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Volumn 1822, Issue 5, 2012, Pages 822-829

Oxidative stress and cerebral endothelial cells: Regulation of the blood-brain-barrier and antioxidant based interventions

Author keywords

Antioxidant; Blood brain barrier; Cerebral endothelial cell; Neurodegeneration; Oxidative stress; Vascularization

Indexed keywords

ACETYLCYSTEINE; ALPHA TOCOPHEROL; ANTIOXIDANT; ASCORBIC ACID; CAROTENOID; FLAVONOID; LEVODOPA; NITECAPONE; NORPHENAZONE; POLYPHENOL; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; RETINOL; SELEGILINE;

EID: 84858153711     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2011.12.009     Document Type: Review
Times cited : (149)

References (136)
  • 1
    • 3242737585 scopus 로고    scopus 로고
    • Energetic basis of brain activity: implications for neuroimaging
    • Shulman R.G., Rothman D.L., Behar K.L., Hyder F. Energetic basis of brain activity: implications for neuroimaging. Trends Neurosci. 2004, 27:489-495.
    • (2004) Trends Neurosci. , vol.27 , pp. 489-495
    • Shulman, R.G.1    Rothman, D.L.2    Behar, K.L.3    Hyder, F.4
  • 2
  • 3
    • 80053458900 scopus 로고    scopus 로고
    • Cerebral microvascular endothelium and the pathogenesis of neurodegenerative diseases
    • Grammas P., Martinez J., Miller B. Cerebral microvascular endothelium and the pathogenesis of neurodegenerative diseases. Expert Rev. Mol. Med. 2011, 13:e19.
    • (2011) Expert Rev. Mol. Med. , vol.13
    • Grammas, P.1    Martinez, J.2    Miller, B.3
  • 4
    • 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, 18:685-716.
    • (2001) Drugs Aging , vol.18 , pp. 685-716
    • Halliwell, B.1
  • 5
    • 0030906870 scopus 로고    scopus 로고
    • Antioxidants and human disease: a general introduction
    • (discussion S49-52)
    • Halliwell B. Antioxidants and human disease: a general introduction. Nutr. Rev. 1997, 55:S44-S49. (discussion S49-52).
    • (1997) Nutr. Rev. , vol.55
    • Halliwell, B.1
  • 6
    • 0032823769 scopus 로고    scopus 로고
    • Antioxidant defence mechanisms: from the beginning to the end (of the beginning)
    • Halliwell B. Antioxidant defence mechanisms: from the beginning to the end (of the beginning). Free Radic. Res. 1999, 31:261-272.
    • (1999) Free Radic. Res. , vol.31 , pp. 261-272
    • Halliwell, B.1
  • 9
    • 0023220937 scopus 로고
    • Enzymatic protection against peroxidative damage in isolated brain capillaries
    • Tayarani I., Chaudiere J., Lefauconnier J.M., Bourre J.M. Enzymatic protection against peroxidative damage in isolated brain capillaries. J. Neurochem. 1987, 48:1399-1402.
    • (1987) J. Neurochem. , vol.48 , pp. 1399-1402
    • Tayarani, I.1    Chaudiere, J.2    Lefauconnier, J.M.3    Bourre, J.M.4
  • 11
  • 13
    • 0032504622 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative disorders
    • Schapira A.H. Mitochondrial dysfunction in neurodegenerative disorders. Biochim. Biophys. Acta 1998, 1366:225-233.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 225-233
    • Schapira, A.H.1
  • 14
    • 84855687153 scopus 로고    scopus 로고
    • Impaired mitochondrial biogenesis contributes to mitochondrial dysfunction in Alzheimer's Disease
    • Sheng B., Wang X., Su B., Lee H.G., Casadesus G., Perry G., Zhu X. Impaired mitochondrial biogenesis contributes to mitochondrial dysfunction in Alzheimer's Disease. J. Neurochem. 2012, 120:419-429.
    • (2012) J. Neurochem. , vol.120 , pp. 419-429
    • Sheng, B.1    Wang, X.2    Su, B.3    Lee, H.G.4    Casadesus, G.5    Perry, G.6    Zhu, X.7
  • 15
    • 77956224679 scopus 로고    scopus 로고
    • The Alzheimer's disease mitochondrial cascade hypothesis
    • Swerdlow R.H., Burns J.M., Khan S.M. The Alzheimer's disease mitochondrial cascade hypothesis. J. Alzheimers Dis. 2010, 20(Suppl 2):S265-S279.
    • (2010) J. Alzheimers Dis. , vol.20 , Issue.SUPPL. 2
    • Swerdlow, R.H.1    Burns, J.M.2    Khan, S.M.3
  • 16
    • 68949158352 scopus 로고    scopus 로고
    • The neurodegenerative mitochondriopathies
    • Swerdlow R.H. The neurodegenerative mitochondriopathies. J. Alzheimers Dis. 2009, 17:737-751.
    • (2009) J. Alzheimers Dis. , vol.17 , pp. 737-751
    • Swerdlow, R.H.1
  • 18
    • 0034612075 scopus 로고    scopus 로고
    • A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients
    • Maurer I., Zierz S., Moller H.J. A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients. Neurobiol. Aging 2000, 21:455-462.
    • (2000) Neurobiol. Aging , vol.21 , pp. 455-462
    • Maurer, I.1    Zierz, S.2    Moller, H.J.3
  • 19
    • 0032973069 scopus 로고    scopus 로고
    • Mitochondrial enzyme expression in the hippocampus in relation to Alzheimer-type pathology
    • Nagy Z., Esiri M.M., LeGris M., Matthews P.M. Mitochondrial enzyme expression in the hippocampus in relation to Alzheimer-type pathology. Acta Neuropathol. 1999, 97:346-354.
