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Volumn 34, Issue 11, 2013, Pages 2517-2524

Drain of the brain: Low-affinity p75 neurotrophin receptor affords a molecular sink for clearance of cortical amyloid β by the cholinergic modulator system

Author keywords

Alzheimer's disease; Amyloid ; Basal forebrain cholinergic neurons; Neurodegenerative disorders; P75 neurotrophin receptor

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; NEUROTROPHIN RECEPTOR P75;

EID: 84881548898     PISSN: 01974580     EISSN: 15581497     Source Type: Journal    
DOI: 10.1016/j.neurobiolaging.2013.05.005     Document Type: Article
Times cited : (16)

References (124)
  • 1
    • 84872168596 scopus 로고    scopus 로고
    • Microglia: scapegoat, saboteur, or something else?
    • Aguzzi A., Barres B.A., Bennett M.L. Microglia: scapegoat, saboteur, or something else?. Science 2013, 339:156-161.
    • (2013) Science , vol.339 , pp. 156-161
    • Aguzzi, A.1    Barres, B.A.2    Bennett, M.L.3
  • 3
    • 0023201044 scopus 로고
    • Long-term neuropathological and neurochemical effects of nucleus basalis lesions in the rat
    • Arendash G.W., Millard W.J., Dunn A.J., Meyer E.M. Long-term neuropathological and neurochemical effects of nucleus basalis lesions in the rat. Science 1987, 238:952-956.
    • (1987) Science , vol.238 , pp. 952-956
    • Arendash, G.W.1    Millard, W.J.2    Dunn, A.J.3    Meyer, E.M.4
  • 4
    • 70450211408 scopus 로고    scopus 로고
    • Amyloid beta serves as an NGF-like neurotrophic factor or acts as a NGF antagonist depending on its concentration
    • Arevalo M.A., Roldan P.M., Chacon P.J., Rodriguez-Tebar A. Amyloid beta serves as an NGF-like neurotrophic factor or acts as a NGF antagonist depending on its concentration. J.Neurochem. 2009, 111:1425-1433.
    • (2009) J.Neurochem. , vol.111 , pp. 1425-1433
    • Arevalo, M.A.1    Roldan, P.M.2    Chacon, P.J.3    Rodriguez-Tebar, A.4
  • 5
    • 0022841967 scopus 로고
    • Behavioral and biochemical effects of nucleus basalis magnocellularis lesions: implications and possible relevance to understanding or treating Alzheimer's disease
    • Bartus R.T., Flicker C., Dean R.L., Fisher S., Pontecorvo M., Figueiredo J. Behavioral and biochemical effects of nucleus basalis magnocellularis lesions: implications and possible relevance to understanding or treating Alzheimer's disease. Prog. Brain Res. 1986, 70:345-361.
    • (1986) Prog. Brain Res. , vol.70 , pp. 345-361
    • Bartus, R.T.1    Flicker, C.2    Dean, R.L.3    Fisher, S.4    Pontecorvo, M.5    Figueiredo, J.6
  • 7
    • 33751165117 scopus 로고    scopus 로고
    • Neurotrophic factors in neurodegeneration
    • Blesch A. Neurotrophic factors in neurodegeneration. Brain Pathol. 2006, 16:295-303.
    • (2006) Brain Pathol. , vol.16 , pp. 295-303
    • Blesch, A.1
  • 8
    • 0029553116 scopus 로고
    • Acetylcholine: a neurotransmitter for learning and memory?
    • Blokland A. Acetylcholine: a neurotransmitter for learning and memory?. Brain Res. Brain Res. Rev. 1995, 21:285-300.
    • (1995) Brain Res. Brain Res. Rev. , vol.21 , pp. 285-300
    • Blokland, A.1
  • 9
    • 34250811784 scopus 로고    scopus 로고
    • LRP in amyloid-beta production and metabolism
    • Bu G., Cam J., Zerbinatti C. LRP in amyloid-beta production and metabolism. Ann. N. Y. Acad. Sci. 2006, 1086:35-53.
    • (2006) Ann. N. Y. Acad. Sci. , vol.1086 , pp. 35-53
    • Bu, G.1    Cam, J.2    Zerbinatti, C.3
  • 10
    • 5344271854 scopus 로고    scopus 로고
    • Memory and executive function in aging and AD: multiple factors that cause decline and reserve factors that compensate
    • Buckner R.L. Memory and executive function in aging and AD: multiple factors that cause decline and reserve factors that compensate. Neuron 2004, 44:195-208.
