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Volumn 5, Issue 1, 2015, Pages 178-193

α-synuclein-induced synapse damage in cultured neurons is mediated by cholesterol-sensitive activation of cytoplasmic phospholipase A2

Author keywords

Alpha synuclein; Cholesterol; Parkinson s disease; Phospholipase A2; Platelet activating factor; Synapse; Synaptophysin

Indexed keywords

ACETYLSALICYLIC ACID; ALPHA SYNUCLEIN; ARACHIDONYL TRIFLUOROMETHYL KETONE; CAFFEIC ACID; CHOLESTEROL; CYSTEINE STRING PROTEIN; CYTOSOLIC PHOSPHOLIPASE A2; GINKGOLIDE B; IBUPROFEN; METHYL ARACHIDONYL FLUOROPHOSPHONATE; NORDIHYDROGUAIARETIC ACID; PHOSPHOLIPASE A2 INHIBITOR; PROSTAGLANDIN E2; PROSTAGLANDIN SYNTHASE INHIBITOR; SYNAPTOPHYSIN; THROMBOCYTE ACTIVATING FACTOR; THROMBOCYTE ACTIVATING FACTOR ANTAGONIST; UNCLASSIFIED DRUG; NEUROPROTECTIVE AGENT; PROTEIN AGGREGATE; RECOMBINANT PROTEIN; SNCA PROTEIN, HUMAN;

EID: 84989323110     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom5010178     Document Type: Article
Times cited : (25)

References (53)
  • 1
    • 41049106214 scopus 로고    scopus 로고
    • Non-motor symptoms in Parkinson’s disease
    • Poewe, W. Non-motor symptoms in Parkinson’s disease. Eur. J. Neurol. 2008, 15, 14–20.
    • (2008) Eur. J. Neurol , vol.15 , pp. 14-20
    • Poewe, W.1
  • 2
    • 0037335814 scopus 로고    scopus 로고
    • Prevalence and characteristics of dementia in Parkinson disease: An 8-year prospective study
    • Aarsland, D.; Andersen, K.; Larsen, J. P.; Lolk, A.; Kragh-Sorensen, P. Prevalence and characteristics of dementia in Parkinson disease: An 8-year prospective study. Arch. Neurol. 2003, 60, 387–392.
    • (2003) Arch. Neurol , vol.60 , pp. 387-392
    • Aarsland, D.1    Andersen, K.2    Larsen, J.P.3    Lolk, A.4    Kragh-Sorensen, P.5
  • 4
    • 27544470486 scopus 로고    scopus 로고
    • Snaring the function of alpha-synuclein
    • Bonini, N. M.; Giasson, B. I. Snaring the function of alpha-synuclein. Cell 2005, 123, 359–361.
    • (2005) Cell , vol.123 , pp. 359-361
    • Bonini, N.M.1    Giasson, B.I.2
  • 5
    • 0037109727 scopus 로고    scopus 로고
    • Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein
    • Cabin, D. E.; Shimazu, K.; Murphy, D.; Cole, N.B.; Gottschalk, W.; McIlwain, K. L.; Orrison, B.; Chen, A.; Ellis, C. E.; Paylor, R.; et al. Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein. J. Neurosci. 2002, 22, 8797–8807.
    • (2002) J. Neurosci , vol.22 , pp. 8797-8807
    • Cabin, D.E.1    Shimazu, K.2    Murphy, D.3    Cole, N.B.4    Gottschalk, W.5    McIlwain, K.L.6    Orrison, B.7    Chen, A.8    Ellis, C.E.9    Paylor, R.10
  • 6
    • 0032102455 scopus 로고    scopus 로고
    • The synucleins: A family of proteins involved in synaptic function, plasticity, neurodegeneration and disease
    • Clayton, D. F.; George, J. M. The synucleins: A family of proteins involved in synaptic function, plasticity, neurodegeneration and disease. Trends Neurosci. 1998, 21, 249–254.
