메뉴 건너뛰기




Volumn 1850, Issue 11, 2015, Pages 2256-2264

Prooxidant and antioxidant properties of salicylaldehyde isonicotinoyl hydrazone iron chelators in HepG2 cells

Author keywords

Antioxidant; Glutathione; Iron; Nrf2; Oxidative stress; Salicylaldehyde isonicotinoyl hydrazone

Indexed keywords

BENZALDEHYDE ISONICOTINOYL HYDRAZONE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; IRON CHELATING AGENT; REACTIVE OXYGEN METABOLITE; SALICYLALDEHYDE ISONICOTINOYL HYDRAZONE; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG; ALDEHYDE; ANTIOXIDANT; HYDRAZONE DERIVATIVE; NFE2L2 PROTEIN, HUMAN;

EID: 84940507070     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2015.08.005     Document Type: Article
Times cited : (19)

References (41)
  • 1
    • 79251623137 scopus 로고    scopus 로고
    • Iron chelation with salicylaldehyde isonicotinoyl hydrazone protects against catecholamine autoxidation and cardiotoxicity
    • P. Hašková, P. Kovaříková, L. Koubková, A. Vávrová, E. Macková, and T. Šimůnek Iron chelation with salicylaldehyde isonicotinoyl hydrazone protects against catecholamine autoxidation and cardiotoxicity Free Radic. Biol. Med. 50 4 2011 537 549
    • (2011) Free Radic. Biol. Med. , vol.50 , Issue.4 , pp. 537-549
    • Hašková, P.1    Kovaříková, P.2    Koubková, L.3    Vávrová, A.4    Macková, E.5    Šimůnek, T.6
  • 2
    • 22244446427 scopus 로고    scopus 로고
    • SIH - a novel lipophilic iron chelator - protects H9c2 cardiomyoblasts from oxidative stress-induced mitochondrial injury and cell death
    • T. Šimůnek, C. Boer, R.A. Bouwman, R. Vlasblom, A.M. Versteilen, M. Štěrba, ..., and R.J. Musters SIH - a novel lipophilic iron chelator - protects H9c2 cardiomyoblasts from oxidative stress-induced mitochondrial injury and cell death J. Mol. Cell. Cardiol. 39 2 2005 345 354
    • (2005) J. Mol. Cell. Cardiol. , vol.39 , Issue.2 , pp. 345-354
    • Šimůnek, T.1    Boer, C.2    Bouwman, R.A.3    Vlasblom, R.4    Versteilen, A.M.5    Štěrba, M.6    Musters, R.J.7
  • 3
    • 79952917106 scopus 로고    scopus 로고
    • Synthesis and initial in vitro evaluations of novel antioxidant aroylhydrazone iron chelators with increased stability against plasma hydrolysis
    • K. Hruskova, P. Kovarikova, P. Bendova, P. Haskova, E. Mackova, J. Stariat, ..., and T. Simunek Synthesis and initial in vitro evaluations of novel antioxidant aroylhydrazone iron chelators with increased stability against plasma hydrolysis Chem. Res. Toxicol. 24 3 2011 290 302
    • (2011) Chem. Res. Toxicol. , vol.24 , Issue.3 , pp. 290-302
    • Hruskova, K.1    Kovarikova, P.2    Bendova, P.3    Haskova, P.4    Mackova, E.5    Stariat, J.6    Simunek, T.7
  • 5
    • 55349103367 scopus 로고    scopus 로고
    • Iron prochelator BSIH protects retinal pigment epithelial cells against cell death induced by hydrogen peroxide
    • L.K. Charkoudian, T. Dentchev, N. Lukinova, N. Wolkow, J.L. Dunaief, and K.J. Franz Iron prochelator BSIH protects retinal pigment epithelial cells against cell death induced by hydrogen peroxide J. Inorg. Biochem. 102 12 2008 2130 2135
    • (2008) J. Inorg. Biochem. , vol.102 , Issue.12 , pp. 2130-2135
    • Charkoudian, L.K.1    Dentchev, T.2    Lukinova, N.3    Wolkow, N.4    Dunaief, J.L.5    Franz, K.J.6
  • 6
    • 50249149460 scopus 로고    scopus 로고
    • Anthracycline toxicity to cardiomyocytes or cancer cells is differently affected by iron chelation with salicylaldehyde isonicotinoyl hydrazone
