메뉴 건너뛰기




Volumn 55, Issue 8, 2009, Pages 796-801

Oligomeric aggregates of amyloid β peptide 1-42 activate ERK/MAPK in SH-SY5Y cells via the α7 nicotinic receptor

Author keywords

7 nicotinic receptor; Amyloid beta; Atomic force microscopy; ERK MAPK; Fibrillar amyloid; Oligomeric amyloid; SH SY5Y cells

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; AMYLOID BETA PROTEIN[1-42]; BUNGAROTOXIN RECEPTOR; METHYLLYCACONITINE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3;

EID: 70349952431     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2009.08.002     Document Type: Article
Times cited : (44)

References (49)
  • 1
    • 5444257609 scopus 로고    scopus 로고
    • MAPK recruitment by β-amyloid in organotypic hippocampal slice cultures depends on physical state and exposure time
    • Bell K.A., O'Riordan K.J., Sweatt J.D., and Dineley K.T. MAPK recruitment by β-amyloid in organotypic hippocampal slice cultures depends on physical state and exposure time. J. Neurochem. 91 (2004) 349-361
    • (2004) J. Neurochem. , vol.91 , pp. 349-361
    • Bell, K.A.1    O'Riordan, K.J.2    Sweatt, J.D.3    Dineley, K.T.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
    • Dahlgren K.N., Manelli A.M., Stine Jr. W.B., Baker L.K., Krafft G.A., and LaDuF M.J. Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability. J. Biol. Chem. 277 (2002) 32046-32053
    • (2002) J. Biol. Chem. , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine Jr., W.B.3    Baker, L.K.4    Krafft, G.A.5    LaDuF, M.J.6
  • 8
    • 0036488178 scopus 로고    scopus 로고
    • Nicotine activates the extracellular signal-regulated kinase 1/2 via the α7 nicotinic acetylcholine receptor and protein kinase A, in SH-SY5Y cells and hippocampal neurones
    • Dajas-Bailador F.A., Soliakov L., and Wonnacott S. Nicotine activates the extracellular signal-regulated kinase 1/2 via the α7 nicotinic acetylcholine receptor and protein kinase A, in SH-SY5Y cells and hippocampal neurones. J. Neurochem. 80 (2002) 520-530
    • (2002) J. Neurochem. , vol.80 , pp. 520-530
    • Dajas-Bailador, F.A.1    Soliakov, L.2    Wonnacott, S.3
  • 10
    • 0032080849 scopus 로고    scopus 로고
    • Inhibition of mitogen-activated protein kinase kinase blocks T cell proliferation but does not induce or prevent anergy
    • DeSilva D.R., Jones E.A., Favata M.F., Jaffee B.D., Magolda R.L., Trzaskos J.M., and Scherle P.A. Inhibition of mitogen-activated protein kinase kinase blocks T cell proliferation but does not induce or prevent anergy. J. Immunol. 160 (1998) 4175-4181
    • (1998) J. Immunol. , vol.160 , pp. 4175-4181
    • DeSilva, D.R.1    Jones, E.A.2    Favata, M.F.3    Jaffee, B.D.4    Magolda, R.L.5    Trzaskos, J.M.6    Scherle, P.A.7
  • 11
    • 0029078972 scopus 로고
    • Correlations of synaptic and pathological markers with cognition of the elderly
    • discussion 298-304
    • Dickson D.W., Crystal H.A., Bevona C., Honer W., Vincent I., and Davies P. Correlations of synaptic and pathological markers with cognition of the elderly. Neurobiol. Aging 16 (1995) 285-298 discussion 298-304
    • (1995) Neurobiol. Aging , vol.16 , pp. 285-298
    • Dickson, D.W.1    Crystal, H.A.2    Bevona, C.3    Honer, W.4    Vincent, I.5    Davies, P.6
  • 12
    • 0037067717 scopus 로고    scopus 로고
    • β-Amyloid peptide activates α7 nicotinic acetylcholine receptors expressed in Xenopus oocytes
    • Dineley K.T., Bell K.A., Bui D., and Sweatt J.D. β-Amyloid peptide activates α7 nicotinic acetylcholine receptors expressed in Xenopus oocytes. J. Biol. Chem. 277 (2002) 25056-25061
    • (2002) J. Biol. Chem. , vol.277 , pp. 25056-25061
    • Dineley, K.T.1    Bell, K.A.2    Bui, D.3    Sweatt, J.D.4
  • 13
    • 0035875962 scopus 로고    scopus 로고
    • β-amyloid activates the mitogen-activated protein kinase cascade via hippocampal α7 nicotinic acetylcholine receptors: in vitro and in vivo mechanisms related to Alzheimer's disease
    • Dineley K.T., Westerman M., Bui D., Bell K., Ashe K.H., and Sweatt J.D. β-amyloid activates the mitogen-activated protein kinase cascade via hippocampal α7 nicotinic acetylcholine receptors: in vitro and in vivo mechanisms related to Alzheimer's disease. J. Neurosci. 21 (2001) 4125-4133
    • (2001) J. Neurosci. , vol.21 , pp. 4125-4133
    • Dineley, K.T.1    Westerman, M.2    Bui, D.3    Bell, K.4    Ashe, K.H.5    Sweatt, J.D.6