    • (1998) Trends Neurosci , vol.21 , pp. 249-254
    • Clayton, D.F.1    George, J.M.2
  • 7
    • 61449084604 scopus 로고    scopus 로고
    • Central role of alpha-synuclein oligomers in neurodegeneration in Parkinson disease
    • Kazantsev, A. G.; Kolchinsky, A. M. Central role of alpha-synuclein oligomers in neurodegeneration in Parkinson disease. Arch. Neurol. 2008, 65, 1577–1581.
    • (2008) Arch. Neurol , vol.65 , pp. 1577-1581
    • Kazantsev, A.G.1    Kolchinsky, A.M.2
  • 8
    • 33846997878 scopus 로고    scopus 로고
    • Presynaptica-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies
    • Kramer, M. L.; Schulz-Schaeffer, W. J. Presynaptic a-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies. J. Neurosci. 2007, 27, 1405–1410.
    • (2007) J. Neurosci , vol.27 , pp. 1405-1410
    • Kramer, M.L.1    Schulz-Schaeffer, W.J.2
  • 9
    • 33749240943 scopus 로고    scopus 로고
    • Mechanisms of Parkinson’s disease linked to pathological  a-synuclein
    • Lee, V.M.Y.; Trojanowski, J.Q. Mechanisms of Parkinson’s disease linked to pathological  a-synuclein: New targets for drug discovery. Neuron 2006, 52, 33–38.
    • (2006) New Targets for Drug Discovery. Neuron , vol.52 , pp. 33-38
    • Lee, V.1    Trojanowski, J.Q.2
  • 11
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin, P.; Melki, R.; Kopito, R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat. Rev. Mol. Cell Biol. 2010, 11, 301–307.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 13
    • 0033539664 scopus 로고    scopus 로고
    • Axon pathology in Parkinson’s disease and Lewy body dementia hippocampus contains alpha-, beta-, and gamma-synuclein
    • USA
    • Galvin, J.E.; Uryu, K.; Lee, V.M.; Trojanowski, J.Q. Axon pathology in Parkinson’s disease and Lewy body dementia hippocampus contains alpha-, beta-, and gamma-synuclein. Proc. Natl. Acad. Sci. USA 1999, 96, 13450–13455.
    • (1999) Proc. Natl. Acad. Sci , vol.96 , pp. 13450-13455
    • Galvin, J.E.1    Uryu, K.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 14
    • 63849332293 scopus 로고    scopus 로고
    • Dynamic changes in presynaptic and axonal transport proteins combined with striatal neuroinflammation precede dopaminergic neuronal loss in a rat model of AAV alpha-synucleinopathy
    • Chung, C. Y.; Koprich, J. B.; Siddiqi, H.; Isacson, O. Dynamic changes in presynaptic and axonal transport proteins combined with striatal neuroinflammation precede dopaminergic neuronal loss in a rat model of AAV alpha-synucleinopathy. J. Neurosci. 2009, 29, 3365–3373.
    • (2009) J. Neurosci , vol.29 , pp. 3365-3373
    • Chung, C.Y.1    Koprich, J.B.2    Siddiqi, H.3    Isacson, O.4
  • 15
    • 78649740289 scopus 로고    scopus 로고
    • A-synuclein induced synapse damage is enhanced by amyloid-b1–42
    • Bate, C.; Gentleman, S.; Williams, A. a-synuclein induced synapse damage is enhanced by amyloid-b1–42. Mol. Neurodegener. 2010, 5, doi:10.1186/1750-1326-5-55.
    • (2010) Mol. Neurodegener , vol.5
    • Bate, C.1    Gentleman, S.2    Williams, A.3
  • 16
    • 77950638702 scopus 로고    scopus 로고
    • Phospholipase A2 inhibitors protect against prion and Ab mediated synapse degeneration
    • Bate, C.; Tayebi, M.; Williams, A. Phospholipase A2 inhibitors protect against prion and Ab mediated synapse degeneration. Mol. Neurodegener. 2010, doi:10.1186/1750-1326-5-13.