    • T. Šimůnek, M. Štěrba, O. Popelova, H. Kaiserova, M. Adamcova, M. Hroch, ..., and V. Geršl Anthracycline toxicity to cardiomyocytes or cancer cells is differently affected by iron chelation with salicylaldehyde isonicotinoyl hydrazone Br. J. Pharmacol. 155 1 2008 138 148
    • (2008) Br. J. Pharmacol. , vol.155 , Issue.1 , pp. 138-148
    • Šimůnek, T.1    Štěrba, M.2    Popelova, O.3    Kaiserova, H.4    Adamcova, M.5    Hroch, M.6    Geršl, V.7
  • 7
    • 0037108199 scopus 로고    scopus 로고
    • The labile iron pool: characterization, measurement, and participation in cellular processes
    • O. Kakhlon, and Z.I. Cabantchik The labile iron pool: characterization, measurement, and participation in cellular processes Free Radic. Biol. Med. 33 8 2002 1037 1046
    • (2002) Free Radic. Biol. Med. , vol.33 , Issue.8 , pp. 1037-1046
    • Kakhlon, O.1    Cabantchik, Z.I.2
  • 8
    • 1942424159 scopus 로고    scopus 로고
    • Antioxidant properties of S-adenosyl-l-methionine in Fe 2 + - initiated oxidations
    • A.A. Caro, and A.I. Cederbaum Antioxidant properties of S-adenosyl-l-methionine in Fe 2 + - initiated oxidations Free Radic. Biol. Med. 36 10 2004 1303 1316
    • (2004) Free Radic. Biol. Med. , vol.36 , Issue.10 , pp. 1303-1316
    • Caro, A.A.1    Cederbaum, A.I.2
  • 9
    • 77953792874 scopus 로고    scopus 로고
    • Comparison of clinically used and experimental iron chelators for protection against oxidative stress-induced cellular injury
    • P. Bendova, E. Mackova, P. Haskova, A. Vavrova, E. Jirkovsky, M. Sterba, ..., and T. Simunek Comparison of clinically used and experimental iron chelators for protection against oxidative stress-induced cellular injury Chem. Res. Toxicol. 23 6 2010 1105 1114
    • (2010) Chem. Res. Toxicol. , vol.23 , Issue.6 , pp. 1105-1114
    • Bendova, P.1    Mackova, E.2    Haskova, P.3    Vavrova, A.4    Jirkovsky, E.5    Sterba, M.6    Simunek, T.7
  • 10
    • 84906351146 scopus 로고    scopus 로고
    • Comparison of food antioxidants and iron chelators in two cellular free radical assays: strong protection by luteolin
    • T. Hofer, T.Ø. Jørgensen, and R.L. Olsen Comparison of food antioxidants and iron chelators in two cellular free radical assays: strong protection by luteolin J. Agric. Food Chem. 62 33 2014 8402 8410
    • (2014) J. Agric. Food Chem. , vol.62 , Issue.33 , pp. 8402-8410
    • Hofer, T.1    Jørgensen T.Ø.2    Olsen, R.L.3
  • 11
    • 0347479372 scopus 로고    scopus 로고
    • Oxidative stress mediates toxicity of pyridoxal isonicotinoyl hydrazone analogs
    • J.L. Buss, J. Neuzil, and P. Ponka Oxidative stress mediates toxicity of pyridoxal isonicotinoyl hydrazone analogs Arch. Biochem. Biophys. 421 1 2004 1 9
    • (2004) Arch. Biochem. Biophys. , vol.421 , Issue.1 , pp. 1-9
    • Buss, J.L.1    Neuzil, J.2    Ponka, P.3
  • 12
    • 27644539382 scopus 로고    scopus 로고
    • Intracellular labile iron pools as direct targets of iron chelators: a fluorescence study of chelator action in living cells
    • H. Glickstein, R.B. El, M. Shvartsman, and Z.I. Cabantchik Intracellular labile iron pools as direct targets of iron chelators: a fluorescence study of chelator action in living cells Blood 106 9 2005 3242 3250
    • (2005) Blood , vol.106 , Issue.9 , pp. 3242-3250
    • Glickstein, H.1    El, R.B.2    Shvartsman, M.3    Cabantchik, Z.I.4
  • 14
    • 0035950067 scopus 로고    scopus 로고
