메뉴 건너뛰기




Volumn 566, Issue , 2014, Pages 125-130

Activity-independent release of the amyloid β-peptide from rat brain nerve terminals

Author keywords

Alzheimer disease; Amyloid peptide; Glutamate; Synapse; Synaptic vesicles; Synaptosomes

Indexed keywords

4 AMINOPYRIDINE; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; BETA SECRETASE; GAMMA SECRETASE; GLUTAMIC ACID; POTASSIUM CHLORIDE;

EID: 84896117270     PISSN: 03043940     EISSN: 18727972     Source Type: Journal    
DOI: 10.1016/j.neulet.2014.02.050     Document Type: Article
Times cited : (13)

References (27)
  • 1
    • 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
  • 4
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta 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., Selkoe D.J. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 2002, 416:535-539.
    • (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
  • 5
    • 84655160766 scopus 로고    scopus 로고
    • Proteolytic processing of Alzheimer's beta-amyloid precursor protein
    • Zhang H., Ma Q., Zhang Y.W., Xu H. Proteolytic processing of Alzheimer's beta-amyloid precursor protein. J. Neurochem. 2012, 120(Suppl 1):9-21.
    • (2012) J. Neurochem. , vol.120 , Issue.SUPPL 1 , pp. 9-21
    • Zhang, H.1    Ma, Q.2    Zhang, Y.W.3    Xu, H.4
  • 6
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease
    • Jarrett J.T., Berger E.P., Lansbury P.T. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 1993, 32:4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 7
    • 0033385632 scopus 로고    scopus 로고
    • Neurotoxicity and oxidative damage of beta amyloid 1-42 versus beta amyloid 1-40 in the mouse cerebral cortex
    • Klein A.M., Kowall N.W., Ferrante R.J. Neurotoxicity and oxidative damage of beta amyloid 1-42 versus beta amyloid 1-40 in the mouse cerebral cortex. Ann. N.Y. Acad. Sci. 1999, 893:314-320.
    • (1999) Ann. N.Y. Acad. Sci. , vol.893 , pp. 314-320
    • Klein, A.M.1    Kowall, N.W.2    Ferrante, R.J.3
  • 9
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway
    • Koo E.H., Squazzo S.L. Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J. Biol. Chem. 1994, 269:17386-17389.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 10
    • 79955529460 scopus 로고    scopus 로고
    • Large quantities of Abeta peptide are constitutively released during amyloid precursor protein metabolism in vivo and in vitro
    • Moghekar A., Rao S., Li M., Ruben D., Mammen A., Tang X., O'Brien R.J. Large quantities of Abeta peptide are constitutively released during amyloid precursor protein metabolism in vivo and in vitro. J. Biol. Chem. 2011, 286:15989-15997.
    • (2011) J. Biol. Chem. , vol.286 , pp. 15989-15997
    • Moghekar, A.1    Rao, S.2    Li, M.3    Ruben, D.4    Mammen, A.5    Tang, X.6    O'Brien, R.J.7
  • 11
    • 77953019895 scopus 로고    scopus 로고
    • Intraneuronal beta-amyloid accumulation and synapse pathology in Alzheimer's disease
    • Gouras G.K., Tampellini D., Takahashi R.H., Capetillo-Zarate E. Intraneuronal beta-amyloid accumulation and synapse pathology in Alzheimer's disease. Acta Neuropathol. 2010, 119:523-541.
    • (2010) Acta Neuropathol. , vol.119 , pp. 523-541
    • Gouras, G.K.1    Tampellini, D.2    Takahashi, R.H.3    Capetillo-Zarate, E.4
  • 13
    • 77953024447 scopus 로고    scopus 로고
    • Analysis of microdissected human neurons by a sensitive ELISA reveals a correlation between elevated intracellular concentrations of Abeta42 and Alzheimer's disease neuropathology
    • Hashimoto M., Bogdanovic N., Volkmann I., Aoki M., Winblad B., Tjernberg L.O. Analysis of microdissected human neurons by a sensitive ELISA reveals a correlation between elevated intracellular concentrations of Abeta42 and Alzheimer's disease neuropathology. Acta Neuropathol. 2010, 119:543-554.