    • (1999) Acta Neuropathol. , vol.97 , pp. 346-354
    • Nagy, Z.1    Esiri, M.M.2    LeGris, M.3    Matthews, P.M.4
  • 21
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression
    • Manczak M., Anekonda T.S., Henson E., Park B.S., Quinn J., Reddy P.H. Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum. Mol. Genet. 2006, 15:1437-1449.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5    Reddy, P.H.6
  • 23
    • 0029971210 scopus 로고    scopus 로고
    • Amyloid beta protein primes cultured rat microglial cells for an enhanced phorbol 12-myristate 13-acetate-induced respiratory burst activity
    • Van Muiswinkel F.L., Veerhuis R., Eikelenboom P. Amyloid beta protein primes cultured rat microglial cells for an enhanced phorbol 12-myristate 13-acetate-induced respiratory burst activity. J. Neurochem. 1996, 66:2468-2476.
    • (1996) J. Neurochem. , vol.66 , pp. 2468-2476
    • Van Muiswinkel, F.L.1    Veerhuis, R.2    Eikelenboom, P.3
  • 24
    • 0030795049 scopus 로고    scopus 로고
    • Beta-amyloid protein enhances macrophage production of oxygen free radicals and glutamate
    • Klegeris A., McGeer P.L. beta-amyloid protein enhances macrophage production of oxygen free radicals and glutamate. J. Neurosci. Res. 1997, 49:229-235.
    • (1997) J. Neurosci. Res. , vol.49 , pp. 229-235
    • Klegeris, A.1    McGeer, P.L.2
  • 25
    • 0033845065 scopus 로고    scopus 로고
    • Prevention of beta-amyloid neurotoxicity by blockade of the ubiquitin-proteasome proteolytic pathway
    • Favit A., Grimaldi M., Alkon D.L. Prevention of beta-amyloid neurotoxicity by blockade of the ubiquitin-proteasome proteolytic pathway. J. Neurochem. 2000, 75:1258-1263.
    • (2000) J. Neurochem. , vol.75 , pp. 1258-1263
    • Favit, A.1    Grimaldi, M.2    Alkon, D.L.3
  • 26
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller J.N., Hanni K.B., Markesbery W.R. Impaired proteasome function in Alzheimer's disease. J. Neurochem. 2000, 75:436-439.
    • (2000) J. Neurochem. , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 27
    • 0033972037 scopus 로고    scopus 로고
    • Possible involvement of proteasome inhibition in aging: implications for oxidative stress
    • Keller J.N., Hanni K.B., Markesbery W.R. Possible involvement of proteasome inhibition in aging: implications for oxidative stress. Mech. Ageing Dev. 2000, 113:61-70.
    • (2000) Mech. Ageing Dev. , vol.113 , pp. 61-70
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 29
    • 0028124916 scopus 로고
    • Nitric oxide synthase activity is elevated in brain microvessels in Alzheimer's disease
    • Dorheim M.A., Tracey W.R., Pollock J.S., Grammas P. Nitric oxide synthase activity is elevated in brain microvessels in Alzheimer's disease. Biochem. Biophys. Res. Commun. 1994, 205:659-665.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 659-665
    • Dorheim, M.A.1    Tracey, W.R.2    Pollock, J.S.3    Grammas, P.4
  • 31
    • 41749104745 scopus 로고    scopus 로고
    • Complex I deficiency in Parkinson's disease frontal cortex
    • Parker W.D., Parks J.K., Swerdlow R.H. Complex I deficiency in Parkinson's disease frontal cortex. Brain Res. 2008, 1189:215-218.
    • (2008) Brain Res. , vol.1189 , pp. 215-218
    • Parker, W.D.1    Parks, J.K.2    Swerdlow, R.H.3
  • 32
    • 67649756320 scopus 로고    scopus 로고
    • Impaired mitochondrial dynamics and function in the pathogenesis of Parkinson's disease
    • Bueler H. Impaired mitochondrial dynamics and function in the pathogenesis of Parkinson's disease. Exp. Neurol. 2009, 218:235-246.
    • (2009) Exp. Neurol. , vol.218 , pp. 235-246
    • Bueler, H.1
  • 33
    • 33646948530 scopus 로고    scopus 로고
    • Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled
    • Keeney P.M., Xie J., Capaldi R.A., Bennett J.P. Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled. J. Neurosci. 2006, 26:5256-5264.
    • (2006) J. Neurosci. , vol.26 , pp. 5256-5264
    • Keeney, P.M.1    Xie, J.2    Capaldi, R.A.3    Bennett, J.P.4
  • 34
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: mechanisms and models
    • Dauer W., Przedborski S. Parkinson's disease: mechanisms and models. Neuron 2003, 39:889-909.
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 35
    • 49349106093 scopus 로고    scopus 로고
    • Redox imbalance in Parkinson's disease
    • Chinta S.J., Andersen J.K. Redox imbalance in Parkinson's disease. Biochim. Biophys. Acta 2008, 1780:1362-1367.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 1362-1367
    • Chinta, S.J.1    Andersen, J.K.2
  • 36
    • 0020680904 scopus 로고
    • Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis
    • Langston J.W., Ballard P., Tetrud J.W., Irwin I. Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis. Science 1983, 219:979-980.
    • (1983) Science , vol.219 , pp. 979-980
    • Langston, J.W.1    Ballard, P.2    Tetrud, J.W.3    Irwin, I.4
  • 37
    • 0023610067 scopus 로고
    • MPTP: an industrial chemical and contaminant of illicit narcotics stimulates a new era in research on Parkinson's disease
    • Kopin I.J. MPTP: an industrial chemical and contaminant of illicit narcotics stimulates a new era in research on Parkinson's disease. Environ. Health Perspect. 1987, 75:45-51.
