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Volumn 22, Issue 1, 2011, Pages 22-29

Docosahexaenoic acid withstands the Aβ25-35-induced neurotoxicity in SH-SY5Y cells

Author keywords

A 25 35 fibrillation; Docosahexaenoic acid; Neurotoxicity; SH SY5Y cells

Indexed keywords

AMYLOID BETA PROTEIN[25-35]; DOCOSAHEXAENOIC ACID; FATTY ACID; LIPID PEROXIDE;

EID: 78649922280     PISSN: 09552863     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jnutbio.2009.11.005     Document Type: Article
Times cited : (31)

References (48)
  • 1
    • 0036319034 scopus 로고    scopus 로고
    • Docosahexaenoic acid provides protection from impairment of learning ability in Alzheimer's disease model rats
    • Hashimoto M., Hossain S., Shimada T., Sugioka K., Yamasaki H., Fujii Y., et al. Docosahexaenoic acid provides protection from impairment of learning ability in Alzheimer's disease model rats. J Neurochem 2002, 81:1084-1091.
    • (2002) J Neurochem , vol.81 , pp. 1084-1091
    • Hashimoto, M.1    Hossain, S.2    Shimada, T.3    Sugioka, K.4    Yamasaki, H.5    Fujii, Y.6
  • 2
    • 14944376646 scopus 로고    scopus 로고
    • Chronic administration of docosahexaenoic acid ameliorates the impairment of spatial cognition learning ability in amyloid β-infused rats
    • Hashimoto M., Tanabe Y., Fujii Y., Kikuta T., Shibata H., Shido O. Chronic administration of docosahexaenoic acid ameliorates the impairment of spatial cognition learning ability in amyloid β-infused rats. J Nutr 2005, 135:549-555.
    • (2005) J Nutr , vol.135 , pp. 549-555
    • Hashimoto, M.1    Tanabe, Y.2    Fujii, Y.3    Kikuta, T.4    Shibata, H.5    Shido, O.6
  • 3
    • 16244416174 scopus 로고    scopus 로고
    • A diet enriched with the omega-3 fatty acid docosahexaenoic acid reduces amyloid burden in an aged Alzheimer mouse model
    • Lim G.P., Calon F., Morihara T., Yang F., Teter B., Ubeda O., et al. A diet enriched with the omega-3 fatty acid docosahexaenoic acid reduces amyloid burden in an aged Alzheimer mouse model. J Neurosci 2005, 25:3032-3040.
    • (2005) J Neurosci , vol.25 , pp. 3032-3040
    • Lim, G.P.1    Calon, F.2    Morihara, T.3    Yang, F.4    Teter, B.5    Ubeda, O.6
  • 4
    • 33750982113 scopus 로고    scopus 로고
    • Plasma Phosphatidylcholine Docosahexaenoic acid content and risk of dementia and Alzheimer disease The Framingham Heart Study
    • Schaefer E.J., Bongard V., Beiser A.S., Lamon-Fava S., Robins S.J., Au R., et al. Plasma Phosphatidylcholine Docosahexaenoic acid content and risk of dementia and Alzheimer disease The Framingham Heart Study. Arch Neurol 2006, 63:1545-1550.
    • (2006) Arch Neurol , vol.63 , pp. 1545-1550
    • Schaefer, E.J.1    Bongard, V.2    Beiser, A.S.3    Lamon-Fava, S.4    Robins, S.J.5    Au, R.6
  • 5
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe D.J. The molecular pathology of Alzheimer's disease. Neuron 1991, 6:487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 6
    • 0028169925 scopus 로고
    • Visualization of Aβ 42(43) and Aβ 40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is Aβ 42(43)
    • Iwatsubo T., Odaka A., Suzuki N., Mizusawa H., Nukina N., Ihara Y. Visualization of Aβ 42(43) and Aβ 40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is Aβ 42(43). Neuron 1994, 13:45-53.
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 7
    • 0037010292 scopus 로고    scopus 로고
    • In vivo conversion of racemized β-amyloid ([D-Ser 26]Aβ 1-40) to truncated and toxic fragments ([D-Ser 26]A 25-35/40) and fragment presence in the brains of Alzheimer's patients
    • Kubo T., Nishimura S., Kumagae Y., Kaneko I. In vivo conversion of racemized β-amyloid ([D-Ser 26]Aβ 1-40) to truncated and toxic fragments ([D-Ser 26]A 25-35/40) and fragment presence in the brains of Alzheimer's patients. J Neurosci Res 2002, 70:474-483.
