D.W.8    Phillips, D.H.9    Stiborova, M.10
  • 30
  • 31
    • 0036257348 scopus 로고    scopus 로고
    • Carcinogenic aristolochic acids upon activation by DT-diaphorase form adducts found in DNA of patients with Chinese herbs nephropathy
    • Stiborová, M.; Frei, E.; Sopko, B.; Wiessler, M.; Schmeiser, H.H. Carcinogenic aristolochic acids upon activation by DT-diaphorase form adducts found in DNA of patients with Chinese herbs nephropathy. Carcinogenesis 2002, 23, 617–625.
    • (2002) Carcinogenesis , vol.23 , pp. 617-625
    • Stiborová, M.1    Frei, E.2    Sopko, B.3    Wiessler, M.4    Schmeiser, H.H.5
  • 32
    • 0142185373 scopus 로고    scopus 로고
    • Human cytosolic enzymes involved in the metabolic activation of carcinogenic aristolochic acid: Evidence for reductive activation by human NAD(P)H:Quinone oxidoreductase
    • Stiborová, M.; Frei, E.; Sopko, B.; Sopková, K.; Marková, V.; Laˇ nková, M.; Kumstýˇrová, T.; Wiessler, M.; Schmeiser, H.H. Human cytosolic enzymes involved in the metabolic activation of carcinogenic aristolochic acid: Evidence for reductive activation by human NAD(P)H:quinone oxidoreductase. Carcinogenesis 2003, 24, 1695–1703.
    • (2003) Carcinogenesis , vol.24 , pp. 1695-1703
    • Stiborová, M.1    Frei, E.2    Sopko, B.3    Sopková, K.4    Marková, V.5    Laˇ Nková, M.6    Kumstýˇrová, T.7    Wiessler, M.8    Schmeiser, H.H.9
  • 33
    • 79955436820 scopus 로고    scopus 로고
    • The human carcinogen aristolochic acid I is activated to form DNA adducts by human NAD(P)H:Quinone oxidoreductase without the contribution of acetyltransferases or sulfotransferases
    • Stiborová, M.; Mareš, J.; Frei, E.; Arlt, V.M.; Martínek, V.; Schmeiser, H.H. The human carcinogen aristolochic acid I is activated to form DNA adducts by human NAD(P)H:quinone oxidoreductase without the contribution of acetyltransferases or sulfotransferases. Environ. Mol. Mutagen. 2011, 52, 448–459.
    • (2011) Environ. Mol. Mutagen , vol.52 , pp. 448-459
    • Stiborová, M.1    Mareš, J.2    Frei, E.3    Arlt, V.M.4    Martínek, V.5    Schmeiser, H.H.6
  • 34
    • 84902268459 scopus 로고    scopus 로고
    • Mechanisms of enzyme-catalyzed reduction of two carcinogenic nitro-aromatics, 3-nitrobenzanthrone and aristolochic acid I: Experimental and theoretical approaches
    • Stiborová, M.; Frei, E.; Schmeiser, H.H.; Arlt, V.M.; Martínek, V. Mechanisms of enzyme-catalyzed reduction of two carcinogenic nitro-aromatics, 3-nitrobenzanthrone and aristolochic acid I: Experimental and theoretical approaches. Int. J. Mol. Sci. 2014, 15, 10271–10295.
    • (2014) Int. J. Mol. Sci. , vol.15 , pp. 10271-10295
    • Stiborová, M.1    Frei, E.2    Schmeiser, H.H.3    Arlt, V.M.4    Martínek, V.5
  • 35
    • 84898847123 scopus 로고    scopus 로고
    • The influence of dicoumarol on the bioactivation of the carcinogen aristolochic acid I in rats
    • Stiborová, M.; Levová, K.; Bárta, F.; Šulc, M.; Frei, E.; Arlt, V.M.; Schmeiser, H.H. The influence of dicoumarol on the bioactivation of the carcinogen aristolochic acid I in rats. Mutagenesis 2014, 29, 189–200.
    • (2014) Mutagenesis , vol.29 , pp. 189-200
    • Stiborová, M.1    Levová, K.2    Bárta, F.3    Šulc, M.4    Frei, E.5    Arlt, V.M.6    Schmeiser, H.H.7
  • 36
    • 84857387612 scopus 로고    scopus 로고
    • Comparison of activation of aristolochic acid I and II with NADPH:Quinone oxidoreductase, sulphotransferases and N-acetyltranferases
    • Martinek, V.; Kubickova, B.; Arlt, V.M.; Frei, E.; Schmeiser, H.H.; Hudĕcek, J.; Stiborova, M. Comparison of activation of aristolochic acid I and II with NADPH:quinone oxidoreductase, sulphotransferases and N-acetyltranferases. Neuro Endocrinol. Lett. 2011, 32, 57–70.
