메뉴 건너뛰기




Volumn 34, Issue 4, 2013, Pages 1032-1044

Effects of different amyloid β-protein analogues on synaptic function

Author keywords

Alzheimer's disease; Amyloid protein; Dentritic spines; Long term potentiation; MEPCS; Methionine 35; PSD 95; Synaptic transmission; Synaptophysin

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; METHIONINE; METHIONINE 35; METHIONINE SULFOXIDE; POSTSYNAPTIC DENSITY PROTEIN 95; SYNAPTOPHYSIN; UNCLASSIFIED DRUG;

EID: 84872281213     PISSN: 01974580     EISSN: 15581497     Source Type: Journal    
DOI: 10.1016/j.neurobiolaging.2012.06.027     Document Type: Article
Times cited : (56)

References (68)
  • 1
    • 70549106846 scopus 로고    scopus 로고
    • Amyloid-beta as a positive endogenous regulator of release probability at hippocampal synapses
    • Abramov E., Dolev I., Fogel H., Ciccotosto G.D., Ruff E., Slutsky I. Amyloid-beta as a positive endogenous regulator of release probability at hippocampal synapses. Nat. Neurosci. 2009, 12:1567-1576.
    • (2009) Nat. Neurosci. , vol.12 , pp. 1567-1576
    • Abramov, E.1    Dolev, I.2    Fogel, H.3    Ciccotosto, G.D.4    Ruff, E.5    Slutsky, I.6
  • 3
    • 0025788797 scopus 로고
    • Excitatory and inhibitory autaptic currents in isolated hippocampal neurons maintained in cell culture
    • Bekkers J.M., Stevens C.F. Excitatory and inhibitory autaptic currents in isolated hippocampal neurons maintained in cell culture. Proc. Natl. Acad. Sci. U. S. A. 1991, 88:7834-7838.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 7834-7838
    • Bekkers, J.M.1    Stevens, C.F.2
  • 9
    • 12844266117 scopus 로고    scopus 로고
    • The critical role of methionine 35 in Alzheimer's amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity
    • Butterfield D.A., Boyd-Kimball D. The critical role of methionine 35 in Alzheimer's amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity. Biochim. Biophys. Acta. 2005, 1703:149-156.
    • (2005) Biochim. Biophys. Acta. , vol.1703 , pp. 149-156
    • Butterfield, D.A.1    Boyd-Kimball, D.2
  • 11
    • 84861470082 scopus 로고    scopus 로고
    • Methionine-35 of Aβ(1-42): importance for oxidative stress in Alzheimer disease
    • Butterfield D.A., Sultana R. Methionine-35 of Aβ(1-42): importance for oxidative stress in Alzheimer disease. J. Amino Acids 2011, 2011:198430.
    • (2011) J. Amino Acids , vol.2011 , pp. 198430
    • Butterfield, D.A.1    Sultana, R.2
  • 12
  • 16
  • 17
    • 77957806490 scopus 로고    scopus 로고
    • Exposure to extremely low-frequency (50 Hz) electromagnetic fields enhances adult hippocampal neurogenesis in C57BL/6 mice
    • Cuccurazzu B., Leone L., Podda M.V., Piacentini R., Riccardi E., Ripoli C., Azzena G.B., Grassi C. Exposure to extremely low-frequency (50 Hz) electromagnetic fields enhances adult hippocampal neurogenesis in C57BL/6 mice. Exp. Neurol. 2010, 226:173-182.
    • (2010) Exp. Neurol. , vol.226 , pp. 173-182
    • Cuccurazzu, B.1    Leone, L.2    Podda, M.V.3    Piacentini, R.4    Riccardi, E.5    Ripoli, C.6    Azzena, G.B.7    Grassi, C.8
  • 19
    • 79955051063 scopus 로고    scopus 로고
    • Linking lipids to Alzheimer's disease: cholesterol and beyond
    • Di Paolo G., Kim T.W. Linking lipids to Alzheimer's disease: cholesterol and beyond. Nat. Rev. Neurosci. 2011, 12:284-296.
    • (2011) Nat. Rev. Neurosci. , vol.12 , pp. 284-296
    • Di Paolo, G.1    Kim, T.W.2
  • 20
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence
    • Dong J., Atwood C.S., Anderson V.E., Siedlak S.L., Smith M.A., Perry G., Carey P.R. Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence. Biochemistry 2003, 42:2768-2773.
    • (2003) Biochemistry , vol.42 , pp. 2768-2773
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3    Siedlak, S.L.4    Smith, M.A.5    Perry, G.6    Carey, P.R.7
  • 21
    • 0026001491 scopus 로고
    • The distribution of synapsin I and synaptophysin in hippocampal neurons developing in culture
