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Volumn 28, Issue 4, 2014, Pages 707-714

Aldo-keto reductase 7A5 (AKR7A5) attenuates oxidative stress and reactive aldehyde toxicity in V79-4 cells

Author keywords

Aldehydes; Aldoketo reductase 7A5; Hydrogen peroxide; Menadione; Oxidative stress

Indexed keywords

ALDEHYDE; ALDEHYDE DERIVATIVE; ALDO KETO REDUCTASE; ALDO KETO REDUCTASE 7A5; GLUTATHIONE; HEXANAL; HYDROGEN PEROXIDE; MENADIONE; METHYLGLYOXAL; OXIDOREDUCTASE; REACTIVE ALDEHYDE; REACTIVE OXYGEN METABOLITE; TRANS 2 NONENAL; UNCLASSIFIED DRUG; ALDEHYDE REDUCTASE; BENZALDEHYDE; BENZALDEHYDE DERIVATIVE; CARBONYL REDUCTASE;

EID: 84896274841     PISSN: 08872333     EISSN: 18793177     Source Type: Journal    
DOI: 10.1016/j.tiv.2014.02.010     Document Type: Article
Times cited : (21)

References (45)
  • 1
    • 80053305353 scopus 로고    scopus 로고
    • Aldo-keto reductase-7A protects liver cells and tissues from acetaminophen-induced oxidative stress and hepatotoxicity
    • Ahmed M.M., Wang T., Luo Y., Ye S., Wu Q., Guo Z., Roebuck B.D., Sutter T.R., Yang J.Y. Aldo-keto reductase-7A protects liver cells and tissues from acetaminophen-induced oxidative stress and hepatotoxicity. Hepatology 2011, 54:1322-1332.
    • (2011) Hepatology , vol.54 , pp. 1322-1332
    • Ahmed, M.M.1    Wang, T.2    Luo, Y.3    Ye, S.4    Wu, Q.5    Guo, Z.6    Roebuck, B.D.7    Sutter, T.R.8    Yang, J.Y.9
  • 2
    • 0035003926 scopus 로고    scopus 로고
    • DNA-protein crosslink and DNA strand break formation in HL-60 cells treated with trans, trans-muconaldehyde, hydroquinone and their mixtures
    • Amin R.P., Witz G. DNA-protein crosslink and DNA strand break formation in HL-60 cells treated with trans, trans-muconaldehyde, hydroquinone and their mixtures. Int. J. Toxicol. 2001, 20:69-80.
    • (2001) Int. J. Toxicol. , vol.20 , pp. 69-80
    • Amin, R.P.1    Witz, G.2
  • 4
    • 54549110136 scopus 로고    scopus 로고
    • The aldo-keto reductase superfamily and its role in drug metabolism and detoxification
    • Barski O.A., Tipparaju S.M., Bhatnagar A. The aldo-keto reductase superfamily and its role in drug metabolism and detoxification. Drug Metab. Rev. 2008, 40:553-624.
    • (2008) Drug Metab. Rev. , vol.40 , pp. 553-624
    • Barski, O.A.1    Tipparaju, S.M.2    Bhatnagar, A.3
  • 6
    • 23144448354 scopus 로고    scopus 로고
    • DNA adducts from acetaldehyde: implications for alcohol-related carcinogenesis
    • Brooks P.J., Theruvathu J.A. DNA adducts from acetaldehyde: implications for alcohol-related carcinogenesis. Alcohol 2005, 35:187-193.
    • (2005) Alcohol , vol.35 , pp. 187-193
    • Brooks, P.J.1    Theruvathu, J.A.2
  • 8
    • 34250864375 scopus 로고    scopus 로고
    • Reactive carbonyls and oxidative stress: potential for therapeutic intervention
    • Ellis E.M. Reactive carbonyls and oxidative stress: potential for therapeutic intervention. Pharmacol. Ther. 2007, 115:13-24.
    • (2007) Pharmacol. Ther. , vol.115 , pp. 13-24
    • Ellis, E.M.1
  • 9
    • 0029564152 scopus 로고
    • Substrate-specificity of an aflatoxin-metabolizing aldehyde reductase
    • Ellis E.M., Hayes J.D. Substrate-specificity of an aflatoxin-metabolizing aldehyde reductase. Biochem. J. 1995, 312:535-541.