    • (2011) Neuro Endocrinol. Lett , vol.32 , pp. 57-70
    • Martinek, V.1    Kubickova, B.2    Arlt, V.M.3    Frei, E.4    Schmeiser, H.H.5    Hudĕcek, J.6    Stiborova, M.7
  • 37
    • 80051678011 scopus 로고    scopus 로고
    • Inhibition of renal NQO1 activity by dicoumarol suppresses nitroreduction of aristolochic acid I and attenuates its nephrotoxicity
    • Chen, M.; Gong, L.; Qi, X.; Xing, G.; Luan, Y.; Wu, Y.; Xiao, Y.; Yao, J.; Li, Y.; Xue, X. et al. Inhibition of renal NQO1 activity by dicoumarol suppresses nitroreduction of aristolochic acid I and attenuates its nephrotoxicity. Toxicol. Sci. 2011, 122, 288–296.
    • (2011) Toxicol. Sci , vol.122 , pp. 288-296
    • Chen, M.1    Gong, L.2    Qi, X.3    Xing, G.4    Luan, Y.5    Wu, Y.6    Xiao, Y.7    Yao, J.8    Li, Y.9    Xue, X.10
  • 38
    • 0034861029 scopus 로고    scopus 로고
    • Human enzymes involved in the metabolic activation of carcinogenic aristolochic acids: Evidence for reductive activation by cytochromes P450 1A1 and 1A2
    • Stiborová, M.; Frei, E.; Wiessler, M.; Schmeiser, H.H. Human enzymes involved in the metabolic activation of carcinogenic aristolochic acids: Evidence for reductive activation by cytochromes P450 1A1 and 1A2. Chem. Res. Toxicol. 2001, 14, 1128–1137.
    • (2001) Chem. Res. Toxicol , vol.14 , pp. 1128-1137
    • Stiborová, M.1    Frei, E.2    Wiessler, M.3    Schmeiser, H.H.4
  • 39
    • 10344258034 scopus 로고    scopus 로고
    • Human hepatic and renal microsomes, cytochromes P450 1A1/2, NADPH:CYP reductase and prostaglandin H synthase mediate the formation of aristolochic acid DNA-adducts found in patients with urothelial cancer
    • Stiborová, M.; Frei, E.; Hodek, P.; Wiessler, M.; Schmeiser, H.H. Human hepatic and renal microsomes, cytochromes P450 1A1/2, NADPH:CYP reductase and prostaglandin H synthase mediate the formation of aristolochic acid DNA-adducts found in patients with urothelial cancer. Int. J. Cancer 2005, 113, 189–197.
    • (2005) Int. J. Cancer , vol.113 , pp. 189-197
    • Stiborová, M.1    Frei, E.2    Hodek, P.3    Wiessler, M.4    Schmeiser, H.H.5
  • 40
    • 26444446947 scopus 로고    scopus 로고
    • The binding of aristolochic acid I to the active site of human cytochromes P450 1A1 and 1A2 explains their potential to reductively activate this human carcinogen
    • Stiborová, M.; Sopko, B.; Hodek, P.; Frei, E.; Schmeiser, H.H.; Hudĕcek, J. The binding of aristolochic acid I to the active site of human cytochromes P450 1A1 and 1A2 explains their potential to reductively activate this human carcinogen. Cancer Lett. 2005, 229, 193–204.
    • (2005) Cancer Lett , vol.229 , pp. 193-204
    • Stiborová, M.1    Sopko, B.2    Hodek, P.3    Frei, E.4    Schmeiser, H.H.5    Hudĕcek, J.6
  • 41
    • 84857427527 scopus 로고    scopus 로고
    • Role of cytochromes P450 in metabolism of carcinogenic aristolochic acid I: Evidence of their contribution to aristolochic acid I detoxication and activation in rat liver
    • Stiborová, M.; Mareš, J.; Levová, K.; Pavlíˇcková, J.; Bárta, F.; Hodek, P.; Frei, E.; Schmeiser, H.H. Role of cytochromes P450 in metabolism of carcinogenic aristolochic acid I: Evidence of their contribution to aristolochic acid I detoxication and activation in rat liver. Neuro Endocrinol. Lett. 2011, 32, 121–130.
    • (2011) Neuro Endocrinol. Lett , vol.32 , pp. 121-130
    • Stiborová, M.1    Mareš, J.2    Levová, K.3    Pavlíˇcková, J.4    Bárta, F.5    Hodek, P.6    Frei, E.7    Schmeiser, H.H.8
  • 42
    • 84928801738 scopus 로고    scopus 로고
    • The Hepatic Reductase Null (HRN™) and Reductase Conditional Null (RCN) mouse models as suitable tools to study metabolism, toxicity and carcinogenicity of environmental pollutants
    • Arlt, V.M.; Henderson, C.J.; Wolf, C.R.; Stiborova, M.; Phillips, D.H. The Hepatic Reductase Null (HRN™) and Reductase Conditional Null (RCN) mouse models as suitable tools to study metabolism, toxicity and carcinogenicity of environmental pollutants. Toxicol. Res. 2015, 4, 548–562.