    • (2010) Mol. Neurodegener
    • Bate, C.1    Tayebi, M.2    Williams, A.3
  • 17
    • 0030872413 scopus 로고    scopus 로고
    • Loss of the presynapticvesicle protein synaptophysin in hippocampus correlates with cognitive decline in Alzheimer disease
    • Sze, C. I.; Troncoso, J. C.; Kawas, C.; Mouton, P.; Price, D. L.; Martin, L. J. Loss of the presynapticvesicle protein synaptophysin in hippocampus correlates with cognitive decline in Alzheimer disease. J. Neuropath Exp. Neurol. 1997, 56, 933–944.
    • (1997) J. Neuropath Exp. Neurol , vol.56 , pp. 933-944
    • Sze, C.I.1    Troncoso, J.C.2    Kawas, C.3    Mouton, P.4    Price, D.L.5    Martin, L.J.6
  • 18
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer’s disease: Synapse loss is the major correlate of cognitive impairment
    • Terry, R. D.; Masliah, E.; Salmon, D. P.; Butters, N.; deTeresa, R.; Hill, R.; Hansen, L.A.; Katzman, R. Physical basis of cognitive alterations in Alzheimer’s disease: Synapse loss is the major correlate of cognitive impairment. Ann. Neurol. 1991, 30, 572–580.
    • (1991) Ann. Neurol , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    Deteresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 19
    • 80055071341 scopus 로고    scopus 로고
    • Amyloid-b-induced synapse damage is mediated via cross-linkage of the cellular prion protein
    • Bate, C.; Williams, A. Amyloid-b-induced synapse damage is mediated via cross-linkage of the cellular prion protein. J. Biol. Chem. 2011, 286, 37955–37963.
    • (2011) J. Biol. Chem , vol.286 , pp. 37955-37963
    • Bate, C.1    Williams, A.2
  • 20
    • 0030249717 scopus 로고    scopus 로고
    • Relative contribution of the de novo and remodelling pathways to the synthesis of platelet-activating factor in brain areas and during ischemia
    • Francescangeli, E.; Domanska-Janik, K.; Goracci, G. Relative contribution of the de novo and remodelling pathways to the synthesis of platelet-activating factor in brain areas and during ischemia. J. Lipid Mediat. Cell Signal. 1996, 14, 89–98.
    • (1996) J. Lipid Mediat. Cell Signal , vol.14 , pp. 89-98
    • Francescangeli, E.1    Domanska-Janik, K.2    Goracci, G.3
  • 21
    • 40149094037 scopus 로고    scopus 로고
    • Ginkgolides protect against amyloid-b1–42-mediated synapse damage in vitro
    • Bate, C.; Tayebi, M.; Williams, A. Ginkgolides protect against amyloid-b1–42-mediated synapse damage in vitro. Mol. Neurodegener. 2008, doi:10.1186/1750-1326-3-1.
    • (2008) Mol. Neurodegener
    • Bate, C.1    Tayebi, M.2    Williams, A.3
  • 22
    • 0030899268 scopus 로고    scopus 로고
    • Characterization of the prostanoid receptors mediating inhibition of PAF-induced aggregation of guinea-pig eosinophils
    • Teixeira, M. M.; al Rashed, S.; Rossi, A. G.; Hellewell, P. G. Characterization of the prostanoid receptors mediating inhibition of PAF-induced aggregation of guinea-pig eosinophils. Br. J. Pharmacol. 1997, 121, 77–82.
    • (1997) Br. J. Pharmacol , vol.121 , pp. 77-82
    • Teixeira, M.M.1    Al Rashed, S.2    Rossi, A.G.3    Hellewell, P.G.4
  • 23
    • 34249729416 scopus 로고    scopus 로고
    • Prostaglandin E receptors
    • Sugimoto, Y.; Narumiya, S. Prostaglandin E receptors. J. Biol. Chem. 2007, 282, 11613–11617.