    • N-Succinyl-(β-alanyl-l-leucyl-l-alanyl-l-leucyl) doxorubicin: an extracellularly tumor-activated prodrug devoid of intravenous acute toxicity
    • A.M. Fernandez, K. Van derpoorten, L. Dasnois, K. Lebtahi, V. Dubois, T.J. Lobl, ..., and A. Trouet N-Succinyl-(β-alanyl-l-leucyl-l-alanyl-l-leucyl) doxorubicin: an extracellularly tumor-activated prodrug devoid of intravenous acute toxicity J. Med. Chem. 44 22 2001 3750 3753
    • (2001) J. Med. Chem. , vol.44 , Issue.22 , pp. 3750-3753
    • Fernandez, A.M.1    Van Derpoorten, K.2    Dasnois, L.3    Lebtahi, K.4    Dubois, V.5    Lobl, T.J.6    Trouet, A.7
  • 15
    • 33749186347 scopus 로고    scopus 로고
    • A pro-chelator triggered by hydrogen peroxide inhibits iron-promoted hydroxyl radical formation
    • L.K. Charkoudian, D.M. Pham, and K.J. Franz A pro-chelator triggered by hydrogen peroxide inhibits iron-promoted hydroxyl radical formation J. Am. Chem. Soc. 128 38 2006 12424 12425
    • (2006) J. Am. Chem. Soc. , vol.128 , Issue.38 , pp. 12424-12425
    • Charkoudian, L.K.1    Pham, D.M.2    Franz, K.J.3
  • 16
    • 35548949315 scopus 로고    scopus 로고
    • Modifications of boronic ester pro-chelators triggered by hydrogen peroxide tune reactivity to inhibit metal-promoted oxidative stress
    • L.K. Charkoudian, D.M. Pham, A.M. Kwon, A.D. Vangeloff, and K.J. Franz Modifications of boronic ester pro-chelators triggered by hydrogen peroxide tune reactivity to inhibit metal-promoted oxidative stress Dalton Trans. 43 2007 5031 5042
    • (2007) Dalton Trans. , vol.43 , pp. 5031-5042
    • Charkoudian, L.K.1    Pham, D.M.2    Kwon, A.M.3    Vangeloff, A.D.4    Franz, K.J.5
  • 18
    • 0037020091 scopus 로고    scopus 로고
    • Iron detoxification properties of escherichia colibacterioferritin attenuation of oxyradical chemistry
    • F. Bou-Abdallah, A.C. Lewin, N.E. Le Brun, G.R. Moore, and N.D. Chasteen Iron detoxification properties of escherichia colibacterioferritin attenuation of oxyradical chemistry J. Biol. Chem. 277 40 2002 37064 37069
    • (2002) J. Biol. Chem. , vol.277 , Issue.40 , pp. 37064-37069
    • Bou-Abdallah, F.1    Lewin, A.C.2    Le Brun, N.E.3    Moore, G.R.4    Chasteen, N.D.5
  • 19
    • 0036882156 scopus 로고    scopus 로고
    • Ca 2 + - dependent and independent mitochondrial damage in HepG2 cells that overexpress CYP2E1
    • A.A. Caro, and A.I. Cederbaum Ca 2 + - dependent and independent mitochondrial damage in HepG2 cells that overexpress CYP2E1 Arch. Biochem. Biophys. 408 2 2002 162 170
    • (2002) Arch. Biochem. Biophys. , vol.408 , Issue.2 , pp. 162-170
    • Caro, A.A.1    Cederbaum, A.I.2
  • 20
    • 0037016768 scopus 로고    scopus 로고
    • Role of calcium and calcium-activated proteases in CYP2E1-dependent toxicity in HEPG2 cells
    • A.A. Caro, and A.I. Cederbaum Role of calcium and calcium-activated proteases in CYP2E1-dependent toxicity in HEPG2 cells J. Biol. Chem. 277 1 2002 104 113
    • (2002) J. Biol. Chem. , vol.277 , Issue.1 , pp. 104-113
    • Caro, A.A.1    Cederbaum, A.I.2
  • 21
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues
    • F. Tietze Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues Anal. Biochem. 27 3 1969 502 522
    • (1969) Anal. Biochem. , vol.27 , Issue.3 , pp. 502-522
    • Tietze, F.1
  • 22
    • 0034685775 scopus 로고    scopus 로고
    • CYP2E1 overexpression in HepG2 cells induces glutathione synthesis by transcriptional activation of γ-glutamylcysteine synthetase