    • (2015) Toxicol. Res , vol.4 , pp. 548-562
    • Arlt, V.M.1    Henderson, C.J.2    Wolf, C.R.3    Stiborova, M.4    Phillips, D.H.5
  • 43
    • 79955410481 scopus 로고    scopus 로고
    • Role of cytochromes P450 1A1/2 in detoxication and activation of carcinogenic aristolochic acid I: Studies with the hepatic NADPH: Cytochrome P450 reductase null (HRN) mouse model
    • Levová, K.; Mizerovská, M.; Kotrbová, V.; Šulc, M.; Henderson, C.J.; Wolf, C.R.; Philips, D.H.; Frei, E.; Schmeiser, H.H.; Mareš, J., et al. Role of cytochromes P450 1A1/2 in detoxication and activation of carcinogenic aristolochic acid I: Studies with the hepatic NADPH: Cytochrome P450 reductase null (HRN) mouse model. Toxicol. Sci. 2011, 121, 43–56.
    • (2011) Toxicol. Sci , vol.121 , pp. 43-56
    • Levová, K.1    Mizerovská, M.2    Kotrbová, V.3    Šulc, M.4    Henderson, C.J.5    Wolf, C.R.6    Philips, D.H.7    Frei, E.8    Schmeiser, H.H.9    Mareš, J.10
  • 44
    • 84870302951 scopus 로고    scopus 로고
    • NAD(P)H:Quinone oxidoreductase expression in Cyp1a-knockout and CYP1A-humanized mouse lines and its effect on bioactivation of the carcinogen aristolochic acid I
    • Levová, K.; Moserova, M.; Nebert, D.W.; Phillips, D.H.; Frei, E.; Schmeiser, H.H.; Arlt, V.M.; Stiborova, M. NAD(P)H:quinone oxidoreductase expression in Cyp1a-knockout and CYP1A-humanized mouse lines and its effect on bioactivation of the carcinogen aristolochic acid I. Toxicol. Appl. Pharmacol. 2012, 265, 360–367.
    • (2012) Toxicol. Appl. Pharmacol , vol.265 , pp. 360-367
    • Levová, K.1    Moserova, M.2    Nebert, D.W.3    Phillips, D.H.4    Frei, E.5    Schmeiser, H.H.6    Arlt, V.M.7    Stiborova, M.8
  • 45
    • 84874806270 scopus 로고    scopus 로고
    • Theoretical investigation of differences in nitroreduction of aristolochic acid I by cytochromes P450 1A1, 1A2 and 1B1
    • Jerabek, P.; Martinek, V.; Stiborova, M. Theoretical investigation of differences in nitroreduction of aristolochic acid I by cytochromes P450 1A1, 1A2 and 1B1. Neuro Endocrinol. Lett. 2012, 33, 25–32.
    • (2012) Neuro Endocrinol. Lett. , vol.33 , pp. 25-32
    • Jerabek, P.1    Martinek, V.2    Stiborova, M.3
  • 46
    • 57149122064 scopus 로고    scopus 로고
    • Human cytochromes P450 1A1 and 1A2 participate in detoxication of carcinogenic aristolochic acid
    • Sistkova, J.; Hudecek, J.; Hodek, P.; Frei, E.; Schmeiser, H.H.; Stiborova, M. Human cytochromes P450 1A1 and 1A2 participate in detoxication of carcinogenic aristolochic acid. Neuro Endocrinol. Lett. 2008, 29, 733–737.
    • (2008) Neuro Endocrinol. Lett , vol.29 , pp. 733-737
    • Sistkova, J.1    Hudecek, J.2    Hodek, P.3    Frei, E.4    Schmeiser, H.H.5    Stiborova, M.6
  • 49
    • 43749122582 scopus 로고    scopus 로고
    • Hepatic cytochrome P450s metabolize aristolochic acid and reduce its kidney toxicity
    • Xiao, Y.; Ge, M.; Xue, X.; Wang, C.; Wang, H.; Wu, X.; Li, L.; Liu, L.; Qi, X.; Zhang, Y., et al. Hepatic cytochrome P450s metabolize aristolochic acid and reduce its kidney toxicity. Kidney Int. 2008, 73, 1231–1239.
    • (2008) Kidney Int , vol.73 , pp. 1231-1239
    • Xiao, Y.1    Ge, M.2    Xue, X.3    Wang, C.4    Wang, H.5    Wu, X.6    Li, L.7    Liu, L.8    Qi, X.9    Zhang, Y.10
  • 50
    • 52449095327 scopus 로고    scopus 로고
    • Induction of P450 1A by 3-methylcholanthrene protects mice from aristolochic acid-I-induced acute renal injury
    • Xue, X.; Xiao, Y.; Zhu, H.; Wang, H.; Liu, Y.; Xie, T.; Ren, J. Induction of P450 1A by 3-methylcholanthrene protects mice from aristolochic acid-I-induced acute renal injury. Nephrol. Dial. Transplant. 2008, 23, 3074–3081.