    • Fletcher T.L., Cameron P., De Camilli P., Banker G. The distribution of synapsin I and synaptophysin in hippocampal neurons developing in culture. J. Neurosci. 1991, 11:1617-1626.
    • (1991) J. Neurosci. , vol.11 , pp. 1617-1626
    • Fletcher, T.L.1    Cameron, P.2    De Camilli, P.3    Banker, G.4
  • 23
    • 0026486613 scopus 로고
    • Induction of calcium-independent nitric oxide synthase activity in primary rat glial cultures
    • Galea E., Feinstein D.L., Reis D.J. Induction of calcium-independent nitric oxide synthase activity in primary rat glial cultures. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:10945-10949.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10945-10949
    • Galea, E.1    Feinstein, D.L.2    Reis, D.J.3
  • 24
    • 33645299024 scopus 로고    scopus 로고
    • Visualizing membrane microdomains by Laurdan 2-photon microscopy
    • Gaus K., Zech T., Harder T. Visualizing membrane microdomains by Laurdan 2-photon microscopy. Mol. Membr. Biol. 2006, 23:41-48.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 41-48
    • Gaus, K.1    Zech, T.2    Harder, T.3
  • 26
    • 0032403433 scopus 로고    scopus 로고
    • Regulation of F-actin stability in dendritic spines by glutamate receptors and calcineurin
    • Halpain S., Hipolito A., Saffer L. Regulation of F-actin stability in dendritic spines by glutamate receptors and calcineurin. J. Neurosci. 1998, 18:9835-9844.
    • (1998) J. Neurosci. , vol.18 , pp. 9835-9844
    • Halpain, S.1    Hipolito, A.2    Saffer, L.3
  • 28
    • 79956210669 scopus 로고    scopus 로고
    • Nonapoptotic function of BAD and BAX in long-term depression of synaptic transmission
    • Jiao S., Li Z. Nonapoptotic function of BAD and BAX in long-term depression of synaptic transmission. Neuron 2011, 70:758-772.
    • (2011) Neuron , vol.70 , pp. 758-772
    • Jiao, S.1    Li, Z.2
  • 30
    • 24744472049 scopus 로고    scopus 로고
    • β-amyloid-induced dynamin 1 depletion in hippocampal neurons. A potential mechanism for early cognitive decline in Alzheimer disease
    • Kelly B.L., Vassar R., Ferreira A. β-amyloid-induced dynamin 1 depletion in hippocampal neurons. A potential mechanism for early cognitive decline in Alzheimer disease. J. Biol. Chem. 2005, 280:31746-31753.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31746-31753
    • Kelly, B.L.1    Vassar, R.2    Ferreira, A.3
  • 32
    • 34447649563 scopus 로고    scopus 로고
    • Abeta oligomer-mediated long-term potentiation impairment involves protein phosphatase 1-dependent mechanisms
    • Knobloch M., Farinelli M., Konietzko U., Nitsch R.M., Mansuy I.M. Abeta oligomer-mediated long-term potentiation impairment involves protein phosphatase 1-dependent mechanisms. J. Neurosci. 2007, 27:7648-7653.
    • (2007) J. Neurosci. , vol.27 , pp. 7648-7653
    • Knobloch, M.1    Farinelli, M.2    Konietzko, U.3    Nitsch, R.M.4    Mansuy, I.M.5
  • 35
    • 17044439021 scopus 로고    scopus 로고
    • Alzheimer's disease: Aβ, tau and synaptic dysfunction
    • LaFerla F.M., Oddo S. Alzheimer's disease: Aβ, tau and synaptic dysfunction. Trends Mol. Med. 2005, 11:170-176.
    • (2005) Trends Mol. Med. , vol.11 , pp. 170-176
    • LaFerla, F.M.1    Oddo, S.2
  • 36
    • 79955769953 scopus 로고    scopus 로고
    • Soluble Aβ oligomers inhibit long-term potentiation through a mechanism involving excessive activation of extrasynaptic NR2B-containing NMDA receptors
    • Li S., Jin M., Koeglsperger T., Shepardson N.E., Shankar G.M., Selkoe D.J. Soluble Aβ oligomers inhibit long-term potentiation through a mechanism involving excessive activation of extrasynaptic NR2B-containing NMDA receptors. J. Neurosci. 2011, 31:6627-6638.
    • (2011) J. Neurosci. , vol.31 , pp. 6627-6638
    • Li, S.1    Jin, M.2    Koeglsperger, T.3    Shepardson, N.E.4    Shankar, G.M.5    Selkoe, D.J.6
  • 37
    • 77953271477 scopus 로고    scopus 로고
    • Caspase-3 activation via mitochondria is required for long-term depression and AMPA receptor internalization