    • (1987) Environ. Health Perspect. , vol.75 , pp. 45-51
    • Kopin, I.J.1
  • 40
    • 0037127197 scopus 로고    scopus 로고
    • The herbicide paraquat causes up-regulation and aggregation of alpha-synuclein in mice: paraquat and alpha-synuclein
    • Manning-Bog A.B., McCormack A.L., Li J., Uversky V.N., Fink A.L., Di Monte D.A. The herbicide paraquat causes up-regulation and aggregation of alpha-synuclein in mice: paraquat and alpha-synuclein. J. Biol. Chem. 2002, 277:1641-1644.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1641-1644
    • Manning-Bog, A.B.1    McCormack, A.L.2    Li, J.3    Uversky, V.N.4    Fink, A.L.5    Di Monte, D.A.6
  • 45
    • 33747179913 scopus 로고    scopus 로고
    • Parkin affects mitochondrial function and apoptosis in neuronal and myogenic cells
    • Kuroda Y., Mitsui T., Kunishige M., Matsumoto T. Parkin affects mitochondrial function and apoptosis in neuronal and myogenic cells. Biochem. Biophys. Res. Commun. 2006, 348:787-793.
    • (2006) Biochem. Biophys. Res. Commun. , vol.348 , pp. 787-793
    • Kuroda, Y.1    Mitsui, T.2    Kunishige, M.3    Matsumoto, T.4
  • 46
  • 47
    • 79956198149 scopus 로고    scopus 로고
    • Mechanisms of neurodegeneration shared between multiple sclerosis and Alzheimer's disease
    • Lassmann H. Mechanisms of neurodegeneration shared between multiple sclerosis and Alzheimer's disease. J. Neural Transm. 2011, 118:747-752.
    • (2011) J. Neural Transm. , vol.118 , pp. 747-752
    • Lassmann, H.1
  • 49
    • 79958771184 scopus 로고    scopus 로고
    • Pathophysiology of inflammation and tissue injury in multiple sclerosis: what are the targets for therapy
    • Lassmann H. Pathophysiology of inflammation and tissue injury in multiple sclerosis: what are the targets for therapy. J. Neurol. Sci. 2011, 306:167-169.
    • (2011) J. Neurol. Sci. , vol.306 , pp. 167-169
    • Lassmann, H.1
  • 50
    • 56549086013 scopus 로고    scopus 로고
    • Review: Mitochondria and disease progression in multiple sclerosis
    • Mahad D., Lassmann H., Turnbull D. Review: Mitochondria and disease progression in multiple sclerosis. Neuropathol. Appl. Neurobiol. 2008, 34:577-589.
    • (2008) Neuropathol. Appl. Neurobiol. , vol.34 , pp. 577-589
    • Mahad, D.1    Lassmann, H.2    Turnbull, D.3
  • 54
    • 77956224840 scopus 로고    scopus 로고
    • Mitochondrial dysfunction is a converging point of multiple pathological pathways in amyotrophic lateral sclerosis
    • Shi P., Wei Y., Zhang J., Gal J., Zhu H. Mitochondrial dysfunction is a converging point of multiple pathological pathways in amyotrophic lateral sclerosis. J. Alzheimers Dis. 2010, 20(Suppl 2):S311-S324.
    • (2010) J. Alzheimers Dis. , vol.20 , Issue.SUPPL. 2
    • Shi, P.1    Wei, Y.2    Zhang, J.3    Gal, J.4    Zhu, H.5
  • 56
    • 0037088793 scopus 로고    scopus 로고
    • Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS
    • Higgins C.M., Jung C., Ding H., Xu Z. Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS. J. Neurosci. 2002, 22:RC215.
    • (2002) J. Neurosci. , vol.22
    • Higgins, C.M.1    Jung, C.2    Ding, H.3    Xu, Z.4
  • 57
    • 3242703300 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria
    • Pasinelli P., Belford M.E., Lennon N., Bacskai B.J., Hyman B.T., Trotti D., Brown R.H. Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria. Neuron 2004, 43:19-30.
    • (2004) Neuron , vol.43 , pp. 19-30
    • Pasinelli, P.1    Belford, M.E.2    Lennon, N.3    Bacskai, B.J.4    Hyman, B.T.5    Trotti, D.6    Brown, R.H.7
  • 58
    • 0033826065 scopus 로고    scopus 로고
    • Differential screening of mutated SOD1 transgenic mice reveals early up-regulation of a fast axonal transport component in spinal cord motor neurons
    • Dupuis L., de Tapia M., Rene F., Lutz-Bucher B., Gordon J.W., Mercken L., Pradier L., Loeffler J.P. Differential screening of mutated SOD1 transgenic mice reveals early up-regulation of a fast axonal transport component in spinal cord motor neurons. Neurobiol. Dis. 2000, 7:274-285.
    • (2000) Neurobiol. Dis. , vol.7 , pp. 274-285
    • Dupuis, L.1    de Tapia, M.2    Rene, F.3    Lutz-Bucher, B.4    Gordon, J.W.5    Mercken, L.6    Pradier, L.7    Loeffler, J.P.8
  • 59
    • 57249086430 scopus 로고    scopus 로고
    • Morphine and HIV-Tat increase microglial-free radical production and oxidative stress: possible role in cytokine regulation
    • Turchan-Cholewo J., Dimayuga F.O., Gupta S., Keller J.N., Knapp P.E., Hauser K.F., Bruce-Keller A.J. Morphine and HIV-Tat increase microglial-free radical production and oxidative stress: possible role in cytokine regulation. J. Neurochem. 2009, 108:202-215.