    • (2007) J. Biol. Chem , vol.282 , pp. 11613-11617
    • Sugimoto, Y.1    Narumiya, S.2
  • 24
    • 0028339812 scopus 로고
    • Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca2+-dependent lipid-binding domain and a Ca2+-independent catalytic domain
    • Nalefski, E. A.; Sultzman, L. A.; Martin, D. M.; Kriz, R. W.; Towler, P. S.; Knopf, J.L.; Clark, J. D. Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca2+-dependent lipid-binding domain and a Ca2+-independent catalytic domain. J. Biol. Chem. 1994, 269, 18239–18249.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18239-18249
    • Nalefski, E.A.1    Sultzman, L.A.2    Martin, D.M.3    Kriz, R.W.4    Towler, P.S.5    Knopf, J.L.6    Clark, J.D.7
  • 25
    • 0029100434 scopus 로고
    • Selective inhibition of cholesterol biosynthesis in brain cells by squalestatin 1
    • Crick, D. C.; Suders, J.; Kluthe, C. M.; Andres, D. A.; Waechter, C. J. Selective inhibition of cholesterol biosynthesis in brain cells by squalestatin 1. J. Neurochem. 1995, 65, 1365–1373.
    • (1995) J. Neurochem , vol.65 , pp. 1365-1373
    • Crick, D.C.1    Suders, J.2    Kluthe, C.M.3    Andres, D.A.4    Waechter, C.J.5
  • 26
    • 34547550818 scopus 로고    scopus 로고
    • Squalestatin protects neurons and reduces the activation of cytoplasmic phospholipase A2 by Ab1–42
    • Bate, C.; Williams, A. Squalestatin protects neurons and reduces the activation of cytoplasmic phospholipase A2 by Ab1–42. Neuropharmacology 2007, 53, 222–231.
    • (2007) Neuropharmacology , vol.53 , pp. 222-231
    • Bate, C.1    Williams, A.2
  • 27
    • 33646594976 scopus 로고    scopus 로고
    • Phospholipase A2-generated lipid mediators in the brain: The good, the bad, and the ugly
    • Farooqui, A. A.; Horrocks, L. A. Phospholipase A2-generated lipid mediators in the brain: The good, the bad, and the ugly. Neuroscientist 2006, 12, 245–260.
    • (2006) Neuroscientist , vol.12 , pp. 245-260
    • Farooqui, A.A.1    Horrocks, L.A.2
  • 28
    • 33748804968 scopus 로고    scopus 로고
    • Inhibitors of brain phospholipase A2 activity: Their neuropharmacological effects and therapeutic importance for the treatment of neurologic disorders
    • Farooqui, A. A.; Ong, W. Y.; Horrocks, L. A. Inhibitors of brain phospholipase A2 activity: Their neuropharmacological effects and therapeutic importance for the treatment of neurologic disorders. Phamacol. Rev. 2006, 58, 591–620.
    • (2006) Phamacol. Rev , vol.58 , pp. 591-620
    • Farooqui, A.A.1    Ong, W.Y.2    Horrocks, L.A.3
  • 31
    • 0031741666 scopus 로고    scopus 로고
    • P.; Beal, M. F.; Ferrante, R. J.; Andreassen, O. A.; Wermer, M.; Chin, M.R.; Bonventre, J.V. Mice deficient in group IV cytosolic phospholipase A2 are resistant to MPTP neurotoxicity
    • Klivenyi
    • Klivenyi, P.; Beal, M. F.; Ferrante, R. J.; Andreassen, O. A.; Wermer, M.; Chin, M.R.; Bonventre, J.V. Mice deficient in group IV cytosolic phospholipase A2 are resistant to MPTP neurotoxicity. J. Neurochem. 1998, 71, 2634–2637.
    • (1998) J. Neurochem , vol.71 , pp. 2634-2637
  • 33
    • 1242297090 scopus 로고    scopus 로고
    • Phospholipase A2 in the central nervous system: Implications for neurodegenerative diseases
    • Sun, G. Y.; Xu, J.; Jensen, M. D.; Simonyi, A. Phospholipase A2 in the central nervous system: Implications for neurodegenerative diseases. J. Lipid Res. 2004, 45, 205–213.
    • (2004) J. Lipid Res , vol.45 , pp. 205-213
    • Sun, G.Y.1    Xu, J.2    Jensen, M.D.3    Simonyi, A.4
  • 34
    • 27644590902 scopus 로고    scopus 로고
    • Synaptic activity becomes excitotoxic in neurons exposed to elevated levels of platelet-activating factor
    • Bellizzi, M. J.; Lu, S. M.; Masliah, E.; Gelbard, H. A. Synaptic activity becomes excitotoxic in neurons exposed to elevated levels of platelet-activating factor. J. Clin. Investig. 2005, 115, 3185–3192.
    • (2005) J. Clin. Investig , vol.115 , pp. 3185-3192
    • Bellizzi, M.J.1    Lu, S.M.2    Masliah, E.3    Gelbard, H.A.4
  • 35
    • 54049119697 scopus 로고    scopus 로고
    • EGb761 protects against nigrostriatal dopaminergic neurotoxicity in 1-methyl-4- phenyl-1,2,3,6-tetrahydropyridine-induced Parkinsonism in mice: Role of oxidative stress
    • Rojas, P.; Serrano-García, N.; Mares-Sámano, J.J.; Medina-Campos, O.N.; Pedraza-Chaverri, J.; Ögren, S.O. EGb761 protects against nigrostriatal dopaminergic neurotoxicity in 1-methyl-4- phenyl-1,2,3,6-tetrahydropyridine-induced Parkinsonism in mice: Role of oxidative stress. Eur. J. Neurosci. 2008, 28, 41–50.
    • (2008) Eur. J. Neurosci , vol.28 , pp. 41-50
    • Rojas, P.1    Serrano-García, N.2    Mares-Sámano, J.J.3    Medina-Campos, O.N.4    Pedraza-Chaverri, J.5    ÖGren, S.O.6
  • 37
    • 12544250740 scopus 로고    scopus 로고
    • Endogenous PGE2 regulates membrane excitability and synaptic transmission in hippocampal CA1 pyramidal neurons
    • Chen, C.; Bazan, N.G. Endogenous PGE2 regulates membrane excitability and synaptic transmission in hippocampal CA1 pyramidal neurons. J. Neurphysiol. 2005, 93, 929–941.
    • (2005) J. Neurphysiol , vol.93 , pp. 929-941
    • Chen, C.1    Bazan, N.G.2
  • 38
    • 28444479505 scopus 로고    scopus 로고
    • Role of cholesterol and lipid organization in disease
    • Maxfield, F. R.; Tabas, I. Role of cholesterol and lipid organization in disease. Nature 2005, 438, 612–621.
    • (2005) Nature , vol.438 , pp. 612-621
    • Maxfield, F.R.1    Tabas, I.2
  • 41
    • 73949132010 scopus 로고    scopus 로고
    • Lovastatin amelioratesa-synuclein accumulation and oxidation in transgenic mouse models of a-synucleinopathies
    • Koob, A. O.; Ubhi, K.; Paulsson, J. F.; Kelly, J.; Rockenstein, E.; Mante, M.; Adame, A.; Masliah, E. Lovastatin amelioratesa-synuclein accumulation and oxidation in transgenic mouse models of a-synucleinopathies. Exp. Neurol. 2010, 221, 267–274.
    • (2010) Exp. Neurol , vol.221 , pp. 267-274
    • Koob, A.O.1    Ubhi, K.2    Paulsson, J.F.3    Kelly, J.4    Rockenstein, E.5    Mante, M.6    Adame, A.7    Masliah, E.8
  • 43
    • 0033772113 scopus 로고    scopus 로고
    • Decreased prevalence of alzheimer disease associated with 3-hydroxy-3-methyglutaryl coenzyme A reductase inhibitors
    • Wolozin, B.; Kellman, W.; Ruosseau, P.; Celesia, G.G.; Siegel, G. Decreased prevalence of alzheimer disease associated with 3-hydroxy-3-methyglutaryl coenzyme A reductase inhibitors. Arch. Neurol. 2000, 57, 1439–1443.
    • (2000) Arch. Neurol , vol.57 , pp. 1439-1443
    • Wolozin, B.1    Kellman, W.2    Ruosseau, P.3    Celesia, G.G.4    Siegel, G.5
  • 44
    • 53349162141 scopus 로고    scopus 로고
    • A nested case control study
    • Samii, A.; Carleton, B. C.; Etminan, M. Statin use and the risk of Parkinson disease: A nested case control study. J. Clin. Neurosci. 2008, 15, 1272–1273.
    • (2008) J. Clin. Neurosci , vol.15 , pp. 1272-1273
    • Samii, A.1    Carleton, B.C.2    Etminan, M.S.3
  • 45
    • 67649307141 scopus 로고    scopus 로고
    • Statins and the risk of Parkinson disease: An update on the controversy
    • Becker, C.; Meier, C.R. Statins and the risk of Parkinson disease: An update on the controversy. Expert Opin. Drug Saf. 2009, 8, 261–271.
    • (2009) Expert Opin. Drug Saf , vol.8 , pp. 261-271
    • Becker, C.1    Meier, C.R.2
  • 47
    • 1642354334 scopus 로고    scopus 로고
    • Lipid rafts: Heterogeneity on the high seas
    • Pike, L. J. Lipid rafts: Heterogeneity on the high seas. Biochem. J. 2004, 378, 281–292.
    • (2004) Biochem. J , vol.378 , pp. 281-292
    • Pike, L.J.1
  • 48
  • 49
    • 5444275741 scopus 로고    scopus 로고
    • Cholesterol- and caveolin-rich membrane domains are essential for phospholipase A2-dependent EDHF formation
    • Graziani, A.; Bricko, V.; Carmignani, M.; Graier, W.F.; Groschner, K. Cholesterol- and caveolin-rich membrane domains are essential for phospholipase A2-dependent EDHF formation. Cardiovasc. Res. 2004, 64, 234–242.
    • (2004) Cardiovasc. Res , vol.64 , pp. 234-242
    • Graziani, A.1    Bricko, V.2    Carmignani, M.3    Graier, W.F.4    Groschner, K.5
  • 50
    • 41549105318 scopus 로고    scopus 로고
    • Sequestration of free cholesterol in cell membranes by prions correlates with cytoplasmic phospholipase A2 activation
    • Bate, C.; Tayebi, M.; Williams, A. Sequestration of free cholesterol in cell membranes by prions correlates with cytoplasmic phospholipase A2 activation. BMC Biol. 2008, doi:10.1186/1741-7007-6-8.
    • (2008) BMC Biol
    • Bate, C.1    Tayebi, M.2    Williams, A.3
  • 52
    • 0034707082 scopus 로고    scopus 로고
    • Insolubility of lipids in Triton X-100: Physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts)
    • London, E.; Brown, D. A. Insolubility of lipids in Triton X-100: Physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts). Biochim. Biophys. Acta 2000, 1508, 182–195.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 182-195
    • London, E.1    Brown, D.A.2
  • 53
    • 79953164948 scopus 로고    scopus 로고
    • Monoacylated cellular prion protein modifies cell membranes, inhibits cell signaling and reduces prion formation
    • Bate, C.; Williams, A. Monoacylated cellular prion protein modifies cell membranes, inhibits cell signaling and reduces prion formation. J. Biol. Chem. 2011, 286, 8752–8758.
    • (2011) J. Biol. Chem , vol.286 , pp. 8752-8758
    • Bate, C.1    Williams, A.2


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