  • 14
    • 33847787591 scopus 로고    scopus 로고
    • Oligomeric amyloid decreases basal levels of brain-derived neurotrophic factor (BDNF) mRNA via specific downregulation of BDNF transcripts IV and V in differentiated human neuroblastoma cells
    • Garzon D.J., and Fahnestock M. Oligomeric amyloid decreases basal levels of brain-derived neurotrophic factor (BDNF) mRNA via specific downregulation of BDNF transcripts IV and V in differentiated human neuroblastoma cells. J. Neurosci. 27 (2007) 2628-2635
    • (2007) J. Neurosci. , vol.27 , pp. 2628-2635
    • Garzon, D.J.1    Fahnestock, M.2
  • 17
    • 0037440717 scopus 로고    scopus 로고
    • Amyloid β(1-42) peptide alters the gating of human and mouse α-bungarotoxin-sensitive nicotinic receptors
    • Grassi F., Palma E., Tonini R., Amici M., Ballivet M., and Eusebi F. Amyloid β(1-42) peptide alters the gating of human and mouse α-bungarotoxin-sensitive nicotinic receptors. J. Physiol. 547 (2003) 147-157
    • (2003) J. Physiol. , vol.547 , pp. 147-157
    • Grassi, F.1    Palma, E.2    Tonini, R.3    Amici, M.4    Ballivet, M.5    Eusebi, F.6
  • 18
    • 1442264828 scopus 로고    scopus 로고
    • Take five-BACE and the gamma-secretase quartet conduct Alzheimer's amyloid β-peptide generation
    • Haass C. Take five-BACE and the gamma-secretase quartet conduct Alzheimer's amyloid β-peptide generation. EMBO J. 23 (2004) 483-488
    • (2004) EMBO J. , vol.23 , pp. 483-488
    • Haass, C.1
  • 20
    • 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., and 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 13 (1994) 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
  • 21
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease
    • Jarrett J.T., Berger E.P., and Landsbury J.T. The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32 (1993) 4693-4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Landsbury, J.T.3
  • 22
    • 41649106212 scopus 로고    scopus 로고
    • Oligomeric β-amyloid(1-42) induces the expression of Alzheimer disease-relevant proteins in cholinergic SN56.B5. G4 cells as revealed by proteomic analysis
    • Joerchel S., Raap M., Bigl M., Eschrich K., and Schliebs R. Oligomeric β-amyloid(1-42) induces the expression of Alzheimer disease-relevant proteins in cholinergic SN56.B5. G4 cells as revealed by proteomic analysis. Int. J. Dev. Neurosci. (2008) 301-308
    • (2008) Int. J. Dev. Neurosci. , pp. 301-308
    • Joerchel, S.1    Raap, M.2    Bigl, M.3    Eschrich, K.4    Schliebs, R.5
  • 23
    • 1542327573 scopus 로고    scopus 로고
    • Soluble oligomeric Aβ disrupts the protein kinase C signaling pathway
    • Kim H., Kim J., Chae S., Park Y., Kwon K., and Hong S. Soluble oligomeric Aβ disrupts the protein kinase C signaling pathway. Neuroreport 15 (2004) 503-507
    • (2004) Neuroreport , vol.15 , pp. 503-507
    • Kim, H.1    Kim, J.2    Chae, S.3    Park, Y.4    Kwon, K.5    Hong, S.6
  • 24
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies
    • Kirkitadze M.D., Bitan G., and Teplow D.B. Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies. J. Neurosci. Res. 69 (2002) 567-577
    • (2002) J. Neurosci. Res. , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0037381479 scopus 로고    scopus 로고
    • Differential physiologic responses of α7 nicotinic acetylcholine receptors to β-amyloid1-40 and β-amyloid1-42
    • Lee D.H., and Wang H.Y. Differential physiologic responses of α7 nicotinic acetylcholine receptors to β-amyloid1-40 and β-amyloid1-42. J. Neurobiol. 55 (2003) 25-30
    • (2003) J. Neurobiol. , vol.55 , pp. 25-30
    • Lee, D.H.1    Wang, H.Y.2
  • 29
    • 0038561173 scopus 로고    scopus 로고
    • Long-term potentiation: outstanding questions and attempted synthesis
    • Lisman J. Long-term potentiation: outstanding questions and attempted synthesis. Philos. Trans. Roy. Soc., Lond. B: Biol. Sci. 358 (2003) 829-842
    • (2003) Philos. Trans. Roy. Soc., Lond. B: Biol. Sci. , vol.358 , pp. 829-842
    • Lisman, J.1
  • 33
    • 0032480771 scopus 로고    scopus 로고
    • The presence of amyloid β-protein in the detergent-insoluble membrane compartment of human neuroblastoma cells
    • Morishima-Kawashima M., and Ihara Y. The presence of amyloid β-protein in the detergent-insoluble membrane compartment of human neuroblastoma cells. Biochemistry 37 (1998) 15247-15253