    • (2009) J. Neurochem. , vol.108 , pp. 202-215
    • Turchan-Cholewo, J.1    Dimayuga, F.O.2    Gupta, S.3    Keller, J.N.4    Knapp, P.E.5    Hauser, K.F.6    Bruce-Keller, A.J.7
  • 63
    • 0035095564 scopus 로고    scopus 로고
    • Brain iron transport and neurodegeneration
    • Qian Z.M., Shen X. Brain iron transport and neurodegeneration. Trends Mol. Med. 2001, 7:103-108.
    • (2001) Trends Mol. Med. , vol.7 , pp. 103-108
    • Qian, Z.M.1    Shen, X.2
  • 65
    • 83755190692 scopus 로고    scopus 로고
    • Caveolin-1 regulates nitric oxide-mediated matrix metalloproteinases activity and blood-brain barrier permeability in focal cerebral ischemia and reperfusion injury
    • Gu Y., Zheng G., Xu M., Li Y., Chen X., Zhu W., Tong Y., Chung S.K., Liu K.J., Shen J. Caveolin-1 regulates nitric oxide-mediated matrix metalloproteinases activity and blood-brain barrier permeability in focal cerebral ischemia and reperfusion injury. J. Neurochem. 2012, 120:147-156.
    • (2012) J. Neurochem. , vol.120 , pp. 147-156
    • Gu, Y.1    Zheng, G.2    Xu, M.3    Li, Y.4    Chen, X.5    Zhu, W.6    Tong, Y.7    Chung, S.K.8    Liu, K.J.9    Shen, J.10
  • 66
    • 80053121818 scopus 로고    scopus 로고
    • Interaction of free radicals, matrix metalloproteinases and caveolin-1 impacts blood-brain barrier permeability
    • Gu Y., Dee C.M., Shen J. Interaction of free radicals, matrix metalloproteinases and caveolin-1 impacts blood-brain barrier permeability. Front. Biosci. (Schol. Ed.) 2011, 3:1216-1231.
    • (2011) Front. Biosci. (Schol. Ed.) , vol.3 , pp. 1216-1231
    • Gu, Y.1    Dee, C.M.2    Shen, J.3
  • 67
    • 38149090292 scopus 로고    scopus 로고
    • The blood-brain barrier in health and chronic neurodegenerative disorders
    • Zlokovic B.V. The blood-brain barrier in health and chronic neurodegenerative disorders. Neuron 2008, 57:178-201.
    • (2008) Neuron , vol.57 , pp. 178-201
    • Zlokovic, B.V.1
  • 68
    • 79960998682 scopus 로고    scopus 로고
    • Current concepts of blood-brain barrier development
    • Liebner S., Czupalla C.J., Wolburg H. Current concepts of blood-brain barrier development. Int. J. Dev. Biol. 2011, 55:467-476.
    • (2011) Int. J. Dev. Biol. , vol.55 , pp. 467-476
    • Liebner, S.1    Czupalla, C.J.2    Wolburg, H.3
  • 70
    • 0032752658 scopus 로고    scopus 로고
    • Potential role of cerebral glutathione in the maintenance of blood-brain barrier integrity in rat
    • Agarwal R., Shukla G.S. Potential role of cerebral glutathione in the maintenance of blood-brain barrier integrity in rat. Neurochem. Res. 1999, 24:1507-1514.
    • (1999) Neurochem. Res. , vol.24 , pp. 1507-1514
    • Agarwal, R.1    Shukla, G.S.2
  • 71
    • 0031666630 scopus 로고    scopus 로고
    • Vitamin E and other endogenous antioxidants in the central nervous system
    • Vatassery G.T. Vitamin E and other endogenous antioxidants in the central nervous system. Geriatrics 1998, 53(Suppl 1):S25-S27.
    • (1998) Geriatrics , vol.53 , Issue.SUPPL. 1
    • Vatassery, G.T.1
  • 72
    • 67649840689 scopus 로고    scopus 로고
    • Regulation of superoxide dismutase genes: implications in disease
    • Miao L., St Clair D.K. Regulation of superoxide dismutase genes: implications in disease. Free Radic. Biol. Med. 2009, 47:344-356.
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 344-356
    • Miao, L.1    St Clair, D.K.2
  • 73
    • 77955282773 scopus 로고    scopus 로고
    • Nitric oxide and oxidative stress in vascular disease
    • Forstermann U. Nitric oxide and oxidative stress in vascular disease. Pflugers Arch. 2010, 459:923-939.
    • (2010) Pflugers Arch. , vol.459 , pp. 923-939
    • Forstermann, U.1
  • 74
    • 79955057180 scopus 로고    scopus 로고
    • The Nrf2/ARE Pathway: A Promising Target to Counteract Mitochondrial Dysfunction in Parkinson's Disease
    • Tufekci K.U., Civi Bayin E., Genc S., Genc K. The Nrf2/ARE Pathway: A Promising Target to Counteract Mitochondrial Dysfunction in Parkinson's Disease. Parkinsons Dis 2011, 2011:314082.
    • (2011) Parkinsons Dis , vol.2011 , pp. 314082
    • Tufekci, K.U.1    Civi Bayin, E.2    Genc, S.3    Genc, K.4
  • 75
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K., Wakabayashi N., Katoh Y., Ishii T., Igarashi K., Engel J.D., Yamamoto M. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev. 1999, 13:76-86.
