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Volumn 50, Issue 2, 2011, Pages 295-304

Human prostaglandin H synthase (hPHS)-1- and hPHS-2-dependent bioactivation, oxidative macromolecular damage, and cytotoxicity of dopamine, its precursor, and its metabolites

Author keywords

Dopamine; Free radicals; Oxidative stress; Prostaglandin H synthase; Reactive oxygen species

Indexed keywords

3 O METHYLDOPAMINE; 3,4 DIHYDROXYPHENYLACETIC ACID; ACETYLSALICYLIC ACID; ARACHIDONIC ACID; CATALASE; DOPAMINE; HOMOVANILLIC ACID; PROSTAGLANDIN SYNTHASE;

EID: 78651234518     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2010.11.010     Document Type: Article
Times cited : (11)

References (60)
  • 4
    • 0033526660 scopus 로고    scopus 로고
    • Distribution of cyclooxygenase-1 and cyclooxygenase-2 mRNAs and proteins in human brain and peripheral organs
    • K. Yasojima, C. Schwab, E.G. McGeer, and P.L. McGeer Distribution of cyclooxygenase-1 and cyclooxygenase-2 mRNAs and proteins in human brain and peripheral organs Brain Res. 830 1999 226 236
    • (1999) Brain Res. , vol.830 , pp. 226-236
    • Yasojima, K.1    Schwab, C.2    McGeer, E.G.3    McGeer, P.L.4
  • 7
    • 0025029234 scopus 로고
    • Prostaglandin synthase-mediated metabolism of carcinogens and a potential role for peroxyl radicals as reactive intermediates
    • L.J. Marnett Prostaglandin synthase-mediated metabolism of carcinogens and a potential role for peroxyl radicals as reactive intermediates Environ. Health Perspect. 88 1990 5 12
    • (1990) Environ. Health Perspect. , vol.88 , pp. 5-12
    • Marnett, L.J.1
  • 8
    • 0018786140 scopus 로고
    • Prostaglandin hydroperoxidase, an integral part of prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes
    • S. Ohki, N. Ogino, S. Yamamoto, and O. Hayaishi Prostaglandin hydroperoxidase, an integral part of prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes J. Biol. Chem. 254 1979 829 836
    • (1979) J. Biol. Chem. , vol.254 , pp. 829-836
    • Ohki, S.1    Ogino, N.2    Yamamoto, S.3    Hayaishi, O.4
  • 9
    • 0023644747 scopus 로고
    • Quantitative studies of hydroperoxide reduction by prostaglandin H synthase: Reducing substrate specificity and the relationship of peroxidase to cyclooxygenase activities
    • C.M. Markey, A. Alward, P.E. Weller, and L.J. Marnett Quantitative studies of hydroperoxide reduction by prostaglandin H synthase: reducing substrate specificity and the relationship of peroxidase to cyclooxygenase activities J. Biol. Chem. 262 1987 6266 6279
    • (1987) J. Biol. Chem. , vol.262 , pp. 6266-6279
    • Markey, C.M.1    Alward, A.2    Weller, P.E.3    Marnett, L.J.4
  • 10
    • 0023678508 scopus 로고
    • Prostaglandin hydroperoxidase-dependent oxidation of phenylbutazone: Relationship to inhibition of prostaglandin cyclooxygenase
    • M.F. Hughes, R.P. Mason, and T.E. Eling Prostaglandin hydroperoxidase-dependent oxidation of phenylbutazone: relationship to inhibition of prostaglandin cyclooxygenase Mol. Pharmacol. 34 1988 186 193
    • (1988) Mol. Pharmacol. , vol.34 , pp. 186-193
    • Hughes, M.F.1    Mason, R.P.2    Eling, T.E.3
  • 11
    • 0032566524 scopus 로고    scopus 로고