    • (2008) Nephrol. Dial. Transplant , vol.23 , pp. 3074-3081
    • Xue, X.1    Xiao, Y.2    Zhu, H.3    Wang, H.4    Liu, Y.5    Xie, T.6    Ren, J.7
  • 51
    • 0023866860 scopus 로고
    • DNA adduct formation of aristolochic acid I and II in vitro and in vivo
    • Schmeiser, H.H.; Schoepe, K.B.; Wiessler, M. DNA adduct formation of aristolochic acid I and II in vitro and in vivo. Carcinogenesis 1988, 9, 297–303.
    • (1988) Carcinogenesis , vol.9 , pp. 297-303
    • Schmeiser, H.H.1    Schoepe, K.B.2    Wiessler, M.3
  • 52
    • 0025195429 scopus 로고
    • 32P-postlabelling analysis of the DNA adducts formed by aristolochic acid I and II
    • Pfau, W.; Schmeiser, H.H.; Wiessler, M. 32P-postlabelling analysis of the DNA adducts formed by aristolochic acid I and II. Carcinogenesis 1990, 11, 1627–1633.
    • (1990) Carcinogenesis , vol.11 , pp. 1627-1633
    • Pfau, W.1    Schmeiser, H.H.2    Wiessler, M.3
  • 53
    • 0028240901 scopus 로고
    • Characterization of DNA adducts formed by aristolochic acids in the target organ (Forestomach) of rats by 32P-postlabelling analysis using different chromatographic procedures
    • Stiborová, M.; Fernando, R.C.; Schmeiser, H.H.; Frei, E.; Pfau, W.; Wiessler, M. Characterization of DNA adducts formed by aristolochic acids in the target organ (forestomach) of rats by 32P-postlabelling analysis using different chromatographic procedures. Carcinogenesis 1994, 15, 1187–1192.
    • (1994) Carcinogenesis , vol.15 , pp. 1187-1192
    • Stiborová, M.1    Fernando, R.C.2    Schmeiser, H.H.3    Frei, E.4    Pfau, W.5    Wiessler, M.6
  • 54
    • 0031284662 scopus 로고    scopus 로고
    • 32P-post-labelling analysis of DNA adducts formed by aristolochic acid in tissues from patients with Chinese herbs nephropathy
    • Bieler, C.A.; Stiborova, M.; Wiessler, M.; Cosyns, J.P.; van Ypersele de Strihou, C.; Schmeiser, H.H. 32P-post-labelling analysis of DNA adducts formed by aristolochic acid in tissues from patients with Chinese herbs nephropathy. Carcinogenesis 1997, 18, 1063–1067.
    • (1997) Carcinogenesis , vol.18 , pp. 1063-1067
    • Bieler, C.A.1    Stiborova, M.2    Wiessler, M.3    Cosyns, J.P.4    Van Ypersele De Strihou, C.5    Schmeiser, H.H.6
  • 57
    • 0028662025 scopus 로고
    • P450 in the rat and man: Methods of investigation, substrate specificities and relevance to cancer
    • Nedelcheva, V.; Gut, I. P450 in the rat and man: Methods of investigation, substrate specificities and relevance to cancer. Xenobiotica 1994, 24, 1151–1175.
    • (1994) Xenobiotica , vol.24 , pp. 1151-1175
    • Nedelcheva, V.1    Gut, I.2
  • 58
    • 0030834058 scopus 로고    scopus 로고
    • Human cytochrome P450 enzymes: A status report summarizing their reactions, substrates, inducers, and inhibitors
    • Rendic, S.; DiCarlo, F.J. Human cytochrome P450 enzymes: A status report summarizing their reactions, substrates, inducers, and inhibitors. Drug Metab. Rev. 1997, 29, 413–480.
    • (1997) Drug Metab. Rev , vol.29 , pp. 413-480
    • Rendic, S.1    Dicarlo, F.J.2
  • 59
    • 0031570724 scopus 로고    scopus 로고
    • Reconstitution of recombinant cytochrome P450 2C10(2C9) and comparison with cytochrome P450 3A4 and other forms: Effects of cytochrome P450–P450 and cytochrome P450-b5 interactions
    • Yamazaki, H.; Gillam, E.M.; Dong, M.S.; Johnson, W.W.; Guengerich, F.P.; Shimada, T. Reconstitution of recombinant cytochrome P450 2C10(2C9) and comparison with cytochrome P450 3A4 and other forms: Effects of cytochrome P450–P450 and cytochrome P450-b5 interactions. Arch. Biochem. Biophys. 1997, 342, 329–337.