    • (2004) Neuron , vol.44 , pp. 195-208
    • Buckner, R.L.1
  • 11
    • 41949121294 scopus 로고    scopus 로고
    • The brain's default network: anatomy, function, and relevance to disease
    • Buckner R.L., Andrews-Hanna J.R., Schacter D.L. The brain's default network: anatomy, function, and relevance to disease. Ann. N. Y. Acad. Sci. 2008, 1124:1-38.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1124 , pp. 1-38
    • Buckner, R.L.1    Andrews-Hanna, J.R.2    Schacter, D.L.3
  • 12
    • 69449091192 scopus 로고    scopus 로고
    • Fates of neurotrophins after retrograde axonal transport: phosphorylation of p75NTR is a sorting signal for delayed degradation
    • Butowt R., von Bartheld C.S. Fates of neurotrophins after retrograde axonal transport: phosphorylation of p75NTR is a sorting signal for delayed degradation. J.Neurosci. 2009, 29:10715-10729.
    • (2009) J.Neurosci. , vol.29 , pp. 10715-10729
    • Butowt, R.1    von Bartheld, C.S.2
  • 13
    • 0036794008 scopus 로고    scopus 로고
    • Declining expression of neprilysin in Alzheimer disease vasculature: possible involvement in cerebral amyloid angiopathy
    • Carpentier M., Robitaille Y., DesGroseillers L., Boileau G., Marcinkiewicz M. Declining expression of neprilysin in Alzheimer disease vasculature: possible involvement in cerebral amyloid angiopathy. J.Neuropathol. Exp. Neurol. 2002, 61:849-856.
    • (2002) J.Neuropathol. Exp. Neurol. , vol.61 , pp. 849-856
    • Carpentier, M.1    Robitaille, Y.2    DesGroseillers, L.3    Boileau, G.4    Marcinkiewicz, M.5
  • 15
    • 50949097728 scopus 로고    scopus 로고
    • Oligomer-specific Abeta toxicity in cell models is mediated by selective uptake
    • Chafekar S.M., Baas F., Scheper W. Oligomer-specific Abeta toxicity in cell models is mediated by selective uptake. Biochim. Biophys. Acta 2008, 1782:523-531.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 523-531
    • Chafekar, S.M.1    Baas, F.2    Scheper, W.3
  • 19
    • 26844507790 scopus 로고    scopus 로고
    • ATrkA-to-p75NTR molecular switch activates amyloid beta-peptide generation during aging
    • Costantini C., Weindruch R., Della Valle G., Puglielli L. ATrkA-to-p75NTR molecular switch activates amyloid beta-peptide generation during aging. Biochem. J. 2005, 391:59-67.
    • (2005) Biochem. J. , vol.391 , pp. 59-67
    • Costantini, C.1    Weindruch, R.2    Della Valle, G.3    Puglielli, L.4
  • 20
    • 16844377812 scopus 로고    scopus 로고
    • The role of nerve growth factor receptors in cholinergic basal forebrain degeneration in prodromal Alzheimer disease
    • Counts S.E., Mufson E.J. The role of nerve growth factor receptors in cholinergic basal forebrain degeneration in prodromal Alzheimer disease. J.Neuropathol. Exp. Neurol. 2005, 64:263-272.
    • (2005) J.Neuropathol. Exp. Neurol. , vol.64 , pp. 263-272
    • Counts, S.E.1    Mufson, E.J.2
  • 21
    • 27644457417 scopus 로고    scopus 로고
    • The choroid plexus removes beta-amyloid from brain cerebrospinal fluid
    • Crossgrove J.S., Li G.J., Zheng W. The choroid plexus removes beta-amyloid from brain cerebrospinal fluid. Exp. Biol. Med. (Maywood) 2005, 230:771-776.
    • (2005) Exp. Biol. Med. (Maywood) , vol.230 , pp. 771-776
    • Crossgrove, J.S.1    Li, G.J.2    Zheng, W.3
  • 22
    • 0034839287 scopus 로고    scopus 로고
    • The amyloid precursor protein (APP)-cytoplasmic fragment generated by gamma-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurones in culture
    • Cupers P., Orlans I., Craessaerts K., Annaert W., De Strooper B. The amyloid precursor protein (APP)-cytoplasmic fragment generated by gamma-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurones in culture. J.Neurochem. 2001, 78:1168-1178.