    • Free radical intermediates of phenytoin and related teratogens: Prostaglandin H synthase-catalyzed bioactivation, electron paramagnetic resonance spectrometry, and photochemical product analysis
    • T. Parman, G. Chen, and P.G. Wells Free radical intermediates of phenytoin and related teratogens: prostaglandin H synthase-catalyzed bioactivation, electron paramagnetic resonance spectrometry, and photochemical product analysis J. Biol. Chem. 273 1998 25079 25088
    • (1998) J. Biol. Chem. , vol.273 , pp. 25079-25088
    • Parman, T.1    Chen, G.2    Wells, P.G.3
  • 13
    • 78651241491 scopus 로고    scopus 로고
    • Neuroprotection against endogenous oxidative stress in aging prostaglandin H synthase-1 (PHS-1) knockout mice
    • P.G. Wells, A. Ramkissoon, and W. Jeng Neuroprotection against endogenous oxidative stress in aging prostaglandin H synthase-1 (PHS-1) knockout mice Toxicol. Sci. Suppl. Toxicol. 78 2004 63
    • (2004) Toxicol. Sci. Suppl. Toxicol. , vol.78 , pp. 63
    • Wells, P.G.1    Ramkissoon, A.2    Jeng, W.3
  • 14
    • 41949108084 scopus 로고    scopus 로고
    • Cyclooxygenase-2 is involved in oxidative damage and alpha-synuclein accumulation in dopaminergic cells
    • S.W. Chae, B.Y. Kang, O. Hwang, and H.J. Choi Cyclooxygenase-2 is involved in oxidative damage and alpha-synuclein accumulation in dopaminergic cells Neurosci. Lett. 436 2008 205 209
    • (2008) Neurosci. Lett. , vol.436 , pp. 205-209
    • Chae, S.W.1    Kang, B.Y.2    Hwang, O.3    Choi, H.J.4
  • 16
    • 23744455470 scopus 로고    scopus 로고
    • Dopaminergic neurotoxicity by 6-OHDA and MPP+: Differential requirement for neuronal cyclooxygenase activity
    • E. Carrasco, D. Casper, and P. Werner Dopaminergic neurotoxicity by 6-OHDA and MPP+: differential requirement for neuronal cyclooxygenase activity J. Neurosci. Res. 81 2005 121 131
    • (2005) J. Neurosci. Res. , vol.81 , pp. 121-131
    • Carrasco, E.1    Casper, D.2    Werner, P.3
  • 17
    • 0032549535 scopus 로고    scopus 로고
    • Comparison of structural stabilities of prostaglandin H synthase-1 and -2
    • G. Xiao, W. Chen, and R.J. Kulmacz Comparison of structural stabilities of prostaglandin H synthase-1 and -2 J. Biol. Chem. 273 1998 6801 6811
    • (1998) J. Biol. Chem. , vol.273 , pp. 6801-6811
    • Xiao, G.1    Chen, W.2    Kulmacz, R.J.3
  • 18
    • 0027454020 scopus 로고
    • Dopamine transporter expression confers cytotoxicity to low doses of the parkinsonism-inducing neurotoxin 1-methyl-4-phenylpyridinium
    • C. Pifl, B. Giros, and M.G. Caron Dopamine transporter expression confers cytotoxicity to low doses of the parkinsonism-inducing neurotoxin 1-methyl-4-phenylpyridinium J. Neurosci. 13 1993 4246 4253
    • (1993) J. Neurosci. , vol.13 , pp. 4246-4253
    • Pifl, C.1    Giros, B.2    Caron, M.G.3
  • 21
    • 0032540344 scopus 로고    scopus 로고
    • Subcellular localization of prostaglandin endoperoxide H synthases-1 and -2 by immunoelectron microscopy
    • A.G. Spencer, J.W. Woods, T. Arakawa, I.I. Singer, and W.L. Smith Subcellular localization of prostaglandin endoperoxide H synthases-1 and -2 by immunoelectron microscopy J. Biol. Chem. 273 1998 9886 9893
    • (1998) J. Biol. Chem. , vol.273 , pp. 9886-9893
    • Spencer, A.G.1    Woods, J.W.2    Arakawa, T.3    Singer, I.I.4    Smith, W.L.5
  • 22
    • 17744417519 scopus 로고    scopus 로고