    • (1997) Arch. Biochem. Biophys , vol.342 , pp. 329-337
    • Yamazaki, H.1    Gillam, E.M.2    Dong, M.S.3    Johnson, W.W.4    Guengerich, F.P.5    Shimada, T.6
  • 60
    • 0035903190 scopus 로고    scopus 로고
    • Stimulation of cytochrome P450 reactions by APO-cytochrome b5: Evidence against transfer of heme from cytochrome P450 3A4 to APO-cytochrome b5 or heme oxygenase
    • Yamazaki, H.; Shimada, T.; Martin, M.V.; Guengerich, F.P. Stimulation of cytochrome P450 reactions by APO-cytochrome b5: Evidence against transfer of heme from cytochrome P450 3A4 to APO-cytochrome b5 or heme oxygenase. J. Biol. Chem. 2001, 276, 30885–30891.
    • (2001) J. Biol. Chem , vol.276 , pp. 30885-30891
    • Yamazaki, H.1    Shimada, T.2    Martin, M.V.3    Guengerich, F.P.4
  • 61
    • 0036947946 scopus 로고    scopus 로고
    • The roles of cytochrome b5 in cytochrome P450 reactions
    • Porter, T.D. The roles of cytochrome b5 in cytochrome P450 reactions. J. Biochem. Mol. Toxicol. 2002, 16, 311–316.
    • (2002) J. Biochem. Mol. Toxicol , vol.16 , pp. 311-316
    • Porter, T.D.1
  • 62
    • 0037306331 scopus 로고    scopus 로고
    • The many roles of cytochrome b5
    • Schenkman, J.B.; Jansson, I. The many roles of cytochrome b5. Pharmacol. Ther. 2003, 97, 139–152.
    • (2003) Pharmacol. Ther , vol.97 , pp. 139-152
    • Schenkman, J.B.1    Jansson, I.2
  • 63
    • 34047220898 scopus 로고    scopus 로고
    • Modulation of CYP1A1-mediated oxidation of carcinogenic azo dye Sudan I and its binding to DNA by cytochrome b5
    • Stiborova, M.; Martinek, V.; Schmeiser, H.H.; Frei, E. Modulation of CYP1A1-mediated oxidation of carcinogenic azo dye Sudan I and its binding to DNA by cytochrome b5. Neuro Endocrinol. Lett. 2006, 27, 35–39.
    • (2006) Neuro Endocrinol. Lett. , vol.27 , pp. 35-39
    • Stiborova, M.1    Martinek, V.2    Schmeiser, H.H.3    Frei, E.4
  • 64
    • 84861319892 scopus 로고    scopus 로고
    • Cytochrome b5 increases cytochrome P450 3A4-mediated activation of anticancer drug ellipticine to 13-hydroxyellipticine whose covalent binding to DNA is elevated by sulfotransferases and N,O-acetyltransferases
    • Stiborova, M.; Indra, R.; Moserova, M.; Cerna, V.; Rupertova, M.; Martinek, V.; Eckschlager, T.; Kizek, R.; Frei, E. Cytochrome b5 increases cytochrome P450 3A4-mediated activation of anticancer drug ellipticine to 13-hydroxyellipticine whose covalent binding to DNA is elevated by sulfotransferases and N,O-acetyltransferases. Chem. Res. Toxicol. 2012, 25, 1075–1085.
    • (2012) Chem. Res. Toxicol , vol.25 , pp. 1075-1085
    • Stiborova, M.1    Indra, R.2    Moserova, M.3    Cerna, V.4    Rupertova, M.5    Martinek, V.6    Eckschlager, T.7    Kizek, R.8    Frei, E.9
  • 65
    • 84891359696 scopus 로고    scopus 로고
    • Ellipticine oxidation and DNA adduct formation in human hepatocytes is catalyzed by human cytochromes P450 and enhanced by cytochrome b5
    • Stiborová, M.; Poljaková, J.; Martínková, E.; Ulrichová, J.; Simánek, V.; Dvoˇrák, Z.; Frei, E. Ellipticine oxidation and DNA adduct formation in human hepatocytes is catalyzed by human cytochromes P450 and enhanced by cytochrome b5. Toxicology 2012, 302, 233–241.
    • (2012) Toxicology , vol.302 , pp. 233-241
    • Stiborová, M.1    Poljaková, J.2    Martínková, E.3    Ulrichová, J.4    Simánek, V.5    Dvoˇrák, Z.6    Frei, E.7
  • 66
    • 57649128309 scopus 로고    scopus 로고
    • Defining the in vivo role for cytochrome b5 in cytochrome P450 function through the conditional hepatic deletion of microsomal cytochrome b5
    • Finn, R.D.; McLaughlin, L.A.; Ronseaux, S.; Rosewell, I.; Houston, J.B.; Henderson, C.J.; Wolf, C.R. Defining the in vivo role for cytochrome b5 in cytochrome P450 function through the conditional hepatic deletion of microsomal cytochrome b5. J. Biol. Chem. 2008, 283, 31385–31393.