    • M. Marí, and A.I. Cederbaum CYP2E1 overexpression in HepG2 cells induces glutathione synthesis by transcriptional activation of γ-glutamylcysteine synthetase J. Biol. Chem. 275 20 2000 15563 15571
    • (2000) J. Biol. Chem. , vol.275 , Issue.20 , pp. 15563-15571
    • Marí, M.1    Cederbaum, A.I.2
  • 23
    • 32844456005 scopus 로고    scopus 로고
    • Docosahexaenoic acid enhances the antioxidant response of human fibroblasts by upregulating γ-glutamyl-cysteinyl ligase and glutathione reductase
    • K. Arab, A. Rossary, F. Flourié, Y. Tourneur, and J.P. Steghens Docosahexaenoic acid enhances the antioxidant response of human fibroblasts by upregulating γ-glutamyl-cysteinyl ligase and glutathione reductase Br. J. Nutr. 95 01 2006 18 26
    • (2006) Br. J. Nutr. , vol.95 , Issue.1 , pp. 18-26
    • Arab, K.1    Rossary, A.2    Flourié, F.3    Tourneur, Y.4    Steghens, J.P.5
  • 24
    • 0032951707 scopus 로고    scopus 로고
    • Determination of the chelatable iron pool of isolated rat hepatocytes by digital fluorescence microscopy using the fluorescent probe, phen green SK
    • F. Petrat, U. Rauen, and H. de Groot Determination of the chelatable iron pool of isolated rat hepatocytes by digital fluorescence microscopy using the fluorescent probe, phen green SK Hepatology 29 4 1999 1171 1179
    • (1999) Hepatology , vol.29 , Issue.4 , pp. 1171-1179
    • Petrat, F.1    Rauen, U.2    De Groot, H.3
  • 25
  • 26
    • 0033045404 scopus 로고    scopus 로고
    • Iron and dioxygen chemistry is an important route to initiation of biological free radical oxidations: an electron paramagnetic resonance spin trapping study
    • S.Y. Qian, and G.R. Buettner Iron and dioxygen chemistry is an important route to initiation of biological free radical oxidations: an electron paramagnetic resonance spin trapping study Free Radic. Biol. Med. 26 11 1999 1447 1456
    • (1999) Free Radic. Biol. Med. , vol.26 , Issue.11 , pp. 1447-1456
    • Qian, S.Y.1    Buettner, G.R.2
  • 27
    • 0036138979 scopus 로고    scopus 로고
    • Ferrous ion autoxidation and its chelation in iron-loaded human liver HepG2 cells
    • X. Huang, J. Dai, J. Fournier, A.M. Ali, Q. Zhang, and K. Frenkel Ferrous ion autoxidation and its chelation in iron-loaded human liver HepG2 cells Free Radic. Biol. Med. 32 1 2002 84 92
    • (2002) Free Radic. Biol. Med. , vol.32 , Issue.1 , pp. 84-92
    • Huang, X.1    Dai, J.2    Fournier, J.3    Ali, A.M.4    Zhang, Q.5    Frenkel, K.6
  • 28
    • 0031744631 scopus 로고    scopus 로고
    • The labile iron pool in hepatocytes: prooxidant-induced increase in free iron precedes oxidative cell injury
    • A. Stäubli, and U.A. Boelsterli The labile iron pool in hepatocytes: prooxidant-induced increase in free iron precedes oxidative cell injury Am. J. Physiol. Gastrointest. Liver Physiol. 274 6 1998 G1031 G1037
    • (1998) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.274 , Issue.6 , pp. G1031-G1037
    • Stäubli, A.1    Boelsterli, U.A.2
  • 29
    • 0037082130 scopus 로고    scopus 로고
    • Iron autoxidation and free radical generation: effects of buffers, ligands, and chelators
    • K.D. Welch, T.Z. Davis, and S.D. Aust Iron autoxidation and free radical generation: effects of buffers, ligands, and chelators Arch. Biochem. Biophys. 397 2 2002 360 369
    • (2002) Arch. Biochem. Biophys. , vol.397 , Issue.2 , pp. 360-369