    • (2001) J.Neurochem. , vol.78 , pp. 1168-1178
    • Cupers, P.1    Orlans, I.2    Craessaerts, K.3    Annaert, W.4    De Strooper, B.5
  • 24
    • 0036830562 scopus 로고    scopus 로고
    • The neurotrophin receptor p75(NTR): novel functions and implications for diseases of the nervous system
    • Dechant G., Barde Y.A. The neurotrophin receptor p75(NTR): novel functions and implications for diseases of the nervous system. Nat. Neurosci. 2002, 5:1131-1136.
    • (2002) Nat. Neurosci. , vol.5 , pp. 1131-1136
    • Dechant, G.1    Barde, Y.A.2
  • 25
    • 35948982195 scopus 로고    scopus 로고
    • Neurotrophins redirect p75NTR from a clathrin-independent to a clathrin-dependent endocytic pathway coupled to axonal transport
    • Deinhardt K., Reversi A., Berninghausen O., Hopkins C.R., Schiavo G. Neurotrophins redirect p75NTR from a clathrin-independent to a clathrin-dependent endocytic pathway coupled to axonal transport. Traffic 2007, 8:1736-1749.
    • (2007) Traffic , vol.8 , pp. 1736-1749
    • Deinhardt, K.1    Reversi, A.2    Berninghausen, O.3    Hopkins, C.R.4    Schiavo, G.5
  • 27
    • 0030664667 scopus 로고    scopus 로고
    • Diffuse transmission by acetylcholine in the CNS
    • Descarries L., Gisiger V., Steriade M. Diffuse transmission by acetylcholine in the CNS. Prog. Neurobiol. 1997, 53:603-625.
    • (1997) Prog. Neurobiol. , vol.53 , pp. 603-625
    • Descarries, L.1    Gisiger, V.2    Steriade, M.3
  • 29
    • 34147115541 scopus 로고    scopus 로고
    • Ccr2 deficiency impairs microglial accumulation and accelerates progression of Alzheimer-like disease
    • El Khoury J., Toft M., Hickman S.E., Means T.K., Terada K., Geula C., Luster A.D. Ccr2 deficiency impairs microglial accumulation and accelerates progression of Alzheimer-like disease. Nat. Med. 2007, 13:432-438.
    • (2007) Nat. Med. , vol.13 , pp. 432-438
    • El Khoury, J.1    Toft, M.2    Hickman, S.E.3    Means, T.K.4    Terada, K.5    Geula, C.6    Luster, A.D.7
  • 30
    • 0030636350 scopus 로고    scopus 로고
    • Central cholinergic systems and cognition
    • Everitt B.J., Robbins T.W. Central cholinergic systems and cognition. Annu. Rev. Psychol. 1997, 48:649-684.
    • (1997) Annu. Rev. Psychol. , vol.48 , pp. 649-684
    • Everitt, B.J.1    Robbins, T.W.2
  • 31
    • 84655164275 scopus 로고    scopus 로고
    • Cholinergic modulation of amyloid precursor protein processingwith emphasis on M1 muscarinic receptor: perspectives and challenges intreatment of Alzheimer's disease
    • Fisher A. Cholinergic modulation of amyloid precursor protein processingwith emphasis on M1 muscarinic receptor: perspectives and challenges intreatment of Alzheimer's disease. J.Neurochem. 2012, 120(suppl 1):22-33.
    • (2012) J.Neurochem. , vol.120 , Issue.SUPPL. 1 , pp. 22-33
    • Fisher, A.1
  • 34
    • 71749107981 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein 1 promotes anti-apoptotic signaling in neurons by activating Akt survival pathway
    • Fuentealba R.A., Liu Q., Kanekiyo T., Zhang J., Bu G. Low density lipoprotein receptor-related protein 1 promotes anti-apoptotic signaling in neurons by activating Akt survival pathway. J.Biol. Chem. 2009, 284:34045-34053.
    • (2009) J.Biol. Chem. , vol.284 , pp. 34045-34053
    • Fuentealba, R.A.1    Liu, Q.2    Kanekiyo, T.3    Zhang, J.4    Bu, G.5
  • 35
  • 36
    • 0031964036 scopus 로고    scopus 로고
    • Relationship between plaques, tangles, and loss of cortical cholinergic fibers in Alzheimer disease
    • Geula C., Mesulam M.M., Saroff D.M., Wu C.K. Relationship between plaques, tangles, and loss of cortical cholinergic fibers in Alzheimer disease. J.Neuropathol. Exp. Neurol. 1998, 57:63-75.