    • (2008) J. Biol. Chem. , vol.283 , pp. 31385-31393
    • Finn, R.D.1    McLaughlin, L.A.2    Ronseaux, S.3    Rosewell, I.4    Houston, J.B.5    Henderson, C.J.6    Wolf, C.R.7
  • 67
    • 67349145382 scopus 로고    scopus 로고
    • Preparation of a biologically active APO-cytochrome b5 via heterologous expression in Escherichia coli
    • Kotrbova, V.; Aimova, D.; Ingr, M.; Borek-Dohalska, L.; Martinek, V.; Stiborova, M. Preparation of a biologically active APO-cytochrome b5 via heterologous expression in Escherichia coli. Protein Exp. Purif. 2009, 66, 203–209.
    • (2009) Protein Exp. Purif , vol.66 , pp. 203-209
    • Kotrbova, V.1    Aimova, D.2    Ingr, M.3    Borek-Dohalska, L.4    Martinek, V.5    Stiborova, M.6
  • 68
    • 80051552143 scopus 로고    scopus 로고
    • Cytochrome b5 shifts oxidation of the anticancer drug ellipticine by cytochromes P450 1A1 and 1A2 from its detoxication to activation, thereby modulating its pharmacological efficacy
    • Kotrbova, V.; Mrazova, B.; Moserova, M.; Martinek, V.; Hodek, P.; Hudecek, J.; Frei, E.; Stiborova, M. Cytochrome b5 shifts oxidation of the anticancer drug ellipticine by cytochromes P450 1A1 and 1A2 from its detoxication to activation, thereby modulating its pharmacological efficacy. Biochem. Pharmacol. 2011, 82, 669–680.
    • (2011) Biochem. Pharmacol , vol.82 , pp. 669-680
    • Kotrbova, V.1    Mrazova, B.2    Moserova, M.3    Martinek, V.4    Hodek, P.5    Hudecek, J.6    Frei, E.7    Stiborova, M.8
  • 69
    • 77954890052 scopus 로고    scopus 로고
    • Deletion of microsomal cytochrome b5 profoundly affects hepatic and extrahepatic drug metabolism
    • McLaughin, L.A.; Ronseaux, S.; Finn, R.D.; Henderson, C.L.; Wolf, C.R. Deletion of microsomal cytochrome b5 profoundly affects hepatic and extrahepatic drug metabolism. Mol. Pharmacol. 2010, 75, 269–278.
    • (2010) Mol. Pharmacol. , vol.75 , pp. 269-278
    • McLaughin, L.A.1    Ronseaux, S.2    Finn, R.D.3    Henderson, C.L.4    Wolf, C.R.5
  • 71
    • 84877805503 scopus 로고    scopus 로고
    • Evidence that cytochrome b5 and cytochrome b5 reductase can act as sole electron donors to the hepatic cytochrome P450 system
    • Henderson, C.J.; McLaughlin, L.A.; Wolf, C.R. Evidence that cytochrome b5 and cytochrome b5 reductase can act as sole electron donors to the hepatic cytochrome P450 system. Mol. Pharmacol. 2013, 83, 1209–1217.
    • (2013) Mol. Pharmacol , vol.83 , pp. 1209-1217
    • Henderson, C.J.1    McLaughlin, L.A.2    Wolf, C.R.3
  • 72
    • 84908307808 scopus 로고    scopus 로고
    • Flexible docking-based molecular dynamics/steered molecular dynamics calculations of protein-protein contacts in a complex of cytochrome P450 1A2 with cytochrome b5
    • Jĕrábek, P.; Florián, J.; Stiborová, M.; Martínek, V. Flexible docking-based molecular dynamics/steered molecular dynamics calculations of protein-protein contacts in a complex of cytochrome P450 1A2 with cytochrome b5. Biochemistry 2014, 53, 6695–6705.
    • (2014) Biochemistry , vol.53 , pp. 6695-6705
    • Jĕrábek, P.1    Florián, J.2    Stiborová, M.3    Martínek, V.4
  • 75
    • 0024445437 scopus 로고
    • Human CYP1A2: Sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression
    • Ikeya, K.; Jaiswal, A.K.; Owens, R.A.; Jones, J.E.; Nebert, D.W.; Kimura, S. Human CYP1A2: Sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression. Mol. Endocrinol. 1989, 3, 1399–1408.