    • Cellular background level of 8-oxo-7, 8-dihydro-2′-deoxyguanosine: An isotope based method to evaluate artefactual oxidation of DNA during its extraction and subsequent work-up
    • J.L. Ravanat, T. Douki, P. Duez, E. Gremaud, K. Herbert, T. Hofer, L. Lasserre, C. Saint-Pierre, A. Favier, and J. Cadet Cellular background level of 8-oxo-7, 8-dihydro-2′-deoxyguanosine: an isotope based method to evaluate artefactual oxidation of DNA during its extraction and subsequent work-up Carcinogenesis 23 2002 1911 1918
    • (2002) Carcinogenesis , vol.23 , pp. 1911-1918
    • Ravanat, J.L.1    Douki, T.2    Duez, P.3    Gremaud, E.4    Herbert, K.5    Hofer, T.6    Lasserre, L.7    Saint-Pierre, C.8    Favier, A.9    Cadet, J.10
  • 23
    • 0026801167 scopus 로고
    • Identification of a pharmacologically distinct prostaglandin H synthase in cultured epithelial cells
    • M.J. Holtzman, J. Turk, and L.P. Shornick Identification of a pharmacologically distinct prostaglandin H synthase in cultured epithelial cells J. Biol. Chem. 267 1992 21438 21445
    • (1992) J. Biol. Chem. , vol.267 , pp. 21438-21445
    • Holtzman, M.J.1    Turk, J.2    Shornick, L.P.3
  • 24
    • 0028339780 scopus 로고
    • Acetylation of human prostaglandin endoperoxide synthase-2 (cyclooxygenase-2) by aspirin
    • M. Lecomte, O. Laneuville, C. Ji, D.L. DeWitt, and W.L. Smith Acetylation of human prostaglandin endoperoxide synthase-2 (cyclooxygenase-2) by aspirin J. Biol. Chem. 269 1994 13207 13215
    • (1994) J. Biol. Chem. , vol.269 , pp. 13207-13215
    • Lecomte, M.1    Laneuville, O.2    Ji, C.3    Dewitt, D.L.4    Smith, W.L.5
  • 25
    • 0043173825 scopus 로고    scopus 로고
    • Dopamine induces autophagic cell death and alpha-synuclein increase in human neuroblastoma SH-SY5Y cells
    • C. Gomez-Santos, I. Ferrer, A.F. Santidrian, M. Barrachina, J. Gil, and S. Ambrosio Dopamine induces autophagic cell death and alpha-synuclein increase in human neuroblastoma SH-SY5Y cells J. Neurosci. Res. 73 2003 341 350
    • (2003) J. Neurosci. Res. , vol.73 , pp. 341-350
    • Gomez-Santos, C.1    Ferrer, I.2    Santidrian, A.F.3    Barrachina, M.4    Gil, J.5    Ambrosio, S.6
  • 26
    • 0018148688 scopus 로고
    • Autoxidation versus covalent binding of quinones as the mechanism of toxicity of dopamine, 6-hydroxydopamine, and related compounds toward C1300 neuroblastoma cells in vitro
    • D.G. Graham, S.M. Tiffany, W.R. Bell Jr., and W.F. Gutknecht Autoxidation versus covalent binding of quinones as the mechanism of toxicity of dopamine, 6-hydroxydopamine, and related compounds toward C1300 neuroblastoma cells in vitro Mol. Pharmacol. 14 1978 644 653
    • (1978) Mol. Pharmacol. , vol.14 , pp. 644-653
    • Graham, D.G.1    Tiffany, S.M.2    Bell Jr., W.R.3    Gutknecht, W.F.4
  • 27
    • 0028812293 scopus 로고
    • Enzymatic oxidation of dopamine: The role of prostaglandin H synthase
    • T.G. Hastings Enzymatic oxidation of dopamine: the role of prostaglandin H synthase J. Neurochem. 64 1995 919 924
    • (1995) J. Neurochem. , vol.64 , pp. 919-924
    • Hastings, T.G.1
  • 29
    • 0028969650 scopus 로고
    • Prostaglandin H synthetase-mediated metabolism of dopamine: Implication for Parkinson's disease
    • M.B. Mattammal, R. Strong, V.M. Lakshmi, H.D. Chung, and A.H. Stephenson Prostaglandin H synthetase-mediated metabolism of dopamine: implication for Parkinson's disease J. Neurochem. 64 1995 1645 1654
    • (1995) J. Neurochem. , vol.64 , pp. 1645-1654
    • Mattammal, M.B.1    Strong, R.2    Lakshmi, V.M.3    Chung, H.D.4    Stephenson, A.H.5
  • 30
    • 0032486311 scopus 로고    scopus 로고
    • Metabolic activation of dopamine o-quinones to o-semiquinones by NADPH cytochrome P450 reductase may play an important role in oxidative stress and apoptotic effects
    • J. Segura-Aguilar, D. Metodiewa, and C.J. Welch Metabolic activation of dopamine o-quinones to o-semiquinones by NADPH cytochrome P450 reductase may play an important role in oxidative stress and apoptotic effects Biochim. Biophys. Acta 1381 1998 1 6
    • (1998) Biochim. Biophys. Acta , vol.1381 , pp. 1-6
    • Segura-Aguilar, J.1    Metodiewa, D.2    Welch, C.J.3
  • 31
    • 0031042677 scopus 로고    scopus 로고
    • Dopamine- and l-beta-3, 4-dihydroxyphenylalanine hydrochloride (L-Dopa)-induced cytotoxicity towards catecholaminergic neuroblastoma SH-SY5Y cells: Effects of oxidative stress and antioxidative factors
    • C.T. Lai, and P.H. Yu Dopamine- and l-beta-3, 4-dihydroxyphenylalanine hydrochloride (L-Dopa)-induced cytotoxicity towards catecholaminergic neuroblastoma SH-SY5Y cells: effects of oxidative stress and antioxidative factors Biochem. Pharmacol. 53 1997 363 372
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 363-372
    • Lai, C.T.1    Yu, P.H.2
  • 32
    • 67649961745 scopus 로고    scopus 로고
    • Prostaglandin H synthase-1-catalyzed bioactivation of neurotransmitters, their precursors, and metabolites: Oxidative DNA damage and electron spin resonance spectroscopy studies
    • L.L. Goncalves, A. Ramkissoon, and P.G. Wells Prostaglandin H synthase-1-catalyzed bioactivation of neurotransmitters, their precursors, and metabolites: oxidative DNA damage and electron spin resonance spectroscopy studies Chem. Res. Toxicol. 22 2009 842 852
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 842-852
    • Goncalves, L.L.1    Ramkissoon, A.2    Wells, P.G.3
  • 33
    • 33646264063 scopus 로고    scopus 로고
    • Prostaglandin H synthase-catalyzed bioactivation of amphetamines to free radical intermediates that cause CNS regional DNA oxidation and nerve terminal degeneration
    • W. Jeng, A. Ramkissoon, T. Parman, and P.G. Wells Prostaglandin H synthase-catalyzed bioactivation of amphetamines to free radical intermediates that cause CNS regional DNA oxidation and nerve terminal degeneration FASEB J. 20 2006 638 650
    • (2006) FASEB J. , vol.20 , pp. 638-650
    • Jeng, W.1    Ramkissoon, A.2    Parman, T.3    Wells, P.G.4
  • 34
    • 77953305867 scopus 로고    scopus 로고
    • Reduced 3, 4-methylenedioxymethamphetamine (MDMA, ecstasy)-initiated oxidative DNA damage and neurodegeneration in prostaglandin H synthase-1 knockout mice
    • W. Jeng, and P.G. Wells Reduced 3, 4-methylenedioxymethamphetamine (MDMA, ecstasy)-initiated oxidative DNA damage and neurodegeneration in prostaglandin H synthase-1 knockout mice ACS Chem. Neurosci. 1 2010 366 380
    • (2010) ACS Chem. Neurosci. , vol.1 , pp. 366-380
    • Jeng, W.1    Wells, P.G.2
  • 35
    • 0036310321 scopus 로고    scopus 로고
    • Embryonic prostaglandin H synthase-2 (PHS-2) expression and benzo[a]pyrene teratogenicity in PHS-2 knockout mice
    • T. Parman, and P.G. Wells Embryonic prostaglandin H synthase-2 (PHS-2) expression and benzo[a]pyrene teratogenicity in PHS-2 knockout mice FASEB J. 16 2002 1001 1009
    • (2002) FASEB J. , vol.16 , pp. 1001-1009
    • Parman, T.1    Wells, P.G.2
  • 36
    • 0032920883 scopus 로고    scopus 로고
    • Free radical-mediated oxidative DNA damage in the mechanism of thalidomide teratogenicity
    • T. Parman, M.J. Wiley, and P.G. Wells Free radical-mediated oxidative DNA damage in the mechanism of thalidomide teratogenicity Nat. Med. 5 1999 582 585
    • (1999) Nat. Med. , vol.5 , pp. 582-585
    • Parman, T.1    Wiley, M.J.2    Wells, P.G.3
  • 37
    • 0037567429 scopus 로고    scopus 로고
    • Comparison of the properties of prostaglandin H synthase-1 and -2
    • R.J. Kulmacz, W.A. van der Donk, and A.L. Tsai Comparison of the properties of prostaglandin H synthase-1 and -2 Prog. Lipid Res. 42 2003 377 404
    • (2003) Prog. Lipid Res. , vol.42 , pp. 377-404
    • Kulmacz, R.J.1    Van Der Donk, W.A.2    Tsai, A.L.3
  • 38
    • 2142695733 scopus 로고    scopus 로고
    • Cyclooxygenases: New forms, new inhibitors, and lessons from the clinic
    • T.D. Warner, and J.A. Mitchell Cyclooxygenases: new forms, new inhibitors, and lessons from the clinic FASEB J. 18 2004 790 804
    • (2004) FASEB J. , vol.18 , pp. 790-804
    • Warner, T.D.1    Mitchell, J.A.2
  • 39
    • 0032479218 scopus 로고    scopus 로고
    • Cellular regulation of prostaglandin H synthase catalysis
    • R.J. Kulmacz Cellular regulation of prostaglandin H synthase catalysis FEBS Lett. 430 1998 154 157
    • (1998) FEBS Lett. , vol.430 , pp. 154-157
    • Kulmacz, R.J.1
  • 40
    • 0032445741 scopus 로고    scopus 로고
    • Activation of heterocyclic amines by combinations of prostaglandin H synthase-1 and -2 with N-acetyltransferase 1 and 2
    • Y. Liu, and G.N. Levy Activation of heterocyclic amines by combinations of prostaglandin H synthase-1 and -2 with N-acetyltransferase 1 and 2 Cancer Lett. 133 1998 115 123
    • (1998) Cancer Lett. , vol.133 , pp. 115-123
    • Liu, Y.1    Levy, G.N.2
  • 41
    • 0028853538 scopus 로고
    • Activation of 2-aminofluorene by prostaglandin endoperoxide H synthase-2
    • Y. Liu, G.N. Levy, and W.W. Weber Activation of 2-aminofluorene by prostaglandin endoperoxide H synthase-2 Biochem. Biophys. Res. Commun. 215 1995 346 354
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 346-354
    • Liu, Y.1    Levy, G.N.2    Weber, W.W.3
  • 42
    • 0035142384 scopus 로고    scopus 로고
    • Carcinogen substrate specificity of human COX-1 and COX-2
    • F.W. Wiese, P.A. Thompson, and F.F. Kadlubar Carcinogen substrate specificity of human COX-1 and COX-2 Carcinogenesis 22 2001 5 10
    • (2001) Carcinogenesis , vol.22 , pp. 5-10
    • Wiese, F.W.1    Thompson, P.A.2    Kadlubar, F.F.3
  • 43
    • 0027146692 scopus 로고
    • Selectivity of nonsteroidal antiinflammatory drugs as inhibitors of constitutive and inducible cyclooxygenase
    • J.A. Mitchell, P. Akarasereenont, C. Thiemermann, R.J. Flower, and J.R. Vane Selectivity of nonsteroidal antiinflammatory drugs as inhibitors of constitutive and inducible cyclooxygenase Proc. Natl Acad. Sci. USA 90 1993 11693 11697
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11693-11697
    • Mitchell, J.A.1    Akarasereenont, P.2    Thiemermann, C.3    Flower, R.J.4    Vane, J.R.5
  • 44
    • 0013925243 scopus 로고
    • A quantitative study on the nigro-neostriatal dopamine neuron system in the rat
    • N.E. Anden, K. Hfuxe, B. Hamberger, and T. Hokfelt A quantitative study on the nigro-neostriatal dopamine neuron system in the rat Acta Physiol. Scand. 67 1966 306 312
    • (1966) Acta Physiol. Scand. , vol.67 , pp. 306-312
    • Anden, N.E.1    Hfuxe, K.2    Hamberger, B.3    Hokfelt, T.4
  • 45
    • 0028025252 scopus 로고
    • Efflux of dopamine from the synaptic cleft in the nucleus accumbens of the rat brain
    • P.A. Garris, E.L. Ciolkowski, P. Pastore, and R.M. Wightman Efflux of dopamine from the synaptic cleft in the nucleus accumbens of the rat brain J. Neurosci. 14 1994 6084 6093
    • (1994) J. Neurosci. , vol.14 , pp. 6084-6093
    • Garris, P.A.1    Ciolkowski, E.L.2    Pastore, P.3    Wightman, R.M.4
  • 46
    • 0038383710 scopus 로고    scopus 로고
    • Intracellular patch electrochemistry: Regulation of cytosolic catecholamines in chromaffin cells
    • E.V. Mosharov, L.W. Gong, B. Khanna, D. Sulzer, and M. Lindau Intracellular patch electrochemistry: regulation of cytosolic catecholamines in chromaffin cells J. Neurosci. 23 2003 5835 5845
    • (2003) J. Neurosci. , vol.23 , pp. 5835-5845
    • Mosharov, E.V.1    Gong, L.W.2    Khanna, B.3    Sulzer, D.4    Lindau, M.5
  • 47
    • 33747348720 scopus 로고    scopus 로고
    • Cyclooxygenase-2-dependent neuronal death proceeds via superoxide anion generation
    • J.Y. Im, D. Kim, S.G. Paik, and P.L. Han Cyclooxygenase-2-dependent neuronal death proceeds via superoxide anion generation Free Radic. Biol. Med. 41 2006 960 972
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 960-972
    • Im, J.Y.1    Kim, D.2    Paik, S.G.3    Han, P.L.4
  • 49
    • 78651234972 scopus 로고    scopus 로고
    • Oxidative DNA damage precedes amyloid plaque formation in amyloid precursor protein (APP) transgenic mice: An animal model of Alzheimer's disease
    • W. Jeng, A. Chrishti, D. Westaway, and P.G. Wells Oxidative DNA damage precedes amyloid plaque formation in amyloid precursor protein (APP) transgenic mice: an animal model of Alzheimer's disease Toxicol. Sci. Suppl. Toxicol. 66 2002 13
    • (2002) Toxicol. Sci. Suppl. Toxicol. , vol.66 , pp. 13
    • Jeng, W.1    Chrishti, A.2    Westaway, D.3    Wells, P.G.4
  • 50
    • 0033963704 scopus 로고    scopus 로고
    • Oxidative stress and gene regulation
    • R.G. Allen, and M. Tresini Oxidative stress and gene regulation Free Radic. Biol. Med. 28 2000 463 499
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 463-499
    • Allen, R.G.1    Tresini, M.2
  • 51
    • 0042026553 scopus 로고    scopus 로고
    • Oxidized guanine lesions as modulators of gene transcription: Altered p50 binding affinity and repair shielding by 7,8-dihydro-8-oxo-2′- deoxyguanosine lesions in the NF-kappaB promoter element
    • M.K. Hailer-Morrison, J.M. Kotler, B.D. Martin, and K.D. Sugden Oxidized guanine lesions as modulators of gene transcription: altered p50 binding affinity and repair shielding by 7,8-dihydro-8-oxo-2′-deoxyguanosine lesions in the NF-kappaB promoter element Biochemistry (Moscow) 42 2003 9761 9770
    • (2003) Biochemistry (Moscow) , vol.42 , pp. 9761-9770
    • Hailer-Morrison, M.K.1    Kotler, J.M.2    Martin, B.D.3    Sugden, K.D.4
  • 53
    • 54049135708 scopus 로고    scopus 로고
    • Oxoguanine glycosylase 1 protects against methamphetamine-enhanced fetal brain oxidative DNA damage and neurodevelopmental deficits
    • A.W. Wong, G.P. McCallum, W. Jeng, and P.G. Wells Oxoguanine glycosylase 1 protects against methamphetamine-enhanced fetal brain oxidative DNA damage and neurodevelopmental deficits J. Neurosci. 28 2008 9047 9054
    • (2008) J. Neurosci. , vol.28 , pp. 9047-9054
    • Wong, A.W.1    McCallum, G.P.2    Jeng, W.3    Wells, P.G.4
  • 54
    • 0031214246 scopus 로고    scopus 로고
    • Formation of DNA adducts and oxidative base damage by copper mediated oxidation of dopamine and 6-hydroxydopamine
    • G. Levay, Q. Ye, and W.J. Bodell Formation of DNA adducts and oxidative base damage by copper mediated oxidation of dopamine and 6-hydroxydopamine Exp. Neurol. 146 1997 570 574
    • (1997) Exp. Neurol. , vol.146 , pp. 570-574
    • Levay, G.1    Ye, Q.2    Bodell, W.J.3
  • 56
    • 0032190264 scopus 로고    scopus 로고
    • Cyclooxygenase and inflammation in Alzheimer's disease: Experimental approaches and clinical interventions
    • G.M. Pasinetti Cyclooxygenase and inflammation in Alzheimer's disease: experimental approaches and clinical interventions J. Neurosci. Res. 54 1998 1 6
    • (1998) J. Neurosci. Res. , vol.54 , pp. 1-6
    • Pasinetti, G.M.1
  • 58
    • 8644252682 scopus 로고    scopus 로고
    • Inhibition of brain mitochondrial respiration by dopamine and its metabolites: Implications for Parkinson's disease and catecholamine-associated diseases
    • M.R. Gluck, and G.D. Zeevalk Inhibition of brain mitochondrial respiration by dopamine and its metabolites: implications for Parkinson's disease and catecholamine-associated diseases J. Neurochem. 91 2004 788 795
    • (2004) J. Neurochem. , vol.91 , pp. 788-795
    • Gluck, M.R.1    Zeevalk, G.D.2
  • 59
    • 33749043629 scopus 로고    scopus 로고
    • One-electron oxidation of catecholamines generates free radicals with an in vitro toxicity correlating with their lifetime
    • O. Terland, B. Almas, T. Flatmark, K.K. Andersson, and M. Sorlie One-electron oxidation of catecholamines generates free radicals with an in vitro toxicity correlating with their lifetime Free Radic. Biol. Med. 41 2006 1266 1271
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 1266-1271
    • Terland, O.1    Almas, B.2    Flatmark, T.3    Andersson, K.K.4    Sorlie, M.5
  • 60
    • 0036074531 scopus 로고    scopus 로고
    • 5-s-Cysteinyl-conjugates of catecholamines induce cell damage, extensive DNA base modification and increases in caspase-3 activity in neurons
    • J.P. Spencer, M. Whiteman, P. Jenner, and B. Halliwell 5-s-Cysteinyl-conjugates of catecholamines induce cell damage, extensive DNA base modification and increases in caspase-3 activity in neurons J. Neurochem. 81 2002 122 129
    • (2002) J. Neurochem. , vol.81 , pp. 122-129
    • Spencer, J.P.1    Whiteman, M.2    Jenner, P.3    Halliwell, B.4


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