    • (1998) J.Neuropathol. Exp. Neurol. , vol.57 , pp. 63-75
    • Geula, C.1    Mesulam, M.M.2    Saroff, D.M.3    Wu, C.K.4
  • 37
    • 41949104908 scopus 로고    scopus 로고
    • Cholinergic neuronal and axonal abnormalities are present early in aging and in Alzheimer disease
    • Geula C., Nagykery N., Nicholas A., Wu C.K. Cholinergic neuronal and axonal abnormalities are present early in aging and in Alzheimer disease. J.Neuropathol. Exp. Neurol. 2008, 67:309-318.
    • (2008) J.Neuropathol. Exp. Neurol. , vol.67 , pp. 309-318
    • Geula, C.1    Nagykery, N.2    Nicholas, A.3    Wu, C.K.4
  • 38
    • 33645301867 scopus 로고    scopus 로고
    • Down regulation of trk but not p75NTR gene expression in single cholinergic basal forebrain neurons mark the progression of Alzheimer's disease
    • Ginsberg S.D., Che S., Wuu J., Counts S.E., Mufson E.J. Down regulation of trk but not p75NTR gene expression in single cholinergic basal forebrain neurons mark the progression of Alzheimer's disease. J.Neurochem. 2006, 97:475-487.
    • (2006) J.Neurochem. , vol.97 , pp. 475-487
    • Ginsberg, S.D.1    Che, S.2    Wuu, J.3    Counts, S.E.4    Mufson, E.J.5
  • 39
    • 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
  • 41
    • 1842427969 scopus 로고    scopus 로고
    • Default-mode network activity distinguishes Alzheimer's disease from healthy aging: evidence from functional MRI
    • Greicius M.D., Srivastava G., Reiss A.L., Menon V. Default-mode network activity distinguishes Alzheimer's disease from healthy aging: evidence from functional MRI. Proc. Natl. Acad. Sci. U.S.A 2004, 101:4637-4642.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 4637-4642
    • Greicius, M.D.1    Srivastava, G.2    Reiss, A.L.3    Menon, V.4
  • 43
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide
    • Haass C., Selkoe D.J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat. Rev. Mol. Cell Biol. 2007, 8:101-112.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 44
    • 35548986304 scopus 로고    scopus 로고
    • Microglia: active sensor and versatile effector cells in the normal and pathologic brain
    • Hanisch U.K., Kettenmann H. Microglia: active sensor and versatile effector cells in the normal and pathologic brain. Nat. Neurosci. 2007, 10:1387-1394.
    • (2007) Nat. Neurosci. , vol.10 , pp. 1387-1394
    • Hanisch, U.K.1    Kettenmann, H.2
  • 45
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 46
    • 77951078680 scopus 로고    scopus 로고
    • Restoring blood-brain barrier P-glycoprotein reduces brain amyloid-beta in a mouse model of Alzheimer's disease
    • Hartz A.M., Miller D.S., Bauer B. Restoring blood-brain barrier P-glycoprotein reduces brain amyloid-beta in a mouse model of Alzheimer's disease. Mol. Pharmacol. 2010, 77:715-723.
    • (2010) Mol. Pharmacol. , vol.77 , pp. 715-723
    • Hartz, A.M.1    Miller, D.S.2    Bauer, B.3
  • 48
    • 42149188846 scopus 로고    scopus 로고
    • Neprilysin and amyloid beta peptide degradation
    • Hersh L.B., Rodgers D.W. Neprilysin and amyloid beta peptide degradation. Curr. Alzheimer Res. 2008, 5:225-231.
    • (2008) Curr. Alzheimer Res. , vol.5 , pp. 225-231
    • Hersh, L.B.1    Rodgers, D.W.2
  • 49
    • 33846621573 scopus 로고    scopus 로고
    • Cysteine protease inhibitors effectively reduce invivo levels of brain beta-amyloid related to Alzheimer's disease
    • Hook V., Kindy M., Hook G. Cysteine protease inhibitors effectively reduce invivo levels of brain beta-amyloid related to Alzheimer's disease. Biol. Chem. 2007, 388:247-252.