    • (2002) J Neurosci Res , vol.70 , pp. 474-483
    • Kubo, T.1    Nishimura, S.2    Kumagae, Y.3    Kaneko, I.4
  • 8
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides
    • Yankner B.A., Duffy L.K., Kirschner D.A. Neurotrophic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides. Science 1990, 250(4978):279-282.
    • (1990) Science , vol.250 , Issue.4978 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 11
    • 56749160419 scopus 로고    scopus 로고
    • Docosahexaenoic acid disrupts in vitro amyloid β fibrillation and concomitantly inhibits amyloid levels in cerebral cortex of Alzheimer's disease model rats
    • Hashimoto M., Shahdat H.M., Yamashita S., Katakura M., Tanabe Y., Fujiwara H., et al. Docosahexaenoic acid disrupts in vitro amyloid β fibrillation and concomitantly inhibits amyloid levels in cerebral cortex of Alzheimer's disease model rats. J Neurochem 2008, 107:1634-1646.
    • (2008) J Neurochem , vol.107 , pp. 1634-1646
    • Hashimoto, M.1    Shahdat, H.M.2    Yamashita, S.3    Katakura, M.4    Tanabe, Y.5    Fujiwara, H.6
  • 12
    • 25144516321 scopus 로고    scopus 로고
    • Implanted cannula-mediated repetitive administration of Aβ25-35 into the mouse cerebral ventricle effectively impairs spatial working memory
    • Yamada M., Chiba T., Sasabe J., Nawa M., Tajima H., Niikura T., et al. Implanted cannula-mediated repetitive administration of Aβ25-35 into the mouse cerebral ventricle effectively impairs spatial working memory. Behav Brain Res 2005, 164:139-146.
    • (2005) Behav Brain Res , vol.164 , pp. 139-146
    • Yamada, M.1    Chiba, T.2    Sasabe, J.3    Nawa, M.4    Tajima, H.5    Niikura, T.6
  • 13
    • 0027276784 scopus 로고
    • The role of essential fatty acids in neural development: implications for perinatal nutrition
    • Crawford M. The role of essential fatty acids in neural development: implications for perinatal nutrition. Am J Clin Nutr 1993, 57:703S-710S.
    • (1993) Am J Clin Nutr , vol.57
    • Crawford, M.1
  • 14
    • 0035183230 scopus 로고    scopus 로고
    • The essentiality of long chain n-3 fatty acids in relation to development and function of the brain and retina
    • Lauritzen L., Hansen H.S., Jorgensen M.H., Michaelsen K.F. The essentiality of long chain n-3 fatty acids in relation to development and function of the brain and retina. Prog Lipid Res 2001, 40:1-94.
    • (2001) Prog Lipid Res , vol.40 , pp. 1-94
    • Lauritzen, L.1    Hansen, H.S.2    Jorgensen, M.H.3    Michaelsen, K.F.4
  • 15
    • 34247108513 scopus 로고    scopus 로고
    • Dietary (n-3) fatty acids and brain development
    • Innis S.M. Dietary (n-3) fatty acids and brain development. J Nutr 2007, 137:855-859.
    • (2007) J Nutr , vol.137 , pp. 855-859
    • Innis, S.M.1
  • 16
    • 0025913434 scopus 로고
    • Fatty acid composition of brain phospholipids in aging and in Alzheimer's disease
    • Söderberg M., Edlund C., Kristensson K., Dallner G. Fatty acid composition of brain phospholipids in aging and in Alzheimer's disease. Lipids 1991, 26:421-425.
    • (1991) Lipids , vol.26 , pp. 421-425
    • Söderberg, M.1    Edlund, C.2    Kristensson, K.3    Dallner, G.4
  • 18
    • 0034913963 scopus 로고    scopus 로고
    • Polyunsaturated fatty acid synthesis and release by brain-derived cells in vitro
    • Moore S.A. Polyunsaturated fatty acid synthesis and release by brain-derived cells in vitro. J Mol Neurosci 2003, 16:195-200.
    • (2003) J Mol Neurosci , vol.16 , pp. 195-200
    • Moore, S.A.1
  • 19
    • 26444598506 scopus 로고    scopus 로고
    • A role for docosahexaenoic acid-derived neuroprotectin D1 in neural cell survival and Alzheimer disease
    • Lukiw W.L., Cui J.G., Marcheselli V.L., Bodker M., Botkjaer A., Gotlinger K., et al. A role for docosahexaenoic acid-derived neuroprotectin D1 in neural cell survival and Alzheimer disease. J Clin Invest 2005, 115:2774-2783.