    • Li Z., Jo J., Jia J.M., Lo S.C., Whitcomb D.J., Jiao S., Cho K., Sheng M. Caspase-3 activation via mitochondria is required for long-term depression and AMPA receptor internalization. Cell 2010, 141:859-871.
    • (2010) Cell , vol.141 , pp. 859-871
    • Li, Z.1    Jo, J.2    Jia, J.M.3    Lo, S.C.4    Whitcomb, D.J.5    Jiao, S.6    Cho, K.7    Sheng, M.8
  • 38
    • 78651282081 scopus 로고    scopus 로고
    • Surprising toxicity and assembly behaviour of amyloid β-protein oxidized to sulfone
    • Maiti P., Piacentini R., Ripoli C., Grassi C., Bitan G. Surprising toxicity and assembly behaviour of amyloid β-protein oxidized to sulfone. Biochem. J. 2011, 433:323-332.
    • (2011) Biochem. J. , vol.433 , pp. 323-332
    • Maiti, P.1    Piacentini, R.2    Ripoli, C.3    Grassi, C.4    Bitan, G.5
  • 39
    • 79955697109 scopus 로고    scopus 로고
    • Impact of beta amyloid on excitatory synaptic transmission and plasticity
    • Springer-Verlag, Berlin Heidelberg, D.J. Selkoe, A. Triller, Y. Christen (Eds.)
    • Malinow R., Hsieh H., Wei W. Impact of beta amyloid on excitatory synaptic transmission and plasticity. Synaptic Plasticity and the Mechanism of Alzheimer's Disease 2008, 63-68. Springer-Verlag, Berlin Heidelberg. D.J. Selkoe, A. Triller, Y. Christen (Eds.).
    • (2008) Synaptic Plasticity and the Mechanism of Alzheimer's Disease , pp. 63-68
    • Malinow, R.1    Hsieh, H.2    Wei, W.3
  • 42
    • 84861803361 scopus 로고    scopus 로고
    • NMDA receptors and BAX are essential for Aβ impairment of LTP
    • Olsen K.M., Sheng M. NMDA receptors and BAX are essential for Aβ impairment of LTP. Sci. Rep. 2012, 2:225.
    • (2012) Sci. Rep. , vol.2 , pp. 225
    • Olsen, K.M.1    Sheng, M.2
  • 43
    • 77449122733 scopus 로고    scopus 로고
    • β-amyloid causes depletion of synaptic vesicles leading to neurotransmission failure
    • Parodi J., Sepúlveda F.J., Roa J., Opazo C., Inestrosa N.C., Aguayo L.G. β-amyloid causes depletion of synaptic vesicles leading to neurotransmission failure. J. Biol. Chem. 2010, 285:2506-2514.
    • (2010) J. Biol. Chem. , vol.285 , pp. 2506-2514
    • Parodi, J.1    Sepúlveda, F.J.2    Roa, J.3    Opazo, C.4    Inestrosa, N.C.5    Aguayo, L.G.6
  • 46
    • 44649199251 scopus 로고    scopus 로고
    • Dysregulation of intracellular calcium homeostasis is responsible for neuronal death in an experimental model of selective hippocampal degeneration induced by trimethyltin
    • Piacentini R., Gangitano C., Ceccariglia S., Del Fà A., Azzena G.B., Michetti F., Grassi C. Dysregulation of intracellular calcium homeostasis is responsible for neuronal death in an experimental model of selective hippocampal degeneration induced by trimethyltin. J. Neurochem. 2008, 105:2109-2121.
    • (2008) J. Neurochem. , vol.105 , pp. 2109-2121
    • Piacentini, R.1    Gangitano, C.2    Ceccariglia, S.3    Del Fà, A.4    Azzena, G.B.5    Michetti, F.6    Grassi, C.7
  • 48
    • 38849129323 scopus 로고    scopus 로고
    • Functional role of cyclic nucleotide-gated channels in rat medial vestibular nucleus neurons
    • Podda M.V., D'Ascenzo M., Leone L., Piacentini R., Azzena G.B., Grassi C. Functional role of cyclic nucleotide-gated channels in rat medial vestibular nucleus neurons. J. Physiol. 2008, 586:803-815.
    • (2008) J. Physiol. , vol.586 , pp. 803-815
    • Podda, M.V.1    D'Ascenzo, M.2    Leone, L.3    Piacentini, R.4    Azzena, G.B.5    Grassi, C.6
  • 53
    • 0036521872 scopus 로고    scopus 로고
    • The effects of temperature on vesicular supply and release in autaptic cultures of rat and mouse hippocampal neurons
    • Pyott S.J., Rosenmund C. The effects of temperature on vesicular supply and release in autaptic cultures of rat and mouse hippocampal neurons. J. Physiol. 2002, 539:523-535.
    • (2002) J. Physiol. , vol.539 , pp. 523-535
    • Pyott, S.J.1    Rosenmund, C.2
  • 55
    • 80055101575 scopus 로고    scopus 로고
    • Photo-induced cross-linking of unmodified proteins (PICUP) applied to amyloidogenic peptides
    • pii:1071
    • Rahimi F., Maiti P., Bitan G. Photo-induced cross-linking of unmodified proteins (PICUP) applied to amyloidogenic peptides. J. Vis. Exp 2009, pii:1071.
    • (2009) J. Vis. Exp
    • Rahimi, F.1    Maiti, P.2    Bitan, G.3
  • 56
    • 49249118742 scopus 로고    scopus 로고
    • Neurotoxic effect of oligomeric and fibrillar species of amyloid-beta peptide 1-42: involvement of endoplasmic reticulum calcium release in oligomer-induced cell death
    • Resende R., Ferreiro E., Pereira C., Resende de Oliveira C. Neurotoxic effect of oligomeric and fibrillar species of amyloid-beta peptide 1-42: involvement of endoplasmic reticulum calcium release in oligomer-induced cell death. Neuroscience 2008, 155:725-737.
    • (2008) Neuroscience , vol.155 , pp. 725-737
    • Resende, R.1    Ferreiro, E.2    Pereira, C.3    Resende de Oliveira, C.4
  • 58
    • 33750904405 scopus 로고    scopus 로고
    • 3 3-kinase A from dendritic spines is rapid and reversible
    • 3 3-kinase A from dendritic spines is rapid and reversible. Eur. J. Neurosci. 2006, 24:2491-2503.
    • (2006) Eur. J. Neurosci. , vol.24 , pp. 2491-2503
    • Schell, M.J.1    Irvine, R.F.2
  • 59
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe D.J. Alzheimer's disease is a synaptic failure. Science 2002, 298:789-791.
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 60
    • 44549087765 scopus 로고    scopus 로고
    • Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior
    • Selkoe D.J. Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior. Behav. Brain Res. 2008, 192:106-113.
    • (2008) Behav. Brain Res. , vol.192 , pp. 106-113
    • Selkoe, D.J.1
  • 61
    • 61349164312 scopus 로고    scopus 로고
    • Beta amyloid oligomers and fibrils stimulate differential activation of primary microglia
    • Sondag C.M., Dhawan G., Combs C.K. Beta amyloid oligomers and fibrils stimulate differential activation of primary microglia. J. Neuroinflammation 2009, 6:1.
    • (2009) J. Neuroinflammation , vol.6 , pp. 1
    • Sondag, C.M.1    Dhawan, G.2    Combs, C.K.3
  • 63
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid- β peptide oligomerization and fibrillogenesis
    • Stine W.B., Dahlgren K.N., Krafft G.A., LaDu M.J. In vitro characterization of conditions for amyloid- β peptide oligomerization and fibrillogenesis. J. Biol. Chem. 2003, 278:11612-11622.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11612-11622
    • Stine, W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    LaDu, M.J.4
  • 64
    • 33846068084 scopus 로고    scopus 로고
    • Amyloid precursor protein overexpression depresses excitatory transmission through both presynaptic and postsynaptic mechanisms
    • Ting J.T., Kelley B.G., Lambert T.J., Cook D.G., Sullivan J.M. Amyloid precursor protein overexpression depresses excitatory transmission through both presynaptic and postsynaptic mechanisms. Proc. Natl. Acad. Sci. U. S. A. 2006, 104:353-358.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 353-358
    • Ting, J.T.1    Kelley, B.G.2    Lambert, T.J.3    Cook, D.G.4    Sullivan, J.M.5
  • 65
    • 1842610852 scopus 로고    scopus 로고
    • Block of long-term potentiation by naturally secreted and synthetic amyloid β-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5
    • Wang Q., Walsh D.M., Rowan M.J., Selkoe D.J., Anwyl R. Block of long-term potentiation by naturally secreted and synthetic amyloid β-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5. J. Neurosci. 2004, 24:3370-3378.
    • (2004) J. Neurosci. , vol.24 , pp. 3370-3378
    • Wang, Q.1    Walsh, D.M.2    Rowan, M.J.3    Selkoe, D.J.4    Anwyl, R.5
  • 67
    • 33751106208 scopus 로고    scopus 로고
    • Aβ42 is more rigid than Aβ40 at the C terminus: implications for Aβ aggregation and toxicity
    • Yan Y., Wang C. Aβ42 is more rigid than Aβ40 at the C terminus: implications for Aβ aggregation and toxicity. J. Mol. Biol. 2006, 364:853-862.
    • (2006) J. Mol. Biol. , vol.364 , pp. 853-862
    • Yan, Y.1    Wang, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.