    • (1989) Mol. Endocrinol , vol.3 , pp. 1399-1408
    • Ikeya, K.1    Jaiswal, A.K.2    Owens, R.A.3    Jones, J.E.4    Nebert, D.W.5    Kimura, S.6
  • 76
    • 0028276386 scopus 로고
    • Complete cDNA sequence of a human dioxin-inducible mRNA identifies a new gene subfamily of cytochrome P450 that maps to chromosome 2
    • Sutter, T.R.; Tang, Y.M.; Hayes, C.L.; Wo, Y.Y.; Jabs, E.W.; Li, X.; Yin, H.; Cody, C.W.; Greenlee, W.F. Complete cDNA sequence of a human dioxin-inducible mRNA identifies a new gene subfamily of cytochrome P450 that maps to chromosome 2. J. Biol. Chem. 1994, 269, 13092–13099.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13092-13099
    • Sutter, T.R.1    Tang, Y.M.2    Hayes, C.L.3    Wo, Y.Y.4    Jabs, E.W.5    Li, X.6    Yin, H.7    Cody, C.W.8    Greenlee, W.F.9
  • 78
    • 0031426565 scopus 로고    scopus 로고
    • Expression of CYP1B1 in human adult and fetal tissues and differential inducibility of CYP1B1 and CYP1A1 by Ah receptor ligands in human placenta and cultured cells
    • Hakkola, J.; Pasanen, M.; Pelkonen, O.; Hukkanen, J.; Evisalmi, S.; Anttila, S.; Rane, A.; Mäntylä, M.; Purkunen, R.; Saarikoski, S. et al. Expression of CYP1B1 in human adult and fetal tissues and differential inducibility of CYP1B1 and CYP1A1 by Ah receptor ligands in human placenta and cultured cells. Carcinogenesis 1997, 18, 391–397.
    • (1997) Carcinogenesis , vol.18 , pp. 391-397
    • Hakkola, J.1    Pasanen, M.2    Pelkonen, O.3    Hukkanen, J.4    Evisalmi, S.5    Anttila, S.6    Rane, A.7    Mäntylä, M.8    Purkunen, R.9    Saarikoski, S.10
  • 79
    • 0031661240 scopus 로고    scopus 로고
    • Development of a comprehensive panel of antibodies against the major xenobiotic metabolising forms of cytochrome P450 in humans
    • Edwards, R.J.; Adams, D.A.; Watts, P.S.; Davies, D.S.; Boobis, A.R. Development of a comprehensive panel of antibodies against the major xenobiotic metabolising forms of cytochrome P450 in humans. Biochem. Pharmacol. 1998, 56, 377–387.
    • (1998) Biochem. Pharmacol , vol.56 , pp. 377-387
    • Edwards, R.J.1    Adams, D.A.2    Watts, P.S.3    Davies, D.S.4    Boobis, A.R.5
  • 80
    • 0037108678 scopus 로고    scopus 로고
    • Sudan I is a potential carcinogen for humans: Evidence for its metabolic activation and detoxication by human recombinant cytochrome P450 1A1 and liver microsomes
    • Stiborová, M.; Martínek, V.; Rýdlová, H.; Hodek, P.; Frei, E. Sudan I is a potential carcinogen for humans: Evidence for its metabolic activation and detoxication by human recombinant cytochrome P450 1A1 and liver microsomes. Cancer Res. 2002, 62, 5678–5684.
    • (2002) Cancer Res , vol.62 , pp. 5678-5684
    • Stiborová, M.1    Martínek, V.2    Rýdlová, H.3    Hodek, P.4    Frei, E.5
  • 81
    • 17644405812 scopus 로고    scopus 로고
    • Expression of cytochrome P450 1A1 and its contribution to oxidation of a potential human carcinogen 1-phenylazo-2-naphthol (Sudan I) in human livers
    • Stiborová, M.; Martínek, V.; Rýdlová, H.; Koblas, T.; Hodek, P. Expression of cytochrome P450 1A1 and its contribution to oxidation of a potential human carcinogen 1-phenylazo-2-naphthol (Sudan I) in human livers. Cancer Lett. 2005, 220, 145–154.
    • (2005) Cancer Lett , vol.220 , pp. 145-154
    • Stiborová, M.1    Martínek, V.2    Rýdlová, H.3    Koblas, T.4    Hodek, P.5
  • 82
    • 84898059625 scopus 로고    scopus 로고
    • Mitochondrial targeting of cytochrome P450 (CYP) 1B1 and its role in polycyclic aromatic hydrocarbon-induced mitochondrial dysfunction
    • Bansal, S.; Leu, A.N.; Gonzalez, F.J.; Guengerich, F.P.; Chowdhury, A.R.; Anandatheerthavarada, H.K.; Avadhani, N.G. Mitochondrial targeting of cytochrome P450 (CYP) 1B1 and its role in polycyclic aromatic hydrocarbon-induced mitochondrial dysfunction. J. Biol. Chem. 2014, 289, 9936–9951.