    • (1995) Biochem. J. , vol.312 , pp. 535-541
    • Ellis, E.M.1    Hayes, J.D.2
  • 10
    • 0027381443 scopus 로고
    • An ethoxyquin-inducible aldehyde reductase from rat liver that metabolises aflatoxin B1 defines a subfammily of aldo-keto reductases
    • Ellis E.M., Judah D.J., Neal G.E., Hayes J.D. An ethoxyquin-inducible aldehyde reductase from rat liver that metabolises aflatoxin B1 defines a subfammily of aldo-keto reductases. Proc. Natl. Acad. Sci. USA 1993, 90:10350-10354.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10350-10354
    • Ellis, E.M.1    Judah, D.J.2    Neal, G.E.3    Hayes, J.D.4
  • 13
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H., Schaur R.J., Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 1991, 11:81-128.
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 14
    • 84869076150 scopus 로고    scopus 로고
    • Synthetic pyrethroid increases lipid and protein oxidation and induces glutathione depletion in the cerebellum of adult rats: ameliorative effect of vitamin C
    • Fetoui H., Gdoura R. Synthetic pyrethroid increases lipid and protein oxidation and induces glutathione depletion in the cerebellum of adult rats: ameliorative effect of vitamin C. Hum. Exp. Toxicol 2012.
    • (2012) Hum. Exp. Toxicol
    • Fetoui, H.1    Gdoura, R.2
  • 15
    • 36048944481 scopus 로고    scopus 로고
    • Transfection of HepG2 cells with hGSTA4 provides protection against 4-hydroxynonenal-mediated oxidative injury
    • Gallagher E.P., Huisden C.M., Gardner J.L. Transfection of HepG2 cells with hGSTA4 provides protection against 4-hydroxynonenal-mediated oxidative injury. Toxicol. In Vitro 2007, 21:1365-1372.
    • (2007) Toxicol. In Vitro , vol.21 , pp. 1365-1372
    • Gallagher, E.P.1    Huisden, C.M.2    Gardner, J.L.3
  • 16
    • 1442331950 scopus 로고    scopus 로고
    • Detoxication of the environmental pollutant acrolein by a rat liver aldo-keto reductase
    • Gardner R., Kazi S., Ellis E. Detoxication of the environmental pollutant acrolein by a rat liver aldo-keto reductase. Toxicol. Lett. 2004, 148:65-72.
    • (2004) Toxicol. Lett. , vol.148 , pp. 65-72
    • Gardner, R.1    Kazi, S.2    Ellis, E.3
  • 17
    • 73449129394 scopus 로고    scopus 로고
    • Hydrogen peroxide as a cell-survival signaling molecule
    • Groeger G., Quiney C., Cotter T.G. Hydrogen peroxide as a cell-survival signaling molecule. Antioxid. Redox Signal. 2009, 11:2655-2671.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2655-2671
    • Groeger, G.1    Quiney, C.2    Cotter, T.G.3
  • 18
    • 0037125225 scopus 로고    scopus 로고
    • Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
    • Hinshelwood A., McGarvie G., Ellis E. Characterisation of a novel mouse liver aldo-keto reductase AKR7A5. FEBS Lett. 2002, 523:213-218.
    • (2002) FEBS Lett. , vol.523 , pp. 213-218
    • Hinshelwood, A.1    McGarvie, G.2    Ellis, E.3
  • 19
  • 20
    • 0017064979 scopus 로고
    • A fluorometric method for determination of oxidized and reduced glutathione in tissues
    • Hissin P.J., Hilf R. A fluorometric method for determination of oxidized and reduced glutathione in tissues. Anal. Biochem. 1976, 74:214-226.
    • (1976) Anal. Biochem. , vol.74 , pp. 214-226
    • Hissin, P.J.1    Hilf, R.2
  • 22
    • 0032524187 scopus 로고    scopus 로고
    • Molecular cloning, expression and catalytic activity of a human AKR7 member of the aldo-keto reductase superfamily: evidence that the major 2-carboxybenzaldehyde reductase from human liver is a homologue of rat aflatoxin B1-aldehyde reductase
    • Ireland L.S., Harrison D.J., Neal G.E., Hayes J.D. Molecular cloning, expression and catalytic activity of a human AKR7 member of the aldo-keto reductase superfamily: evidence that the major 2-carboxybenzaldehyde reductase from human liver is a homologue of rat aflatoxin B1-aldehyde reductase. Biochem. J. 1998, 332(Pt 1):21-34.
    • (1998) Biochem. J. , vol.332 , Issue.PART 1 , pp. 21-34
    • Ireland, L.S.1    Harrison, D.J.2    Neal, G.E.3    Hayes, J.D.4
  • 23
    • 0035969891 scopus 로고    scopus 로고
    • The aldo-keto reductase superfamily: an update
    • Jez J., Penning T. The aldo-keto reductase superfamily: an update. Chemico-biol. Interact. 2001, 130-132:499-525.
    • (2001) Chemico-biol. Interact. , pp. 499-525
    • Jez, J.1    Penning, T.2
  • 24
    • 33847021147 scopus 로고    scopus 로고
    • Aldo-keto reductases and bioactivation/detoxication
    • Jin Y., Penning T.M. Aldo-keto reductases and bioactivation/detoxication. Annu. Rev. Pharmacol. Toxicol. 2007, 47:263-292.
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 263-292
    • Jin, Y.1    Penning, T.M.2
  • 25
    • 84873443918 scopus 로고    scopus 로고
    • Identification of aldo-keto reductases as NRF2-target marker genes in human cells
    • Jung K.A., Choi B.H., Nam C.W., Song M., Kim S.T., Lee J.Y., Kwak M.K. Identification of aldo-keto reductases as NRF2-target marker genes in human cells. Toxicol. Lett. 2013, 218:39-49.
    • (2013) Toxicol. Lett. , vol.218 , pp. 39-49
    • Jung, K.A.1    Choi, B.H.2    Nam, C.W.3    Song, M.4    Kim, S.T.5    Lee, J.Y.6    Kwak, M.K.7
  • 26
    • 84863442754 scopus 로고    scopus 로고
    • Literature review of the role of hydroxyl radicals in chemically-induced mutagenicity and carcinogenicity for the risk assessment of a disinfection system utilizing photolysis of hydrogen peroxide
    • Kanno T., Nakamura K., Ikai H., Kikuchi K., Sasaki K., Niwano Y. Literature review of the role of hydroxyl radicals in chemically-induced mutagenicity and carcinogenicity for the risk assessment of a disinfection system utilizing photolysis of hydrogen peroxide. J. Clin. Biochem. Nutr. 2012, 51:9-14.
    • (2012) J. Clin. Biochem. Nutr. , vol.51 , pp. 9-14
    • Kanno, T.1    Nakamura, K.2    Ikai, H.3    Kikuchi, K.4    Sasaki, K.5    Niwano, Y.6
  • 27
    • 0037106619 scopus 로고    scopus 로고
    • Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate synthases that associate with the Golgi apparatus define a distinct subclass of aldo-keto reductase 7 family proteins
    • Kelly V.P., Sherratt P.J., Crouch D.H., Hayes J.D. Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate synthases that associate with the Golgi apparatus define a distinct subclass of aldo-keto reductase 7 family proteins. Biochem. J. 2002, 366:847-861.
    • (2002) Biochem. J. , vol.366 , pp. 847-861
    • Kelly, V.P.1    Sherratt, P.J.2    Crouch, D.H.3    Hayes, J.D.4
  • 28
    • 0032814943 scopus 로고    scopus 로고
    • CDNA cloning, expression and activity of a second human aflatoxin B1-metabolizing member of the aldo-keto reductase superfamily, AKR7A3
    • Knight L.P., Primiano T., Groopman J.D., Kensler T.W., Sutter T.R. cDNA cloning, expression and activity of a second human aflatoxin B1-metabolizing member of the aldo-keto reductase superfamily, AKR7A3. Carcinogenesis 1999, 20:1215-1223.
    • (1999) Carcinogenesis , vol.20 , pp. 1215-1223
    • Knight, L.P.1    Primiano, T.2    Groopman, J.D.3    Kensler, T.W.4    Sutter, T.R.5
  • 29
    • 84867234457 scopus 로고    scopus 로고
    • Inducible protection of human astrocytoma 1321N1 cells against hydrogen peroxide and aldehyde toxicity by 7-hydroxycoumarin is associated with the upregulation of aldo-keto reductases
    • Li D., Ellis E.M. Inducible protection of human astrocytoma 1321N1 cells against hydrogen peroxide and aldehyde toxicity by 7-hydroxycoumarin is associated with the upregulation of aldo-keto reductases. Neurotoxicology 2012, 33:1368-1374.
    • (2012) Neurotoxicology , vol.33 , pp. 1368-1374
    • Li, D.1    Ellis, E.M.2
  • 30
    • 33748640611 scopus 로고    scopus 로고
    • Mouse aldo-keto reductase AKR7A5 protects V79 cells against 4-hydroxynonenal-induced apoptosis
    • Li D., Hinshelwood A., Gardner R., McGarvie G., Ellis E.M. Mouse aldo-keto reductase AKR7A5 protects V79 cells against 4-hydroxynonenal-induced apoptosis. Toxicology 2006, 226:172-180.
    • (2006) Toxicology , vol.226 , pp. 172-180
    • Li, D.1    Hinshelwood, A.2    Gardner, R.3    McGarvie, G.4    Ellis, E.M.5
  • 31
    • 82055200076 scopus 로고    scopus 로고
    • Human aldo--keto reductase AKR7A2 protects against the cytotoxicity and mutagenicity of reactive aldehydes and lowers intracellular reactive oxygen species in hamster V79-4 cells
    • Li D., Ferrari M., Ellis E.M. Human aldo--keto reductase AKR7A2 protects against the cytotoxicity and mutagenicity of reactive aldehydes and lowers intracellular reactive oxygen species in hamster V79-4 cells. Chem. Biol. Interact. 2012, 195:25-34.
    • (2012) Chem. Biol. Interact. , vol.195 , pp. 25-34
    • Li, D.1    Ferrari, M.2    Ellis, E.M.3
  • 32
    • 84871716357 scopus 로고    scopus 로고
    • Aldo-keto reductases mediate constitutive and inducible protection against aldehyde toxicity in human neuroblastoma SH-SY5Y cells
    • Lyon R.C., Li D., McGarvie G., Ellis E.M. Aldo-keto reductases mediate constitutive and inducible protection against aldehyde toxicity in human neuroblastoma SH-SY5Y cells. Neurochem. Int. 2013, 62:113-121.
    • (2013) Neurochem. Int. , vol.62 , pp. 113-121
    • Lyon, R.C.1    Li, D.2    McGarvie, G.3    Ellis, E.M.4
  • 33
    • 77957145640 scopus 로고    scopus 로고
    • Molecular characterization, expression analysis, and role of ALDH3B1 in the cellular protection against oxidative stress
    • Marchitti S.A., Brocker C., Orlicky D.J., Vasiliou V. Molecular characterization, expression analysis, and role of ALDH3B1 in the cellular protection against oxidative stress. Free Radic. Biol. Med. 2010, 49:1432-1443.
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 1432-1443
    • Marchitti, S.A.1    Brocker, C.2    Orlicky, D.J.3    Vasiliou, V.4
  • 34
    • 70350787143 scopus 로고    scopus 로고
    • Aldo-keto reductase (AKR) superfamily: genomics and annotation
    • Mindnich R.D., Penning T.M. Aldo-keto reductase (AKR) superfamily: genomics and annotation. Hum. Genomics 2009, 3:362-370.
    • (2009) Hum. Genomics , vol.3 , pp. 362-370
    • Mindnich, R.D.1    Penning, T.M.2
  • 35
    • 0030591438 scopus 로고    scopus 로고
    • Cytotoxic and chemotactic potencies of several aldehydic components of oxidised low density lipoprotein for human monocyte-macrophages
    • Muller K., Hardwick S.J., Marchant C.E., Law N.S., Waeg G., Esterbauer H., Carpenter K.L., Mitchinson M.J. Cytotoxic and chemotactic potencies of several aldehydic components of oxidised low density lipoprotein for human monocyte-macrophages. FEBS Lett. 1996, 388:165-168.
    • (1996) FEBS Lett. , vol.388 , pp. 165-168
    • Muller, K.1    Hardwick, S.J.2    Marchant, C.E.3    Law, N.S.4    Waeg, G.5    Esterbauer, H.6    Carpenter, K.L.7    Mitchinson, M.J.8
  • 38
    • 0043172509 scopus 로고    scopus 로고
    • Basic aspects of the biochemical reactivity of 4-hydroxynonenal
    • Schaur R.J. Basic aspects of the biochemical reactivity of 4-hydroxynonenal. Mol. Aspects Med. 2003, 24:149-159.
    • (2003) Mol. Aspects Med. , vol.24 , pp. 149-159
    • Schaur, R.J.1
  • 39
    • 34547675729 scopus 로고    scopus 로고
    • Effects of 4-hydroxy-2-nonenal, a marker of oxidative stress, on spermatogenesis and expression of p53 protein in male infertility
    • discussion 1017
    • Shiraishi K., Naito K. Effects of 4-hydroxy-2-nonenal, a marker of oxidative stress, on spermatogenesis and expression of p53 protein in male infertility. J. Urol. 2007, 178:1012-1017. discussion 1017.
    • (2007) J. Urol. , vol.178 , pp. 1012-1017
    • Shiraishi, K.1    Naito, K.2
  • 40
    • 84884901013 scopus 로고    scopus 로고
    • Lipid peroxidation triggers neurodegeneration: a redox proteomics view into the Alzheimer disease brain
    • Sultana R., Perluigi M., Allan Butterfield D. Lipid peroxidation triggers neurodegeneration: a redox proteomics view into the Alzheimer disease brain. Free Radic. Biol. Med 2012.
    • (2012) Free Radic. Biol. Med
    • Sultana, R.1    Perluigi, M.2    Allan Butterfield, D.3
  • 41
    • 3042795659 scopus 로고    scopus 로고
    • Emission of hexanal and carbon monoxide from storage of wood pellets, a potential occupational and domestic health hazard
    • Svedberg U.R., Hogberg H.E., Hogberg J., Galle B. Emission of hexanal and carbon monoxide from storage of wood pellets, a potential occupational and domestic health hazard. Ann. Occup. Hyg. 2004, 48:339-349.
    • (2004) Ann. Occup. Hyg. , vol.48 , pp. 339-349
    • Svedberg, U.R.1    Hogberg, H.E.2    Hogberg, J.3    Galle, B.4
  • 42
    • 79958238542 scopus 로고    scopus 로고
    • Hydrogen peroxide as a signaling molecule
    • Veal E., Day A. Hydrogen peroxide as a signaling molecule. Antioxid. Redox Signal. 2011, 15:147-151.
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 147-151
    • Veal, E.1    Day, A.2
  • 43
    • 0032820452 scopus 로고    scopus 로고
    • Quantifying cellular oxidative stress by dichlorofluorescein assay using microplate reader
    • Wang H., Joseph J.A. Quantifying cellular oxidative stress by dichlorofluorescein assay using microplate reader. Free Radic. Biol. Med. 1999, 27:612-616.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 612-616
    • Wang, H.1    Joseph, J.A.2
  • 44
    • 33744935554 scopus 로고    scopus 로고
    • Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in mild cognitive impairment and early Alzheimer's disease
    • Williams T.I., Lynn B.C., Markesbery W.R., Lovell M.A. Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in mild cognitive impairment and early Alzheimer's disease. Neurobiol. Aging 2006, 27:1094-1099.
    • (2006) Neurobiol. Aging , vol.27 , pp. 1094-1099
    • Williams, T.I.1    Lynn, B.C.2    Markesbery, W.R.3    Lovell, M.A.4
  • 45
    • 0025278233 scopus 로고
    • Genetic toxicity of the benzene metabolite trans, trans-muconaldehyde in mammalian and bacterial cells
    • Witz G., Gad S.C., Tice R.R., Oshiro Y., Piper C.E., Goldstein B.D. Genetic toxicity of the benzene metabolite trans, trans-muconaldehyde in mammalian and bacterial cells. Mutat. Res. 1990, 240:295-306.
    • (1990) Mutat. Res. , vol.240 , pp. 295-306
    • Witz, G.1    Gad, S.C.2    Tice, R.R.3    Oshiro, Y.4    Piper, C.E.5    Goldstein, B.D.6


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