    • Welch, K.D.1    Davis, T.Z.2    Aust, S.D.3
  • 30
    • 26644449682 scopus 로고    scopus 로고
    • Glutamate Cysteine ligase catalysis dependence on ATP and modifier subunit for regulation of tissue glutathione levels
    • Y. Chen, H.G. Shertzer, S.N. Schneider, D.W. Nebert, and T.P. Dalton Glutamate Cysteine ligase catalysis dependence on ATP and modifier subunit for regulation of tissue glutathione levels J. Biol. Chem. 280 40 2005 33766 33774
    • (2005) J. Biol. Chem. , vol.280 , Issue.40 , pp. 33766-33774
    • Chen, Y.1    Shertzer, H.G.2    Schneider, S.N.3    Nebert, D.W.4    Dalton, T.P.5
  • 31
    • 70249087960 scopus 로고    scopus 로고
    • The role of c-Jun phosphorylation in EpRE activation of phase II genes
    • S. Levy, A.K. Jaiswal, and H.J. Forman The role of c-Jun phosphorylation in EpRE activation of phase II genes Free Radic. Biol. Med. 47 8 2009 1172 1179
    • (2009) Free Radic. Biol. Med. , vol.47 , Issue.8 , pp. 1172-1179
    • Levy, S.1    Jaiswal, A.K.2    Forman, H.J.3
  • 32
    • 84869043780 scopus 로고    scopus 로고
    • The predicted molecular weight of Nrf2: it is what it is not
    • A. Lau, W. Tian, S.A. Whitman, and D.D. Zhang The predicted molecular weight of Nrf2: it is what it is not Antioxid. Redox Signal. 18 1 2013 91 93
    • (2013) Antioxid. Redox Signal. , vol.18 , Issue.1 , pp. 91-93
    • Lau, A.1    Tian, W.2    Whitman, S.A.3    Zhang, D.D.4
  • 36
    • 84870445676 scopus 로고    scopus 로고
    • Docosahexaenoic acid inhibition of inflammation is partially via cross-talk between Nrf2/heme oxygenase 1 and IKK/NF-κB pathways
    • Y.C. Yang, C.K. Lii, Y.L. Wei, C.C. Li, C.Y. Lu, K.L. Liu, and H.W. Chen Docosahexaenoic acid inhibition of inflammation is partially via cross-talk between Nrf2/heme oxygenase 1 and IKK/NF-κB pathways J. Nutr. Biochem. 24 1 2013 204 212
    • (2013) J. Nutr. Biochem. , vol.24 , Issue.1 , pp. 204-212
    • Yang, Y.C.1    Lii, C.K.2    Wei, Y.L.3    Li, C.C.4    Lu, C.Y.5    Liu, K.L.6    Chen, H.W.7
  • 38
    • 37549066891 scopus 로고    scopus 로고
    • Antioxidants as potential therapeutics for lung fibrosis
    • B.J. Day Antioxidants as potential therapeutics for lung fibrosis Antioxid. Redox Signal. 10 2 2008 355 370
    • (2008) Antioxid. Redox Signal. , vol.10 , Issue.2 , pp. 355-370
    • Day, B.J.1
  • 40
    • 77951046942 scopus 로고    scopus 로고
    • Targeting iron homeostasis induces cellular differentiation and synergizes with differentiating agents in acute myeloid leukemia
    • C. Callens, S. Coulon, J. Naudin, I. Radford-Weiss, N. Boissel, E. Raffoux, ..., and O. Hermine Targeting iron homeostasis induces cellular differentiation and synergizes with differentiating agents in acute myeloid leukemia J. Exp. Med. 207 4 2010 731 750
    • (2010) J. Exp. Med. , vol.207 , Issue.4 , pp. 731-750
    • Callens, C.1    Coulon, S.2    Naudin, J.3    Radford-Weiss, I.4    Boissel, N.5    Raffoux, E.6    Hermine, O.7
  • 41
    • 79651473123 scopus 로고    scopus 로고
    • The iron-chelating drug triapine causes pronounced mitochondrial thiol redox stress
    • J.M. Myers, W.E. Antholine, J. Zielonka, and C.R. Myers The iron-chelating drug triapine causes pronounced mitochondrial thiol redox stress Toxicol. Lett. 201 2 2011 130 136
    • (2011) Toxicol. Lett. , vol.201 , Issue.2 , pp. 130-136
    • Myers, J.M.1    Antholine, W.E.2    Zielonka, J.3    Myers, C.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.