    • (2005) J Clin Invest , vol.115 , pp. 2774-2783
    • Lukiw, W.L.1    Cui, J.G.2    Marcheselli, V.L.3    Bodker, M.4    Botkjaer, A.5    Gotlinger, K.6
  • 20
    • 0022548964 scopus 로고
    • Direct transesterification of all classes of lipids in a one- step reaction
    • Lepage G., Roy C.C. Direct transesterification of all classes of lipids in a one- step reaction. J Lipid Res 1986, 27:114-120.
    • (1986) J Lipid Res , vol.27 , pp. 114-120
    • Lepage, G.1    Roy, C.C.2
  • 21
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa H., Ohishi N., Yagi K. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Biochem 1979, 95:351-358.
    • (1979) Anal Biochem , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 22
    • 0033009199 scopus 로고    scopus 로고
    • Antioxidative effects of docosahexaenoic acid in the cerebrum versus cerebellum and brainstem of aged hypercholesterolemic rats
    • Hossain M.S., Hashimoto M., Gamoh S., Masumura S. Antioxidative effects of docosahexaenoic acid in the cerebrum versus cerebellum and brainstem of aged hypercholesterolemic rats. J Neurochem 1999, 72:1133-1138.
    • (1999) J Neurochem , vol.72 , pp. 1133-1138
    • Hossain, M.S.1    Hashimoto, M.2    Gamoh, S.3    Masumura, S.4
  • 24
    • 0027333557 scopus 로고
    • Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide
    • Haass C., Selkoe D. Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide. Cell 1993, 75:1039-1042.
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Haass, C.1    Selkoe, D.2
  • 25
    • 0027526419 scopus 로고
    • Release of excess amyloid β protein from a mutant amyloid β protein precursor
    • Cai X.D., Golde T.E., Younkin S.G. Release of excess amyloid β protein from a mutant amyloid β protein precursor. Science 1993, 259:514-516.
    • (1993) Science , vol.259 , pp. 514-516
    • Cai, X.D.1    Golde, T.E.2    Younkin, S.G.3
  • 26
    • 0028180518 scopus 로고
    • A model for β-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease
    • Hensley K., Carney J.M., Mattson M.P., Aksenova M., Harris M., Wu J.F., et al. A model for β-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease. Proc Natl Acad Sci USA 1994, 91:3270-3274.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3270-3274
    • Hensley, K.1    Carney, J.M.2    Mattson, M.P.3    Aksenova, M.4    Harris, M.5    Wu, J.F.6
  • 27
    • 0029145084 scopus 로고
    • Are reactive oxygen species involved in Alzheimer's disease?
    • Benzi G., Moretti A. Are reactive oxygen species involved in Alzheimer's disease?. Neurobiol Aging 1995, 16:661-674.
    • (1995) Neurobiol Aging , vol.16 , pp. 661-674
    • Benzi, G.1    Moretti, A.2
  • 28
    • 0029245289 scopus 로고
    • A potential role for apoptosis in neurodegeneration and Alzheimer's disease
    • Cotman C., Anderson A. A potential role for apoptosis in neurodegeneration and Alzheimer's disease. Mol Neurobiol 1995, 10:19-45.
    • (1995) Mol Neurobiol , vol.10 , pp. 19-45
    • Cotman, C.1    Anderson, A.2
  • 29
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid b protein toxicity
    • Behl C., Davis J., Lesley R., Schubert D. Hydrogen peroxide mediates amyloid b protein toxicity. Cell 1994, 77:817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.2    Lesley, R.3    Schubert, D.4
  • 30
    • 0029040824 scopus 로고
    • The intracellular component of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by beta-amyloid peptides
    • Shearman M.S., Hawtin S.R., Tailor V.J. The intracellular component of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by beta-amyloid peptides. J Neurochem 1995, 65:218-227.
    • (1995) J Neurochem , vol.65 , pp. 218-227
    • Shearman, M.S.1    Hawtin, S.R.2    Tailor, V.J.3
  • 31
    • 0035979843 scopus 로고    scopus 로고
    • Phospholipid fatty acids and neurotoxicity in human neuroblastoma SH-SY5Y cells
    • Reynolds L.M., Dalton C.F., Reynolds G.P. Phospholipid fatty acids and neurotoxicity in human neuroblastoma SH-SY5Y cells. Neurosci Letts 2001, 309:193-196.
    • (2001) Neurosci Letts , vol.309 , pp. 193-196
    • Reynolds, L.M.1    Dalton, C.F.2    Reynolds, G.P.3
  • 33
    • 0027300736 scopus 로고
    • Lipid peroxidation: its mechanisms, measurement, and significance
    • Halliwell B., Chirico S. Lipid peroxidation: its mechanisms, measurement, and significance. Am J Clin Nutr 1993, 57(Suppl):715S-725S.
    • (1993) Am J Clin Nutr , vol.57 , Issue.SUPPL
    • Halliwell, B.1    Chirico, S.2
  • 34
    • 0034536758 scopus 로고    scopus 로고
    • Polyunsaturated (n-3) fatty acids susceptible to peroxidation are increased in plasma and tissue lipids of rats fed docosahexaenoic acid-containing oils
    • Song J.H., Fujimoto K., Miyazawa T. Polyunsaturated (n-3) fatty acids susceptible to peroxidation are increased in plasma and tissue lipids of rats fed docosahexaenoic acid-containing oils. J Nutr 2000, 130:3028-3033.
    • (2000) J Nutr , vol.130 , pp. 3028-3033
    • Song, J.H.1    Fujimoto, K.2    Miyazawa, T.3
  • 35
    • 0032923143 scopus 로고    scopus 로고
    • Protective effect of docosahexaenoic acid against hydrogen peroxide-induced oxidative stress in human lymphocytes
    • Bechoua S., Dubois M., Dominguez Z., Goncalves A., Némoz G., Lagarde M., et al. Protective effect of docosahexaenoic acid against hydrogen peroxide-induced oxidative stress in human lymphocytes. Biochem Pharmacol 1999, 57:1021-1030.
    • (1999) Biochem Pharmacol , vol.57 , pp. 1021-1030
    • Bechoua, S.1    Dubois, M.2    Dominguez, Z.3    Goncalves, A.4    Némoz, G.5    Lagarde, M.6
  • 36
    • 33646396777 scopus 로고    scopus 로고
    • Neuroblastoma cell death in response to docosahexaenoic acid: sensitization to chemotherapy and arsenic-induced oxidative stress
    • Lindskog M., Gleissman H., Ponthan F., Castro J., Kogner P., Johnsen J.I. Neuroblastoma cell death in response to docosahexaenoic acid: sensitization to chemotherapy and arsenic-induced oxidative stress. Int J Cancer 2006, 118:2584-2593.
    • (2006) Int J Cancer , vol.118 , pp. 2584-2593
    • Lindskog, M.1    Gleissman, H.2    Ponthan, F.3    Castro, J.4    Kogner, P.5    Johnsen, J.I.6
  • 37
    • 0034924664 scopus 로고    scopus 로고
    • Inhibition of neuronal apoptosis by polyunsaturated fatty acids
    • Kim H.Y., Akbar M., Kim K.Y. Inhibition of neuronal apoptosis by polyunsaturated fatty acids. J Mol Neurosci 2001, 16:223-227.
    • (2001) J Mol Neurosci , vol.16 , pp. 223-227
    • Kim, H.Y.1    Akbar, M.2    Kim, K.Y.3
  • 38
    • 0036014858 scopus 로고    scopus 로고
    • Docosahexaenoic acid abundance in the brain: a biodevice to combat oxidative stress
    • Yavin E., Brand A., Green P. Docosahexaenoic acid abundance in the brain: a biodevice to combat oxidative stress. Nutr Neurosci 2002, 5:149-157.
    • (2002) Nutr Neurosci , vol.5 , pp. 149-157
    • Yavin, E.1    Brand, A.2    Green, P.3
  • 39
    • 33646138943 scopus 로고    scopus 로고
    • Docosahexaenoic acid promotes neurogenesis in vitro and in vivo
    • Kawakita E., Hashimoto M., Shido O. Docosahexaenoic acid promotes neurogenesis in vitro and in vivo. Neuroscience 2006, 139:991-997.
    • (2006) Neuroscience , vol.139 , pp. 991-997
    • Kawakita, E.1    Hashimoto, M.2    Shido, O.3
  • 40
    • 64449086153 scopus 로고    scopus 로고
    • Docosahexaenoic acid promotes neuronal differentiation by regulating basic helix-loop-helix transcription factors and cell cycle in neural stem cells
    • Katakura M., Hashimoto M., Shahdat H.M., Gamoh S., et al. Docosahexaenoic acid promotes neuronal differentiation by regulating basic helix-loop-helix transcription factors and cell cycle in neural stem cells. Neuroscience 2009, 160:651-660.
    • (2009) Neuroscience , vol.160 , pp. 651-660
    • Katakura, M.1    Hashimoto, M.2    Shahdat, H.M.3    Gamoh, S.4
  • 41
    • 0034634590 scopus 로고    scopus 로고
    • Inhibition of neuronal apoptosis by docosahexaenoic acid (22:6n-3)
    • Kim H.-Y., Akbar M., Lau A., Edsall L. Inhibition of neuronal apoptosis by docosahexaenoic acid (22:6n-3). J Biol Chem 2000, 275:35215-35223.
    • (2000) J Biol Chem , vol.275 , pp. 35215-35223
    • Kim, H.-Y.1    Akbar, M.2    Lau, A.3    Edsall, L.4
  • 42
    • 0028001754 scopus 로고
    • Polyunsaturated fatty acids increase lipid radical formation induced by oxidant stress in endothelial cells
    • Alexander-North L.S., North J.A., Kiminyo K.P., Buettner G.R., Spector A.A. Polyunsaturated fatty acids increase lipid radical formation induced by oxidant stress in endothelial cells. J Lipid Res 1994, 35:1773-1785.
    • (1994) J Lipid Res , vol.35 , pp. 1773-1785
    • Alexander-North, L.S.1    North, J.A.2    Kiminyo, K.P.3    Buettner, G.R.4    Spector, A.A.5
  • 43
    • 0035479963 scopus 로고    scopus 로고
    • Mechanism of apoptosis in HL-60 cells induced by n-3 and n-6 polyunsaturated fatty acids
    • Arita K., Kobuchi H., Utsumi T., Takehara Y., Akiyama J., Horton A.A., et al. Mechanism of apoptosis in HL-60 cells induced by n-3 and n-6 polyunsaturated fatty acids. Biochem Pharmacol 2001, 62:821-828.
    • (2001) Biochem Pharmacol , vol.62 , pp. 821-828
    • Arita, K.1    Kobuchi, H.2    Utsumi, T.3    Takehara, Y.4    Akiyama, J.5    Horton, A.A.6
  • 44
    • 0037407743 scopus 로고    scopus 로고
    • Protective effect of docosahexaenoic acid on oxidative stress-induced apoptosis of retina photoreceptors
    • Rotstein N.P., Politi L.F., German O.L., Girotti R. Protective effect of docosahexaenoic acid on oxidative stress-induced apoptosis of retina photoreceptors. Invest Ophthalmol Vis Sci 2003, 44:2252-2259.
    • (2003) Invest Ophthalmol Vis Sci , vol.44 , pp. 2252-2259
    • Rotstein, N.P.1    Politi, L.F.2    German, O.L.3    Girotti, R.4
  • 45
    • 0036905921 scopus 로고    scopus 로고
    • Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review
    • Butterfield D.A. Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review. Free Radic Res 2002, 36:1307-1313.
    • (2002) Free Radic Res , vol.36 , pp. 1307-1313
    • Butterfield, D.A.1
  • 46
    • 0033133579 scopus 로고    scopus 로고
    • In vitro and in vivo oxidative stress associated with Alzheimer's amyloid beta-peptide (1-42)
    • [discussion 339-342]
    • Yatin S.M., Varadarajan S., Link C.D., Butterfield D.A. In vitro and in vivo oxidative stress associated with Alzheimer's amyloid beta-peptide (1-42). Neurobiol Aging 1999, 20:325-330. [discussion 339-342].
    • (1999) Neurobiol Aging , vol.20 , pp. 325-330
    • Yatin, S.M.1    Varadarajan, S.2    Link, C.D.3    Butterfield, D.A.4
  • 47
    • 33644875009 scopus 로고    scopus 로고
    • Docosahexaenoic acid prevents neuronal apoptosis induced by soluble amyloid- b oligomers
    • Florent S., Malaplate-Armand C., Youssef I., Kriem B., Koziel V., Escanye M.C., et al. Docosahexaenoic acid prevents neuronal apoptosis induced by soluble amyloid- b oligomers. J Neurochem 2006, 96:385-395.
    • (2006) J Neurochem , vol.96 , pp. 385-395
    • Florent, S.1    Malaplate-Armand, C.2    Youssef, I.3    Kriem, B.4    Koziel, V.5    Escanye, M.C.6
  • 48
    • 9444284334 scopus 로고    scopus 로고
    • Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease beta-amyloid
    • Barnham K.J., Haeffner F., Ciccotosto G.D., Curtain C.C., Tew D., Mavros C., et al. Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease beta-amyloid. FASEB J 2004, 18:1427-1429.
    • (2004) FASEB J , vol.18 , pp. 1427-1429
    • Barnham, K.J.1    Haeffner, F.2    Ciccotosto, G.D.3    Curtain, C.C.4    Tew, D.5    Mavros, C.6


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