    • (2014) J. Biol. Chem. , vol.289 , pp. 9936-9951
    • Bansal, S.1    Leu, A.N.2    Gonzalez, F.J.3    Guengerich, F.P.4    Chowdhury, A.R.5    Anandatheerthavarada, H.K.6    Avadhani, N.G.7
  • 83
    • 33751079125 scopus 로고    scopus 로고
    • Rat cytochrome P450 2C11 in liver microsomes involved in oxidation of anesthetic agent propofol and deactivated by prior treatment with propofol
    • Yamazaki, H.; Shimizu, M.; Nagashima, T.; Minoshima, M.; Murayama, N. Rat cytochrome P450 2C11 in liver microsomes involved in oxidation of anesthetic agent propofol and deactivated by prior treatment with propofol. Drug Metab. Dispos. 2006, 34, 1803–1805.
    • (2006) Drug Metab. Dispos , vol.34 , pp. 1803-1805
    • Yamazaki, H.1    Shimizu, M.2    Nagashima, T.3    Minoshima, M.4    Murayama, N.5
  • 84
    • 33947716119 scopus 로고    scopus 로고
    • Asemiempirical free energy force field with charge-based desolvation
    • Huey, R.; Morris, G.M.; Olson, A.J.; Goodsell, D.S. Asemiempirical free energy force field with charge-based desolvation. J. Comput. Chem. 2007, 28, 1145–1152.
    • (2007) J. Comput. Chem. , vol.28 , pp. 1145-1152
    • Huey, R.1    Morris, G.M.2    Olson, A.J.3    Goodsell, D.S.4
  • 86
    • 84893970694 scopus 로고    scopus 로고
    • Oxidation of carcinogenic benzo[a]pyrene by human and rat cytochrome P450 1A1 and its influencing by cytochrome b5—A comparative study
    • Indra, R.; M0oserova, M.; Sulc, M.; Frei, E.; Stiborova, M. Oxidation of carcinogenic benzo[a]pyrene by human and rat cytochrome P450 1A1 and its influencing by cytochrome b5—A comparative study. Neuro Endocrinol. Lett. 2014, 34, 55–63.
    • (2014) Neuro Endocrinol. Lett , vol.34 , pp. 55-63
    • Indra, R.1    M0oserova, M.2    Sulc, M.3    Frei, E.4    Stiborova, M.5
  • 87
    • 0023877690 scopus 로고
    • A new way to carcinogenicity of azo dyes: The benzenediazonium ion formed from a non-aminoazo dye, 1-phenylazo-2-hydroxynaphthalene (Sudan I) by microsomal enzymes binds to deoxyguanosine residues of DNA
    • Stiborová, M.; Asfaw, B.; Anzenbacher, P.; Hodek, P. A new way to carcinogenicity of azo dyes: The benzenediazonium ion formed from a non-aminoazo dye, 1-phenylazo-2-hydroxynaphthalene (Sudan I) by microsomal enzymes binds to deoxyguanosine residues of DNA. Cancer Lett. 1988, 40, 327–333.
    • (1988) Cancer Lett , vol.40 , pp. 327-333
    • Stiborová, M.1    Asfaw, B.2    Anzenbacher, P.3    Hodek, P.4
  • 88
    • 84877134071 scopus 로고    scopus 로고
    • Human cytochrome P450 1A1 structure and utility in understanding drug and xenobiotic metabolism
    • Walsh, A.A.; Szklarz, G.D.; Scott, E.E. Human cytochrome P450 1A1 structure and utility in understanding drug and xenobiotic metabolism. J. Biol. Chem. 2013, 288, 12932–12943.
    • (2013) J. Biol. Chem , vol.288 , pp. 12932-12943
    • Walsh, A.A.1    Szklarz, G.D.2    Scott, E.E.3
  • 89
    • 34347235844 scopus 로고    scopus 로고
    • Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2
    • Sansen, S.; Yano, J.K.; Reynald, R.L.; Schoch, G.A.; Griffin, K.J.; Stout, C.D.; Johnson, E.F. Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2. J. Biol. Chem. 2007, 282, 14348–14355.
    • (2007) J. Biol. Chem , vol.282 , pp. 14348-14355
    • Sansen, S.1    Yano, J.K.2    Reynald, R.L.3    Schoch, G.A.4    Griffin, K.J.5    Stout, C.D.6    Johnson, E.F.7
  • 90
    • 64849096515 scopus 로고    scopus 로고
    • Linear energy relationships for the octahedral preference of Mg, Ca and transition metal ions
    • Pontikis, G.; Borden, J.; Martínek, V.; Florián, J. Linear energy relationships for the octahedral preference of Mg, Ca and transition metal ions. J. Phys. Chem. 2009, 113, 3588–3593.
    • (2009) J. Phys. Chem. , vol.113 , pp. 3588-3593
    • Pontikis, G.1    Borden, J.2    Martínek, V.3    Florián, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.