    • (2007) Biol. Chem. , vol.388 , pp. 247-252
    • Hook, V.1    Kindy, M.2    Hook, G.3
  • 50
    • 33845411954 scopus 로고    scopus 로고
    • AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss
    • Hsieh H., Boehm J., Sato C., Iwatsubo T., Tomita T., Sisodia S., Malinow R. AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss. Neuron 2006, 52:831-843.
    • (2006) Neuron , vol.52 , pp. 831-843
    • Hsieh, H.1    Boehm, J.2    Sato, C.3    Iwatsubo, T.4    Tomita, T.5    Sisodia, S.6    Malinow, R.7
  • 53
    • 0028169925 scopus 로고
    • Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 42(43)
    • Iwatsubo T., Odaka A., Suzuki N., Mizusawa H., Nukina N., Ihara Y. Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 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
  • 57
    • 0026778656 scopus 로고
    • Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/beta protein
    • Knauer M.F., Soreghan B., Burdick D., Kosmoski J., Glabe C.G. Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/beta protein. Proc. Natl. Acad. Sci. U.S.A 1992, 89:7437-7441.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 7437-7441
    • Knauer, M.F.1    Soreghan, B.2    Burdick, D.3    Kosmoski, J.4    Glabe, C.G.5
  • 59
    • 7744235869 scopus 로고    scopus 로고
    • Microglial phagocytosis of fibrillar beta-amyloid through a beta1 integrin-dependent mechanism
    • Koenigsknecht J., Landreth G. Microglial phagocytosis of fibrillar beta-amyloid through a beta1 integrin-dependent mechanism. J.Neurosci. 2004, 24:9838-9846.
    • (2004) J.Neurosci. , vol.24 , pp. 9838-9846
    • Koenigsknecht, J.1    Landreth, G.2
  • 60
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • LaFerla F.M., Green K.N., Oddo S. Intracellular amyloid-beta in Alzheimer's disease. Nat. Rev. Neurosci. 2007, 8:499-509.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 499-509
    • LaFerla, F.M.1    Green, K.N.2    Oddo, S.3
  • 61
    • 79251550418 scopus 로고    scopus 로고
    • Mechanisms of amyloid-beta peptide uptake by neurons: the role of lipid rafts and lipid raft-associated proteins
    • Lai A.Y., McLaurin J. Mechanisms of amyloid-beta peptide uptake by neurons: the role of lipid rafts and lipid raft-associated proteins. Int. J. Alzheimers Dis. 2010, 2011:548380.
    • (2010) Int. J. Alzheimers Dis. , vol.2011 , pp. 548380
    • Lai, A.Y.1    McLaurin, J.2
  • 63
    • 84871397626 scopus 로고    scopus 로고
    • Cholinergic degeneration is associated with increased plaque deposition and cognitive impairment in APPswe/PS1dE9 mice
    • Laursen B., Mork A., Plath N., Kristiansen U., Bastlund J.F. Cholinergic degeneration is associated with increased plaque deposition and cognitive impairment in APPswe/PS1dE9 mice. Behav. Brain Res. 2013, 240:146-152.
    • (2013) Behav. Brain Res. , vol.240 , pp. 146-152
    • Laursen, B.1    Mork, A.2    Plath, N.3    Kristiansen, U.4    Bastlund, J.F.5
  • 64
    • 84871749175 scopus 로고    scopus 로고
    • Differential regulation of amyloid-beta endocytic trafficking and lysosomal degradation by apolipoprotein E isoforms
    • Li J., Kanekiyo T., Shinohara M., Zhang Y., LaDu M.J., Xu H., Bu G. Differential regulation of amyloid-beta endocytic trafficking and lysosomal degradation by apolipoprotein E isoforms. J.Biol. Chem. 2012, 287:44593-44601.
    • (2012) J.Biol. Chem. , vol.287 , pp. 44593-44601
    • Li, J.1    Kanekiyo, T.2    Shinohara, M.3    Zhang, Y.4    LaDu, M.J.5    Xu, H.6    Bu, G.7
  • 65
    • 78650166808 scopus 로고    scopus 로고
    • Alpha-secretase in Alzheimer's disease: molecular identity, regulation and therapeutic potential
    • Lichtenthaler S.F. Alpha-secretase in Alzheimer's disease: molecular identity, regulation and therapeutic potential. J.Neurochem. 2011, 116:10-21.