    • (1998) Biochemistry , vol.37 , pp. 15247-15253
    • Morishima-Kawashima, M.1    Ihara, Y.2
  • 35
    • 56849091064 scopus 로고    scopus 로고
    • Selective induction of calcineurin activity and signaling by oligomeric amyloid beta
    • Reese L.C., Zhang W.R., Dineley K.T., Kayed R., and Taglialatela G. Selective induction of calcineurin activity and signaling by oligomeric amyloid beta. Aging Cell 7 (2008) 824-835
    • (2008) Aging Cell , vol.7 , pp. 824-835
    • Reese, L.C.1    Zhang, W.R.2    Dineley, K.T.3    Kayed, R.4    Taglialatela, G.5
  • 36
    • 0034871936 scopus 로고    scopus 로고
    • Differential effects of chronic drug treatment on α3* and α7 nicotinic receptor binding sites, in hippocampal neurones and SH-SY5Y cells
    • Ridley D.L., Rogers A., and Wonnacott S. Differential effects of chronic drug treatment on α3* and α7 nicotinic receptor binding sites, in hippocampal neurones and SH-SY5Y cells. Br. J. Pharmacol. 133 (2001) 1286-1295
    • (2001) Br. J. Pharmacol. , vol.133 , pp. 1286-1295
    • Ridley, D.L.1    Rogers, A.2    Wonnacott, S.3
  • 41
    • 33646171899 scopus 로고    scopus 로고
    • A model of the roles of essential kinases in the induction and expression of late long-term potentiation
    • Smolen P., Baxter D.A., and Byrne J.H. A model of the roles of essential kinases in the induction and expression of late long-term potentiation. Biophys. J. 90 (2006) 2760-2775
    • (2006) Biophys. J. , vol.90 , pp. 2760-2775
    • Smolen, P.1    Baxter, D.A.2    Byrne, J.H.3
  • 42
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
    • Stine Jr. W.B., Dahlgren K.N., Krafft G.A., and LaDu M.J. In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis. J. Biol. Chem. 278 (2003) 11612-11622
    • (2003) J. Biol. Chem. , vol.278 , pp. 11612-11622
    • Stine Jr., W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    LaDu, M.J.4
  • 43
    • 0035166616 scopus 로고    scopus 로고
    • The neuronal MAP kinase cascade: a biochemical signal integration system subserving synaptic plasticity and memory
    • Sweatt J.D. The neuronal MAP kinase cascade: a biochemical signal integration system subserving synaptic plasticity and memory. J. Neurochem. 76 (2001) 1-10
    • (2001) J. Neurochem. , vol.76 , pp. 1-10
    • Sweatt, J.D.1
  • 44
    • 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., and Katzman R. Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann. Neurol. 30 (1991) 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
  • 45
    • 36348935683 scopus 로고    scopus 로고
    • Soluble Aβ inhibits specific signal transduction cascades common to the insulin receptor pathway
    • Townsend M., Mehta T., and Selkoe D.J. Soluble Aβ inhibits specific signal transduction cascades common to the insulin receptor pathway. J. Biol. Chem. 282 (2007) 33305-33312
    • (2007) J. Biol. Chem. , vol.282 , pp. 33305-33312
    • Townsend, M.1    Mehta, T.2    Selkoe, D.J.3
  • 46
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., Rowan M.J., and Selkoe D.J. Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002) 535-539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 47
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers-a decade of discovery
    • Walsh D.M., and Selkoe D.J. Aβ oligomers-a decade of discovery. J. Neurochem. 101 (2007) 1172-1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 48
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of amyloid β-protein begins intracellularly in cells derived from human brain
    • Walsh D.M., Tseng B.P., Rydel R.E., Podlisny M.B., and Selkoe D.J. The oligomerization of amyloid β-protein begins intracellularly in cells derived from human brain. Biochemistry 39 (2000) 10831-10839
    • (2000) Biochemistry , vol.39 , pp. 10831-10839
    • Walsh, D.M.1    Tseng, B.P.2    Rydel, R.E.3    Podlisny, M.B.4    Selkoe, D.J.5
  • 49
    • 0042357192 scopus 로고    scopus 로고
    • α7 nicotinic acetylcholine receptors mediate β-amyloid peptide-induced tau protein phosphorylation
    • Wang H.Y., Li W., Benedetti N.J., and Lee D.H. α7 nicotinic acetylcholine receptors mediate β-amyloid peptide-induced tau protein phosphorylation. J. Biol. Chem. 278 (2003) 31547-31553
    • (2003) J. Biol. Chem. , vol.278 , pp. 31547-31553
    • Wang, H.Y.1    Li, W.2    Benedetti, N.J.3    Lee, D.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.