    • (2010) Acta Neuropathol. , vol.119 , pp. 543-554
    • Hashimoto, M.1    Bogdanovic, N.2    Volkmann, I.3    Aoki, M.4    Winblad, B.5    Tjernberg, L.O.6
  • 14
    • 33746593662 scopus 로고    scopus 로고
    • Alzheimer's disease beta-amyloid peptides are released in association with exosomes
    • Rajendran L., Honsho M., Zahn T.R., Keller P., Geiger K.D., Verkade P., Simons K. Alzheimer's disease beta-amyloid peptides are released in association with exosomes. PNAS 2006, 103:11172-11177.
    • (2006) PNAS , vol.103 , pp. 11172-11177
    • Rajendran, L.1    Honsho, M.2    Zahn, T.R.3    Keller, P.4    Geiger, K.D.5    Verkade, P.6    Simons, K.7
  • 22
    • 0017904468 scopus 로고
    • Calcium transport and porton electrochemical potential gradient in mitochondria from guinea-pig cerebral cortex and rat heart
    • Nicholls D.G. Calcium transport and porton electrochemical potential gradient in mitochondria from guinea-pig cerebral cortex and rat heart. Biochem. J. 1978, 170:511-522.
    • (1978) Biochem. J. , vol.170 , pp. 511-522
    • Nicholls, D.G.1
  • 23
    • 0023370658 scopus 로고
    • Calcium-dependent and -independent release of glutamate from synaptosomes monitored by continuous fluorometry
    • Nicholls D.G., Sihra T.S., Sanchez-Prieto J. Calcium-dependent and -independent release of glutamate from synaptosomes monitored by continuous fluorometry. J. Neurochem. 1987, 49:50-57.
    • (1987) J. Neurochem. , vol.49 , pp. 50-57
    • Nicholls, D.G.1    Sihra, T.S.2    Sanchez-Prieto, J.3
  • 24
    • 0021043142 scopus 로고
    • Substance P release from K+ -depolarized rat brain synaptosomes at one-second resolution
    • Floor E. Substance P release from K+ -depolarized rat brain synaptosomes at one-second resolution. Brain Res. 1983, 279:321-324.
    • (1983) Brain Res. , vol.279 , pp. 321-324
    • Floor, E.1
  • 25
    • 0025969663 scopus 로고
    • Characterization of the release of cholecystokinin-8 from isolated nerve terminals and comparison with exocytosis of classical transmitters
    • Verhage M., Ghijsen W.E., Nicholls D.G., Wiegant V.M. Characterization of the release of cholecystokinin-8 from isolated nerve terminals and comparison with exocytosis of classical transmitters. J. Neurochem. 1991, 56:1394-1400.
    • (1991) J. Neurochem. , vol.56 , pp. 1394-1400
    • Verhage, M.1    Ghijsen, W.E.2    Nicholls, D.G.3    Wiegant, V.M.4
  • 26
    • 77949669251 scopus 로고    scopus 로고
    • Group II metabotropic glutamate receptor stimulation triggers production and release of Alzheimer's amyloid(beta)42 from isolated intact nerve terminals
    • Kim S.H., Fraser P.E., Westaway D., St George-Hyslop P.H., Ehrlich M.E., Gandy S. Group II metabotropic glutamate receptor stimulation triggers production and release of Alzheimer's amyloid(beta)42 from isolated intact nerve terminals. J. Neurosci. 2010, 30:3870-3875.
    • (2010) J. Neurosci. , vol.30 , pp. 3870-3875
    • Kim, S.H.1    Fraser, P.E.2    Westaway, D.3    St George-Hyslop, P.H.4    Ehrlich, M.E.5    Gandy, S.6
  • 27
    • 84881496428 scopus 로고    scopus 로고
    • Activity-induced convergence of APP and BACE-1 in acidic microdomains via an endocytosis-dependent pathway
    • Das U., Scott D.A., Ganguly A., Koo E.H., Tang Y., Roy S. Activity-induced convergence of APP and BACE-1 in acidic microdomains via an endocytosis-dependent pathway. Neuron 2013, 79:447-460.
    • (2013) Neuron , vol.79 , pp. 447-460
    • Das, U.1    Scott, D.A.2    Ganguly, A.3    Koo, E.H.4    Tang, Y.5    Roy, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.