    • (2011) J.Neurochem. , vol.116 , pp. 10-21
    • Lichtenthaler, S.F.1
  • 67
    • 0028217645 scopus 로고
    • High affinity nerve growth factor binding displays a faster rate of association than p140trk binding. Implications for multi-subunit polypeptide receptors
    • Mahadeo D., Kaplan L., Chao M.V., Hempstead B.L. High affinity nerve growth factor binding displays a faster rate of association than p140trk binding. Implications for multi-subunit polypeptide receptors. J.Biol. Chem. 1994, 269:6884-6891.
    • (1994) J.Biol. Chem. , vol.269 , pp. 6884-6891
    • Mahadeo, D.1    Kaplan, L.2    Chao, M.V.3    Hempstead, B.L.4
  • 69
    • 24944524929 scopus 로고    scopus 로고
    • Brain cholinergic vulnerability: relevance to behavior and disease
    • McKinney M., Jacksonville M.C. Brain cholinergic vulnerability: relevance to behavior and disease. Biochem. Pharmacol. 2005, 70:1115-1124.
    • (2005) Biochem. Pharmacol. , vol.70 , pp. 1115-1124
    • McKinney, M.1    Jacksonville, M.C.2
  • 70
    • 0842304284 scopus 로고    scopus 로고
    • The cholinergic lesion of Alzheimer's disease: pivotal factor or side show?
    • Mesulam M. The cholinergic lesion of Alzheimer's disease: pivotal factor or side show?. Learn Mem. 2004, 11:43-49.
    • (2004) Learn Mem. , vol.11 , pp. 43-49
    • Mesulam, M.1
  • 71
    • 0344441293 scopus 로고    scopus 로고
    • The cholinergic innervation of the human cerebral cortex
    • Mesulam M.M. The cholinergic innervation of the human cerebral cortex. Prog. Brain Res. 2004, 145:67-78.
    • (2004) Prog. Brain Res. , vol.145 , pp. 67-78
    • Mesulam, M.M.1
  • 72
    • 0023715013 scopus 로고
    • Nucleus basalis (Ch4) and cortical cholinergic innervation in the human brain: observations based on the distribution of acetylcholinesterase and choline acetyltransferase
    • Mesulam M.M., Geula C. Nucleus basalis (Ch4) and cortical cholinergic innervation in the human brain: observations based on the distribution of acetylcholinesterase and choline acetyltransferase. J.Comp. Neurol. 1988, 275:216-240.
    • (1988) J.Comp. Neurol. , vol.275 , pp. 216-240
    • Mesulam, M.M.1    Geula, C.2
  • 75
    • 34548672350 scopus 로고    scopus 로고
    • Cholinotrophic molecular substrates of mild cognitive impairment in the elderly
    • Mufson E.J., Counts S.E., Fahnestock M., Ginsberg S.D. Cholinotrophic molecular substrates of mild cognitive impairment in the elderly. Curr. Alzheimer Res. 2007, 4:340-350.
    • (2007) Curr. Alzheimer Res. , vol.4 , pp. 340-350
    • Mufson, E.J.1    Counts, S.E.2    Fahnestock, M.3    Ginsberg, S.D.4
  • 76
    • 55849111494 scopus 로고    scopus 로고
    • Cholinergic system during the progression of Alzheimer's disease: therapeutic implications
    • Mufson E.J., Counts S.E., Perez S.E., Ginsberg S.D. Cholinergic system during the progression of Alzheimer's disease: therapeutic implications. Expert Rev. Neurother. 2008, 8:1703-1718.
    • (2008) Expert Rev. Neurother. , vol.8 , pp. 1703-1718
    • Mufson, E.J.1    Counts, S.E.2    Perez, S.E.3    Ginsberg, S.D.4
  • 77
    • 0035074341 scopus 로고    scopus 로고
    • The molecular machinery for lysosome biogenesis
    • Mullins C., Bonifacino J.S. The molecular machinery for lysosome biogenesis. Bioessays 2001, 23:333-343.
    • (2001) Bioessays , vol.23 , pp. 333-343
    • Mullins, C.1    Bonifacino, J.S.2
  • 78
    • 0038117796 scopus 로고    scopus 로고
    • Correlation between elevated levels of amyloid beta-peptide in the brain and cognitive decline
    • Naslund J., Haroutunian V., Mohs R., Davis K.L., Davies P., Greengard P., Buxbaum J.D. Correlation between elevated levels of amyloid beta-peptide in the brain and cognitive decline. JAMA 2000, 283:1571-1577.
    • (2000) JAMA , vol.283 , pp. 1571-1577
    • