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Volumn 33, Issue 5, 2012, Pages 1368-1374

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

Author keywords

Aldo keto reductases; Carbonyl toxicity; Neurotoxicity; SiRNA

Indexed keywords

ALDEHYDE; ALDO KETO REDUCTASE; HYDROGEN PEROXIDE; OXIDOREDUCTASE; SMALL INTERFERING RNA; UMBELLIFERONE; UNCLASSIFIED DRUG;

EID: 84867234457     PISSN: 0161813X     EISSN: 18729711     Source Type: Journal    
DOI: 10.1016/j.neuro.2012.08.015     Document Type: Article
Times cited : (20)

References (48)
  • 1
    • 84857918033 scopus 로고    scopus 로고
    • Transcriptomic and proteomic profiling of KEAP1 disrupted and sulforaphane-treated human breast epithelial cells reveals common expression profiles
    • Agyeman A.S., Chaerkady R., Shaw P.G., Davidson N.E., Visvanathan K., Pandey A., et al. Transcriptomic and proteomic profiling of KEAP1 disrupted and sulforaphane-treated human breast epithelial cells reveals common expression profiles. Breast Cancer Res Treat 2011, 132:175-180.
    • (2011) Breast Cancer Res Treat , vol.132 , pp. 175-180
    • Agyeman, A.S.1    Chaerkady, R.2    Shaw, P.G.3    Davidson, N.E.4    Visvanathan, K.5    Pandey, A.6
  • 2
    • 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., et al. 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
  • 3
    • 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, 40:553-560.
    • (2008) Drug Metab Rev , vol.40 , pp. 553-560
    • Barski, O.A.1    Tipparaju, S.M.2    Bhatnagar, A.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-250.
    • (1976) Anal Biochem , vol.72 , pp. 248-250
    • Bradford, M.M.1
  • 5
    • 0034129716 scopus 로고    scopus 로고
    • The antihypertensive hydralazine is an efficient scavenger of acrolein
    • Burcham P.C., Kerr P.G., Fontaine F. The antihypertensive hydralazine is an efficient scavenger of acrolein. Redox Rep 2000, 5:47-50.
    • (2000) Redox Rep , vol.5 , pp. 47-50
    • Burcham, P.C.1    Kerr, P.G.2    Fontaine, F.3
  • 6
    • 0035951825 scopus 로고    scopus 로고
    • The reactive oxygen species- and Michael acceptor-inducible human aldo-keto reductase AKR1C1 reduces the alpha,beta-unsaturated aldehyde 4-hydroxy-2-nonenal to 1,4-dihydroxy-2-nonene
    • Burczynski M.E., Sridhar G.R., Palackal N.T., Penning T.M. The reactive oxygen species- and Michael acceptor-inducible human aldo-keto reductase AKR1C1 reduces the alpha,beta-unsaturated aldehyde 4-hydroxy-2-nonenal to 1,4-dihydroxy-2-nonene. J Biol Chem 2001, 276:2890-2897.
    • (2001) J Biol Chem , vol.276 , pp. 2890-2897
    • Burczynski, M.E.1    Sridhar, G.R.2    Palackal, N.T.3    Penning, T.M.4
  • 7
    • 0036239372 scopus 로고    scopus 로고
    • Substrate-induced up-regulation of aldose reductase by methylglyoxal, a reactive oxoaldehyde elevated in diabetes
    • Chang K.C., Paek K.S., Kim H.J., Lee Y.S., Yabe-Nishimura C., Seo H.G. Substrate-induced up-regulation of aldose reductase by methylglyoxal, a reactive oxoaldehyde elevated in diabetes. Mol Pharmacol 2002, 61:1184-1191.
    • (2002) Mol Pharmacol , vol.61 , pp. 1184-1191
    • Chang, K.C.1    Paek, K.S.2    Kim, H.J.3    Lee, Y.S.4    Yabe-Nishimura, C.5    Seo, H.G.6
  • 8
    • 41049113672 scopus 로고    scopus 로고
    • Dihydrodiol dehydrogenases regulate the generation of reactive oxygen species and the development of cisplatin resistance in human ovarian carcinoma cells
    • Chen J., Adikari M., Pallai R., Parekh H.K., Simpkins H. Dihydrodiol dehydrogenases regulate the generation of reactive oxygen species and the development of cisplatin resistance in human ovarian carcinoma cells. Cancer Chemother Pharmacol 2008, 61:979-980.
    • (2008) Cancer Chemother Pharmacol , vol.61 , pp. 979-980
    • Chen, J.1    Adikari, M.2    Pallai, R.3    Parekh, H.K.4    Simpkins, H.5
  • 9
    • 0016803884 scopus 로고
    • Factors influencing the effect of hormones on the accumulation of cyclic AMP in cultured human astrocytoma cells
    • Clark R.B., Su Y.F., Ortmann R., Cubeddu L., Johnson G.L., Perkins J.P. Factors influencing the effect of hormones on the accumulation of cyclic AMP in cultured human astrocytoma cells. Metabolism 1975, 24:343-350.
    • (1975) Metabolism , vol.24 , pp. 343-350
    • Clark, R.B.1    Su, Y.F.2    Ortmann, R.3    Cubeddu, L.4    Johnson, G.L.5    Perkins, J.P.6
  • 10
    • 79961184252 scopus 로고    scopus 로고
    • Distribution and time-course of 4-hydroxynonenal, heat shock protein 110/105 family members and cyclooxygenase-2 expression in the hippocampus of rat during trimethyltin-induced neurodegeneration
    • Corvino V., Marchese E., Zarkovic N., Zarkovic K., Cindric M., Waeg G., et al. Distribution and time-course of 4-hydroxynonenal, heat shock protein 110/105 family members and cyclooxygenase-2 expression in the hippocampus of rat during trimethyltin-induced neurodegeneration. Neurochem Res 2011, 36:1490-1500.
    • (2011) Neurochem Res , vol.36 , pp. 1490-1500
    • Corvino, V.1    Marchese, E.2    Zarkovic, N.3    Zarkovic, K.4    Cindric, M.5    Waeg, G.6
  • 11
    • 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, 115:13-20.
    • (2007) Pharmacol Ther , vol.115 , pp. 13-20
    • Ellis, E.M.1
  • 12
    • 1642483509 scopus 로고    scopus 로고
    • Neurodegenerative diseases and oxidative stress
    • Emerit J., Edeas M., Bricaire F. Neurodegenerative diseases and oxidative stress. Biomed Pharmacother 2004, 58:39-40.
    • (2004) Biomed Pharmacother , vol.58 , pp. 39-40
    • Emerit, J.1    Edeas, M.2    Bricaire, F.3
  • 13
    • 0023019005 scopus 로고
    • Use of MTT colorimetric assay to measure cell activation
    • Gerlier D., Thomasset N. Use of MTT colorimetric assay to measure cell activation. J Immunol Methods 1986, 94:57-60.
    • (1986) J Immunol Methods , vol.94 , pp. 57-60
    • Gerlier, D.1    Thomasset, N.2
  • 14
    • 0034796353 scopus 로고    scopus 로고
    • Role of free radicals in the neurodegenerative diseases: therapeutic implications for antioxidant treatment
    • Halliwell B. Role of free radicals in the neurodegenerative diseases: therapeutic implications for antioxidant treatment. Drugs Aging 2001, 18:685-690.
    • (2001) Drugs Aging , vol.18 , pp. 685-690
    • Halliwell, B.1
  • 15
    • 33745013111 scopus 로고    scopus 로고
    • Oxidative stress and neurodegeneration: where are we now?
    • Halliwell B. Oxidative stress and neurodegeneration: where are we now?. J Neurochem 2006, 97:1634-1658.
    • (2006) J Neurochem , vol.97 , pp. 1634-1658
    • Halliwell, B.1
  • 16
    • 79954574488 scopus 로고    scopus 로고
    • Mechanisms of induction of cytosolic and microsomal glutathione transferase (GST) genes by xenobiotics and pro-inflammatory agents
    • Higgins L.G., Hayes J.D. Mechanisms of induction of cytosolic and microsomal glutathione transferase (GST) genes by xenobiotics and pro-inflammatory agents. Drug Metab Rev 2011, 43:92-100.
    • (2011) Drug Metab Rev , vol.43 , pp. 92-100
    • Higgins, L.G.1    Hayes, J.D.2
  • 17
    • 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):21-30.
    • (1998) Biochem J , vol.332 , Issue.PART 1 , pp. 21-30
    • Ireland, L.S.1    Harrison, D.J.2    Neal, G.E.3    Hayes, J.D.4
  • 18
    • 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, 47:263-270.
    • (2007) Annu Rev Pharmacol Toxicol , vol.47 , pp. 263-270
    • Jin, Y.1    Penning, T.M.2
  • 20
    • 0034651240 scopus 로고    scopus 로고
    • Chemoprevention of aflatoxin B1 hepatocarcinogenesis by coumarin, a natural benzopyrone that is a potent inducer of aflatoxin B1-aldehyde reductase, the glutathione S-transferase A5 and P1 subunits, and NAD(P)H:quinone oxidoreductase in rat liver
    • Kelly V.P., Ellis E.M., Manson M.M., Chanas S.A., Moffat G.J., McLeod R., et al. Chemoprevention of aflatoxin B1 hepatocarcinogenesis by coumarin, a natural benzopyrone that is a potent inducer of aflatoxin B1-aldehyde reductase, the glutathione S-transferase A5 and P1 subunits, and NAD(P)H:quinone oxidoreductase in rat liver. Cancer Res 2000, 60:957-960.
    • (2000) Cancer Res , vol.60 , pp. 957-960
    • Kelly, V.P.1    Ellis, E.M.2    Manson, M.M.3    Chanas, S.A.4    Moffat, G.J.5    McLeod, R.6
  • 21
    • 0030986669 scopus 로고    scopus 로고
    • Evidence that 4-hydroxynonenal mediates oxidative stress-induced neuronal apoptosis
    • Kruman I., Bruce-Keller A.J., Bredesen D., Waeg G., Mattson M.P. Evidence that 4-hydroxynonenal mediates oxidative stress-induced neuronal apoptosis. J Neurosci 1997, 17:5089-5100.
    • (1997) J Neurosci , vol.17 , pp. 5089-5100
    • Kruman, I.1    Bruce-Keller, A.J.2    Bredesen, D.3    Waeg, G.4    Mattson, M.P.5
  • 22
    • 77956809165 scopus 로고    scopus 로고
    • Long-term in vitro treatment of human glioblastoma cells with temozolomide increases resistance in vivo through up-regulation of GLUT transporter and aldo-keto reductase enzyme AKR1C expression
    • Le Calve B., Rynkowski M., Le Mercier M., Bruyere C., Lonez C., Gras T., et al. Long-term in vitro treatment of human glioblastoma cells with temozolomide increases resistance in vivo through up-regulation of GLUT transporter and aldo-keto reductase enzyme AKR1C expression. Neoplasia 2010, 12:727-730.
    • (2010) Neoplasia , vol.12 , pp. 727-730
    • Le Calve, B.1    Rynkowski, M.2    Le Mercier, M.3    Bruyere, C.4    Lonez, C.5    Gras, T.6
  • 23
    • 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, 195:25-30.
    • (2012) Chem Biol Interact , vol.195 , pp. 25-30
    • Li, D.1    Ferrari, M.2    Ellis, E.M.3
  • 24
    • 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
  • 25
    • 33645893202 scopus 로고    scopus 로고
    • Induction of AKR1C2 by phase II inducers: identification of a distal consensus antioxidant response element regulated by Nrf2
    • Lou H., Du S., Ji Q., Stolz A. Induction of AKR1C2 by phase II inducers: identification of a distal consensus antioxidant response element regulated by Nrf2. Mol Pharmacol 2006, 69:1662-1672.
    • (2006) Mol Pharmacol , vol.69 , pp. 1662-1672
    • Lou, H.1    Du, S.2    Ji, Q.3    Stolz, A.4
  • 26
    • 0035112495 scopus 로고    scopus 로고
    • Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures
    • Lovell M.A., Xie C., Markesbery W.R. Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures. Neurobiol Aging 2001, 22:187-190.
    • (2001) Neurobiol Aging , vol.22 , pp. 187-190
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 27
    • 34548831366 scopus 로고    scopus 로고
    • Synthesis and catabolism of gamma-hydroxybutyrate in SH-SY5Y human neuroblastoma cells: role of the aldo-keto reductase AKR7A2
    • Lyon R.C., Johnston S.M., Watson D.G., McGarvie G., Ellis E.M. Synthesis and catabolism of gamma-hydroxybutyrate in SH-SY5Y human neuroblastoma cells: role of the aldo-keto reductase AKR7A2. J Biol Chem 2007, 282:25986-25992.
    • (2007) J Biol Chem , vol.282 , pp. 25986-25992
    • Lyon, R.C.1    Johnston, S.M.2    Watson, D.G.3    McGarvie, G.4    Ellis, E.M.5
  • 28
    • 84875805187 scopus 로고    scopus 로고
    • Aldo-keto reductases mediate constitutive and inducible protection against aldehyde toxicity in human neuroblastoma SH-SY5Y cells, unpublished.
    • Lyon RC, Li D, McGarvie G, Ellis EM. Aldo-keto reductases mediate constitutive and inducible protection against aldehyde toxicity in human neuroblastoma SH-SY5Y cells, unpublished.
    • Lyon, R.C.1    Li, D.2    McGarvie, G.3    Ellis, E.M.4
  • 29
    • 0031980065 scopus 로고    scopus 로고
    • Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease
    • Markesbery W.R., Lovell M.A. Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease. Neurobiol Aging 1998, 19:33-40.
    • (1998) Neurobiol Aging , vol.19 , pp. 33-40
    • Markesbery, W.R.1    Lovell, M.A.2
  • 30
    • 33750159449 scopus 로고    scopus 로고
    • Neurohormetic phytochemicals: low-dose toxins that induce adaptive neuronal stress responses
    • Mattson M.P., Cheng A. Neurohormetic phytochemicals: low-dose toxins that induce adaptive neuronal stress responses. Trends Neurosci 2006, 29:632-640.
    • (2006) Trends Neurosci , vol.29 , pp. 632-640
    • Mattson, M.P.1    Cheng, A.2
  • 31
    • 0033569574 scopus 로고    scopus 로고
    • Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members
    • O'Connor T., Ireland L.S., Harrison D.J., Hayes J.D. Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members. Biochem J 1999, 343(Pt 2):487-490.
    • (1999) Biochem J , vol.343 , Issue.PART 2 , pp. 487-490
    • O'Connor, T.1    Ireland, L.S.2    Harrison, D.J.3    Hayes, J.D.4
  • 32
    • 79953156544 scopus 로고    scopus 로고
    • Differential expression of type 2 3alpha/type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3) in tumors of the central nervous system
    • Park A.L., Lin H.K., Yang Q., Sing C.W., Fan M., Mapstone T.B., et al. Differential expression of type 2 3alpha/type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3) in tumors of the central nervous system. Int J Clin Exp Pathol 2010, 3:743-750.
    • (2010) Int J Clin Exp Pathol , vol.3 , pp. 743-750
    • Park, A.L.1    Lin, H.K.2    Yang, Q.3    Sing, C.W.4    Fan, M.5    Mapstone, T.B.6
  • 34
    • 0026975733 scopus 로고
    • Peroxyl radical scavenging by a series of coumarins
    • Paya M., Halliwell B., Hoult J.R. Peroxyl radical scavenging by a series of coumarins. Free Radic Res Commun 1992, 17:293-300.
    • (1992) Free Radic Res Commun , vol.17 , pp. 293-300
    • Paya, M.1    Halliwell, B.2    Hoult, J.R.3
  • 35
    • 0035914218 scopus 로고    scopus 로고
    • Elevation of AKR7A2 (succinic semialdehyde reductase) in neurodegenerative disease
    • Picklo M.J., Olson S.J., Hayes J.D., Markesbery W.R., Montine T.J. Elevation of AKR7A2 (succinic semialdehyde reductase) in neurodegenerative disease. Brain Res 2001, 916:229-230.
    • (2001) Brain Res , vol.916 , pp. 229-230
    • Picklo, M.J.1    Olson, S.J.2    Hayes, J.D.3    Markesbery, W.R.4    Montine, T.J.5
  • 36
    • 80052261937 scopus 로고    scopus 로고
    • Lipid peroxidation and neurodegenerative disease
    • Reed T.T. Lipid peroxidation and neurodegenerative disease. Free Radic Biol Med 2011, 51:1302-1319.
    • (2011) Free Radic Biol Med , vol.51 , pp. 1302-1319
    • Reed, T.T.1
  • 37
    • 0019435865 scopus 로고
    • The enzymes catalysing succinic semialdehyde reduction in rat brain
    • Rivett A.J., Smith I.L., Tipton K.F. The enzymes catalysing succinic semialdehyde reduction in rat brain. Biochem Pharmacol 1981, 30:741-750.
    • (1981) Biochem Pharmacol , vol.30 , pp. 741-750
    • Rivett, A.J.1    Smith, I.L.2    Tipton, K.F.3
  • 38
    • 0033231456 scopus 로고    scopus 로고
    • Cloning and expression of succinic semialdehyde reductase from human brain
    • Schaller M., Schaffhauser M., Sans N., Wermuth B. Cloning and expression of succinic semialdehyde reductase from human brain. Eur J Biochem 1999, 265:1056-1060.
    • (1999) Eur J Biochem , vol.265 , pp. 1056-1060
    • Schaller, M.1    Schaffhauser, M.2    Sans, N.3    Wermuth, B.4
  • 39
    • 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, 24:149-150.
    • (2003) Mol Aspects Med , vol.24 , pp. 149-150
    • Schaur, R.J.1
  • 40
    • 0033791424 scopus 로고    scopus 로고
    • Regulation of rat glutamate-cysteine ligase (gamma-glutamylcysteine synthetase) subunits by chemopreventive agents and in aflatoxin B(1)-induced preneoplasia
    • Shepherd A.G., Manson M.M., Ball H.W., McLellan L.I. Regulation of rat glutamate-cysteine ligase (gamma-glutamylcysteine synthetase) subunits by chemopreventive agents and in aflatoxin B(1)-induced preneoplasia. Carcinogenesis 2000, 21:1827-1834.
    • (2000) Carcinogenesis , vol.21 , pp. 1827-1834
    • Shepherd, A.G.1    Manson, M.M.2    Ball, H.W.3    McLellan, L.I.4
  • 41
    • 0029562272 scopus 로고
    • Lipid peroxidation product, 4-hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase
    • Srivastava S., Chandra A., Bhatnagar A., Srivastava S.K., Ansari N.H. Lipid peroxidation product, 4-hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase. Biochem Biophys Res Commun 1995, 217:741-746.
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 741-746
    • Srivastava, S.1    Chandra, A.2    Bhatnagar, A.3    Srivastava, S.K.4    Ansari, N.H.5
  • 42
    • 78650547215 scopus 로고    scopus 로고
    • Esculetin-induced protection of human hepatoma HepG2 cells against hydrogen peroxide is associated with the Nrf2-dependent induction of the NAD(P)H: quinone oxidoreductase 1 gene
    • Subramaniam S.R., Ellis E.M. Esculetin-induced protection of human hepatoma HepG2 cells against hydrogen peroxide is associated with the Nrf2-dependent induction of the NAD(P)H: quinone oxidoreductase 1 gene. Toxicol Appl Pharmacol 2011, 250:130-140.
    • (2011) Toxicol Appl Pharmacol , vol.250 , pp. 130-140
    • Subramaniam, S.R.1    Ellis, E.M.2
  • 43
    • 84875807420 scopus 로고    scopus 로고
    • Neuroprotective effects of umbelliferone and esculetin in a mouse model of Parkinson's Disease, unpublished.
    • Subramaniam SR, Ellis EM. Neuroprotective effects of umbelliferone and esculetin in a mouse model of Parkinson's Disease, unpublished.
    • Subramaniam, S.R.1    Ellis, E.M.2
  • 44
    • 69949187968 scopus 로고    scopus 로고
    • Dual anti-oxidative effects of fraxetin isolated from Fraxinus rhinchophylla
    • Thuong P.T., Pokharel Y.R., Lee M.Y., Kim S.K., Bae K., Su N.D., et al. Dual anti-oxidative effects of fraxetin isolated from Fraxinus rhinchophylla. Biol Pharm Bull 2009, 32:1527-1532.
    • (2009) Biol Pharm Bull , vol.32 , pp. 1527-1532
    • Thuong, P.T.1    Pokharel, Y.R.2    Lee, M.Y.3    Kim, S.K.4    Bae, K.5    Su, N.D.6
  • 45
    • 33847312147 scopus 로고    scopus 로고
    • Sepiapterin reductase expression is increased in Parkinson's disease brain tissue
    • Tobin J.E., Cui J., Wilk J.B., Latourelle J.C., Laramie J.M., McKee A.C., et al. Sepiapterin reductase expression is increased in Parkinson's disease brain tissue. Brain Res 2007, 1139:42-50.
    • (2007) Brain Res , vol.1139 , pp. 42-50
    • Tobin, J.E.1    Cui, J.2    Wilk, J.B.3    Latourelle, J.C.4    Laramie, J.M.5    McKee, A.C.6
  • 46
    • 70149116449 scopus 로고    scopus 로고
    • Induction of 1C aldoketoreductases and other drug dose-dependent genes upon acquisition of anthracycline resistance
    • Veitch Z.W., Guo B., Hembruff S.L., Bewick A.J., Heibein A.D., Eng J., et al. Induction of 1C aldoketoreductases and other drug dose-dependent genes upon acquisition of anthracycline resistance. Pharmacogenet Genomics 2009, 19:477-480.
    • (2009) Pharmacogenet Genomics , vol.19 , pp. 477-480
    • Veitch, Z.W.1    Guo, B.2    Hembruff, S.L.3    Bewick, A.J.4    Heibein, A.D.5    Eng, J.6
  • 47
    • 15844378818 scopus 로고    scopus 로고
    • The carbonyl scavengers aminoguanidine and tenilsetam protect against the neurotoxic effects of methylglyoxal
    • Webster J., Urban C., Berbaum K., Loske C., Alpar A., Gartner U., et al. The carbonyl scavengers aminoguanidine and tenilsetam protect against the neurotoxic effects of methylglyoxal. Neurotox Res 2005, 7:95-100.
    • (2005) Neurotox Res , vol.7 , pp. 95-100
    • Webster, J.1    Urban, C.2    Berbaum, K.3    Loske, C.4    Alpar, A.5    Gartner, U.6
  • 48
    • 12644290275 scopus 로고
    • Analysis and processing of Chinese herbal drugs: the study of Fructus aurantti immaturus
    • Wu F.J., Sheu S.J. Analysis and processing of Chinese herbal drugs: the study of Fructus aurantti immaturus. Chin Pharm J 1992, 44:257-260.
    • (1992) Chin Pharm J , vol.44 , pp. 257-260
    • Wu, F.J.1    Sheu, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.