    • (1999) Genes Dev. , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 76
    • 0031424783 scopus 로고    scopus 로고
    • Inflammatory events at the blood brain barrier: regulation of adhesion molecules, cytokines, and chemokines by reactive nitrogen and oxygen species
    • Merrill J.E., Murphy S.P. Inflammatory events at the blood brain barrier: regulation of adhesion molecules, cytokines, and chemokines by reactive nitrogen and oxygen species. Brain Behav. Immun. 1997, 11:245-263.
    • (1997) Brain Behav. Immun. , vol.11 , pp. 245-263
    • Merrill, J.E.1    Murphy, S.P.2
  • 77
    • 0027939807 scopus 로고
    • Gases as biological messengers: nitric oxide and carbon monoxide in the brain
    • Dawson T.M., Snyder S.H. Gases as biological messengers: nitric oxide and carbon monoxide in the brain. J. Neurosci. 1994, 14:5147-5159.
    • (1994) J. Neurosci. , vol.14 , pp. 5147-5159
    • Dawson, T.M.1    Snyder, S.H.2
  • 78
    • 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, 19:33-36.
    • (1998) Neurobiol. Aging , vol.19 , pp. 33-36
    • Markesbery, W.R.1    Lovell, M.A.2
  • 79
    • 77953257870 scopus 로고    scopus 로고
    • Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease
    • Butterfield D.A., Bader Lange M.L., Sultana R. Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease. Biochim. Biophys. Acta 2010, 1801:924-929.
    • (2010) Biochim. Biophys. Acta , vol.1801 , pp. 924-929
    • Butterfield, D.A.1    Bader Lange, M.L.2    Sultana, R.3
  • 80
    • 0043172468 scopus 로고    scopus 로고
    • 4-hydroxynonenal and neurodegenerative diseases
    • Zarkovic K. 4-hydroxynonenal and neurodegenerative diseases. Mol. Aspects Med. 2003, 24:293-303.
    • (2003) Mol. Aspects Med. , vol.24 , pp. 293-303
    • Zarkovic, K.1
  • 81
    • 0023869451 scopus 로고
    • Effect of aging on the blood-brain barrier
    • Mooradian A.D. Effect of aging on the blood-brain barrier. Neurobiol. Aging 1988, 9:31-39.
    • (1988) Neurobiol. Aging , vol.9 , pp. 31-39
    • Mooradian, A.D.1
  • 82
    • 77449152992 scopus 로고    scopus 로고
    • Oxidative stress and its role in the pathogenesis of ischaemic stroke
    • Allen C.L., Bayraktutan U. Oxidative stress and its role in the pathogenesis of ischaemic stroke. Int. J. Stroke 2009, 4:461-470.
    • (2009) Int. J. Stroke , vol.4 , pp. 461-470
    • Allen, C.L.1    Bayraktutan, U.2
  • 83
    • 33748326080 scopus 로고    scopus 로고
    • NADPH-oxidase activity is elevated in penumbral and non-ischemic cerebral arteries following stroke
    • Miller A.A., Dusting G.J., Roulston C.L., Sobey C.G. NADPH-oxidase activity is elevated in penumbral and non-ischemic cerebral arteries following stroke. Brain Res. 2006, 1111:111-116.
    • (2006) Brain Res. , vol.1111 , pp. 111-116
    • Miller, A.A.1    Dusting, G.J.2    Roulston, C.L.3    Sobey, C.G.4
  • 84
    • 0842289183 scopus 로고    scopus 로고
    • Increased NADPH-oxidase activity and Nox4 expression during chronic hypertension is associated with enhanced cerebral vasodilatation to NADPH in vivo
    • Paravicini T.M., Chrissobolis S., Drummond G.R., Sobey C.G. Increased NADPH-oxidase activity and Nox4 expression during chronic hypertension is associated with enhanced cerebral vasodilatation to NADPH in vivo. Stroke 2004, 35:584-589.
    • (2004) Stroke , vol.35 , pp. 584-589
    • Paravicini, T.M.1    Chrissobolis, S.2    Drummond, G.R.3    Sobey, C.G.4
  • 85
    • 0031685094 scopus 로고    scopus 로고
    • Role of potassium channels in regulation of cerebral vascular tone
    • Faraci F.M., Sobey C.G. Role of potassium channels in regulation of cerebral vascular tone. J. Cereb. Blood Flow Metab. 1998, 18:1047-1063.
    • (1998) J. Cereb. Blood Flow Metab. , vol.18 , pp. 1047-1063
    • Faraci, F.M.1    Sobey, C.G.2
  • 86
    • 79957603259 scopus 로고    scopus 로고
    • Milestones in Parkinson's disease therapeutics
    • Rascol O., Lozano A., Stern M., Poewe W. Milestones in Parkinson's disease therapeutics. Mov. Disord. 2011, 26:1072-1082.
    • (2011) Mov. Disord. , vol.26 , pp. 1072-1082
    • Rascol, O.1    Lozano, A.2    Stern, M.3    Poewe, W.4
  • 88
    • 0346154805 scopus 로고    scopus 로고
    • Clinical pharmacology of MAO inhibitors: safety and future
    • Yamada M., Yasuhara H. Clinical pharmacology of MAO inhibitors: safety and future. Neurotoxicology 2004, 25:215-221.
    • (2004) Neurotoxicology , vol.25 , pp. 215-221
    • Yamada, M.1    Yasuhara, H.2
  • 89
    • 31044453010 scopus 로고    scopus 로고
    • Effects of selegiline on antioxidant systems in the nigrostriatum in rat
    • Takahata K., Shimazu S., Katsuki H., Yoneda F., Akaike A. Effects of selegiline on antioxidant systems in the nigrostriatum in rat. J. Neural Transm. 2006, 113:151-158.
    • (2006) J. Neural Transm. , vol.113 , pp. 151-158
    • Takahata, K.1    Shimazu, S.2    Katsuki, H.3    Yoneda, F.4    Akaike, A.5
  • 90
    • 80155177695 scopus 로고    scopus 로고
    • The evidence for disease modification in Parkinson's disease
    • Lew M.F. The evidence for disease modification in Parkinson's disease. Int. J. Neurosci. 2011, 121(Suppl 2):18-26.
    • (2011) Int. J. Neurosci. , vol.121 , Issue.SUPPL. 2 , pp. 18-26
    • Lew, M.F.1
  • 91
    • 36849087430 scopus 로고    scopus 로고
    • Novel screening assay for antioxidant protection against peroxyl radical-induced loss of protein function
    • Bertolini F., Novaroli L., Carrupt P.A., Reist M. Novel screening assay for antioxidant protection against peroxyl radical-induced loss of protein function. J. Pharm. Sci. 2007, 96:2931-2944.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 2931-2944
    • Bertolini, F.1    Novaroli, L.2    Carrupt, P.A.3    Reist, M.4
  • 92
    • 0345647071 scopus 로고    scopus 로고
    • Extending levodopa action: COMT inhibition
    • (discussion S44-28)
    • Martinez-Martin P., O'Brien C.F. Extending levodopa action: COMT inhibition. Neurology 1998, 50:S27-S32. (discussion S44-28).
    • (1998) Neurology , vol.50
    • Martinez-Martin, P.1    O'Brien, C.F.2
  • 93
    • 0028137620 scopus 로고
    • Effect of entacapone, a peripherally acting catechol-O-methyltransferase inhibitor, on the motor response to acute treatment with levodopa in patients with Parkinson's disease
    • Merello M., Lees A.J., Webster R., Bovingdon M., Gordin A. Effect of entacapone, a peripherally acting catechol-O-methyltransferase inhibitor, on the motor response to acute treatment with levodopa in patients with Parkinson's disease. J. Neurol. Neurosurg. Psychiatry 1994, 57:186-189.
    • (1994) J. Neurol. Neurosurg. Psychiatry , vol.57 , pp. 186-189
    • Merello, M.1    Lees, A.J.2    Webster, R.3    Bovingdon, M.4    Gordin, A.5
  • 94
    • 79955548741 scopus 로고    scopus 로고
    • Management of paracetamol poisoning
    • Ferner R.E., Dear J.W., Bateman D.N. Management of paracetamol poisoning. BMJ 2011, 342:d2218.
    • (2011) BMJ , vol.342
    • Ferner, R.E.1    Dear, J.W.2    Bateman, D.N.3
  • 95
    • 79955035339 scopus 로고    scopus 로고
    • Chronic N-acetylcysteine during abstinence or extinction after cocaine self-administration produces enduring reductions in drug seeking
    • Reichel C.M., Moussawi K., Do P.H., Kalivas P.W., See R.E. Chronic N-acetylcysteine during abstinence or extinction after cocaine self-administration produces enduring reductions in drug seeking. J. Pharmacol. Exp. Ther. 2011, 337:487-493.
    • (2011) J. Pharmacol. Exp. Ther. , vol.337 , pp. 487-493
    • Reichel, C.M.1    Moussawi, K.2    Do, P.H.3    Kalivas, P.W.4    See, R.E.5
  • 96
    • 79956004865 scopus 로고    scopus 로고
    • Nutraceuticals in the treatment of obsessive compulsive disorder (OCD): a review of mechanistic and clinical evidence
    • Camfield D.A., Sarris J., Berk M. Nutraceuticals in the treatment of obsessive compulsive disorder (OCD): a review of mechanistic and clinical evidence. Prog. Neuropsychopharmacol. Biol. Psychiatry 2011, 35:887-895.
    • (2011) Prog. Neuropsychopharmacol. Biol. Psychiatry , vol.35 , pp. 887-895
    • Camfield, D.A.1    Sarris, J.2    Berk, M.3
  • 97
    • 67649340808 scopus 로고    scopus 로고
    • Hyperglycemia-induced alterations in synaptosomal membrane fluidity and activity of membrane bound enzymes: beneficial effect of N-acetylcysteine supplementation
    • Kamboj S.S., Chopra K., Sandhir R. Hyperglycemia-induced alterations in synaptosomal membrane fluidity and activity of membrane bound enzymes: beneficial effect of N-acetylcysteine supplementation. Neuroscience 2009, 162:349-358.
    • (2009) Neuroscience , vol.162 , pp. 349-358
    • Kamboj, S.S.1    Chopra, K.2    Sandhir, R.3
  • 99
    • 44349104572 scopus 로고    scopus 로고
    • The antioxidant role of glutathione and N-acetyl-cysteine supplements and exercise-induced oxidative stress
    • Kerksick C., Willoughby D. The antioxidant role of glutathione and N-acetyl-cysteine supplements and exercise-induced oxidative stress. J Int Soc Sports Nutr 2005, 2:38-44.
    • (2005) J Int Soc Sports Nutr , vol.2 , pp. 38-44
    • Kerksick, C.1    Willoughby, D.2
  • 100
    • 0024394697 scopus 로고
    • The antioxidant action of N-acetylcysteine: its reaction with hydrogen peroxide, hydroxyl radical, superoxide, and hypochlorous acid
    • Aruoma O.I., Halliwell B., Hoey B.M., Butler J. The antioxidant action of N-acetylcysteine: its reaction with hydrogen peroxide, hydroxyl radical, superoxide, and hypochlorous acid. Free Radic. Biol. Med. 1989, 6:593-597.
    • (1989) Free Radic. Biol. Med. , vol.6 , pp. 593-597
    • Aruoma, O.I.1    Halliwell, B.2    Hoey, B.M.3    Butler, J.4
  • 102
    • 65449119946 scopus 로고    scopus 로고
    • N-acetylcysteine amide decreases oxidative stress but not cell death induced by doxorubicin in H9c2 cardiomyocytes
    • Shi R., Huang C.C., Aronstam R.S., Ercal N., Martin A., Huang Y.W. N-acetylcysteine amide decreases oxidative stress but not cell death induced by doxorubicin in H9c2 cardiomyocytes. BMC Pharmacol. 2009, 9:7.
    • (2009) BMC Pharmacol. , vol.9 , pp. 7
    • Shi, R.1    Huang, C.C.2    Aronstam, R.S.3    Ercal, N.4    Martin, A.5    Huang, Y.W.6
  • 103
    • 79960202053 scopus 로고    scopus 로고
    • A randomized controlled clinical trial to compare the safety and efficacy of edaravone in acute ischemic stroke
    • Sharma P., Sinha M., Shukla R., Garg R.K., Verma R., Singh M.K. A randomized controlled clinical trial to compare the safety and efficacy of edaravone in acute ischemic stroke. Ann Indian Acad Neurol 2011, 14:103-106.
    • (2011) Ann Indian Acad Neurol , vol.14 , pp. 103-106
    • Sharma, P.1    Sinha, M.2    Shukla, R.3    Garg, R.K.4    Verma, R.5    Singh, M.K.6
  • 104
    • 79953103571 scopus 로고    scopus 로고
    • Free radical scavenger, edaravone, reduces the lesion size of lacunar infarction in human brain ischemic stroke
    • Nakase T., Yoshioka S., Suzuki A. Free radical scavenger, edaravone, reduces the lesion size of lacunar infarction in human brain ischemic stroke. BMC Neurol. 2011, 11:39.
    • (2011) BMC Neurol. , vol.11 , pp. 39
    • Nakase, T.1    Yoshioka, S.2    Suzuki, A.3
  • 105
    • 34250730257 scopus 로고    scopus 로고
    • Edaravone (3-methyl-1-phenyl-2-pyrazolin-5-one), a radical scavenger, prevents 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced neurotoxicity in the substantia nigra but not the striatum
    • Kawasaki T., Ishihara K., Ago Y., Baba A., Matsuda T. Edaravone (3-methyl-1-phenyl-2-pyrazolin-5-one), a radical scavenger, prevents 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced neurotoxicity in the substantia nigra but not the striatum. J. Pharmacol. Exp. Ther. 2007, 322:274-281.
    • (2007) J. Pharmacol. Exp. Ther. , vol.322 , pp. 274-281
    • Kawasaki, T.1    Ishihara, K.2    Ago, Y.3    Baba, A.4    Matsuda, T.5
  • 108
    • 60549111009 scopus 로고    scopus 로고
    • Edaravone, a free radical scavenger, inhibits MMP-9-related brain hemorrhage in rats treated with tissue plasminogen activator
    • Yagi K., Kitazato K.T., Uno M., Tada Y., Kinouchi T., Shimada K., Nagahiro S. Edaravone, a free radical scavenger, inhibits MMP-9-related brain hemorrhage in rats treated with tissue plasminogen activator. Stroke 2009, 40:626-631.
    • (2009) Stroke , vol.40 , pp. 626-631
    • Yagi, K.1    Kitazato, K.T.2    Uno, M.3    Tada, Y.4    Kinouchi, T.5    Shimada, K.6    Nagahiro, S.7
  • 109
    • 7944227151 scopus 로고    scopus 로고
    • Efficacy of dietary antioxidants to prevent oxidative damage and inhibit chronic disease
    • Frei B. Efficacy of dietary antioxidants to prevent oxidative damage and inhibit chronic disease. J. Nutr. 2004, 134:3196S-3198S.
    • (2004) J. Nutr. , vol.134
    • Frei, B.1
  • 110
    • 84856220825 scopus 로고    scopus 로고
    • Strategies to target mitochondria and oxidative stress by antioxidants: key points and perspectives
    • Edeas M. Strategies to target mitochondria and oxidative stress by antioxidants: key points and perspectives. Pharm. Res. 2011, 28:2771-2779.
    • (2011) Pharm. Res. , vol.28 , pp. 2771-2779
    • Edeas, M.1
  • 111
    • 0037093739 scopus 로고    scopus 로고
    • Effect of diet on cancer development: is oxidative DNA damage a biomarker?
    • Halliwell B. Effect of diet on cancer development: is oxidative DNA damage a biomarker?. Free Radic. Biol. Med. 2002, 32:968-974.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 968-974
    • Halliwell, B.1
  • 112
    • 78649465557 scopus 로고    scopus 로고
    • Antioxidant vitamins and their use in preventing cardiovascular disease
    • Farbstein D., Kozak-Blickstein A., Levy A.P. Antioxidant vitamins and their use in preventing cardiovascular disease. Molecules 2010, 15:8098-8110.
    • (2010) Molecules , vol.15 , pp. 8098-8110
    • Farbstein, D.1    Kozak-Blickstein, A.2    Levy, A.P.3
  • 114
    • 0036084541 scopus 로고    scopus 로고
    • Antioxidant strategies for Alzheimer's disease
    • Grundman M., Delaney P. Antioxidant strategies for Alzheimer's disease. Proc. Nutr. Soc. 2002, 61:191-202.
    • (2002) Proc. Nutr. Soc. , vol.61 , pp. 191-202
    • Grundman, M.1    Delaney, P.2
  • 116
    • 0032921546 scopus 로고    scopus 로고
    • Plasma chain-breaking antioxidants in Alzheimer's disease, vascular dementia and Parkinson's disease
    • Foy C.J., Passmore A.P., Vahidassr M.D., Young I.S., Lawson J.T. Plasma chain-breaking antioxidants in Alzheimer's disease, vascular dementia and Parkinson's disease. QJM 1999, 92:39-45.
    • (1999) QJM , vol.92 , pp. 39-45
    • Foy, C.J.1    Passmore, A.P.2    Vahidassr, M.D.3    Young, I.S.4    Lawson, J.T.5
  • 119
    • 0026547646 scopus 로고
    • Plasma concentrations of vitamins A and E and carotenoids in Alzheimer's disease
    • Zaman Z., Roche S., Fielden P., Frost P.G., Niriella D.C., Cayley A.C. Plasma concentrations of vitamins A and E and carotenoids in Alzheimer's disease. Age Ageing 1992, 21:91-94.
    • (1992) Age Ageing , vol.21 , pp. 91-94
    • Zaman, Z.1    Roche, S.2    Fielden, P.3    Frost, P.G.4    Niriella, D.C.5    Cayley, A.C.6
  • 123
    • 0032125872 scopus 로고    scopus 로고
    • Cohort study of vitamin C intake and cognitive impairment
    • Paleologos M., Cumming R.G., Lazarus R. Cohort study of vitamin C intake and cognitive impairment. Am. J. Epidemiol. 1998, 148:45-50.
    • (1998) Am. J. Epidemiol. , vol.148 , pp. 45-50
    • Paleologos, M.1    Cumming, R.G.2    Lazarus, R.3
  • 124
    • 79955457391 scopus 로고    scopus 로고
    • The role of vitamin E (tocopherol) supplementation in the prevention of stroke. A meta-analysis of 13 randomised controlled trials
    • Bin Q., Hu X., Cao Y., Gao F. The role of vitamin E (tocopherol) supplementation in the prevention of stroke. A meta-analysis of 13 randomised controlled trials. Thromb. Haemost. 2011, 105:579-585.
    • (2011) Thromb. Haemost. , vol.105 , pp. 579-585
    • Bin, Q.1    Hu, X.2    Cao, Y.3    Gao, F.4
  • 125
    • 28544444991 scopus 로고    scopus 로고
    • Vitamin C and vitamin E for Alzheimer's disease
    • Boothby L.A., Doering P.L. Vitamin C and vitamin E for Alzheimer's disease. Ann. Pharmacother. 2005, 39:2073-2080.
    • (2005) Ann. Pharmacother. , vol.39 , pp. 2073-2080
    • Boothby, L.A.1    Doering, P.L.2
  • 126
    • 0033042955 scopus 로고    scopus 로고
    • Establishing the significance and optimal intake of dietary antioxidants: the biomarker concept
    • Halliwell B. Establishing the significance and optimal intake of dietary antioxidants: the biomarker concept. Nutr. Rev. 1999, 57:104-113.
    • (1999) Nutr. Rev. , vol.57 , pp. 104-113
    • Halliwell, B.1
  • 127
    • 65249103435 scopus 로고    scopus 로고
    • Nox4 NADPH oxidase mediates oxidative stress and apoptosis caused by TNF-alpha in cerebral vascular endothelial cells
    • Basuroy S., Bhattacharya S., Leffler C.W., Parfenova H. Nox4 NADPH oxidase mediates oxidative stress and apoptosis caused by TNF-alpha in cerebral vascular endothelial cells. Am. J. Physiol. Cell Physiol. 2009, 296:C422-C432.
    • (2009) Am. J. Physiol. Cell Physiol. , vol.296
    • Basuroy, S.1    Bhattacharya, S.2    Leffler, C.W.3    Parfenova, H.4
  • 132
    • 78650882643 scopus 로고    scopus 로고
    • Reactive oxygen species and vascular biology: implications in human hypertension
    • Touyz R.M., Briones A.M. Reactive oxygen species and vascular biology: implications in human hypertension. Hypertens. Res. 2011, 34:5-14.
    • (2011) Hypertens. Res. , vol.34 , pp. 5-14
    • Touyz, R.M.1    Briones, A.M.2
  • 134
  • 135
    • 0033742539 scopus 로고    scopus 로고
    • Ironing-out mechanisms of neuronal injury under hypoxic-ischemic conditions and potential role of iron chelators as neuroprotective agents
    • Sorond F.A., Ratan R.R. Ironing-out mechanisms of neuronal injury under hypoxic-ischemic conditions and potential role of iron chelators as neuroprotective agents. Antioxid. Redox Signal. 2000, 2:421-436.
    • (2000) Antioxid. Redox Signal. , vol.2 , pp. 421-436
    • Sorond, F.A.1    Ratan, R.R.2
  • 136
    • 67449128444 scopus 로고    scopus 로고
    • Occludin oligomeric assemblies at tight junctions of the blood-brain barrier are altered by hypoxia and reoxygenation stress
    • McCaffrey G., Willis C.L., Staatz W.D., Nametz N., Quigley C.A., Hom S., Lochhead J.J., Davis T.P. Occludin oligomeric assemblies at tight junctions of the blood-brain barrier are altered by hypoxia and reoxygenation stress. J. Neurochem. 2009, 110:58-71.
    • (2009) J. Neurochem. , vol.110 , pp. 58-71
    • McCaffrey, G.1    Willis, C.L.2    Staatz, W.D.3    Nametz, N.4    Quigley, C.A.5    Hom, S.6    Lochhead, J.J.7    Davis, T.P.8


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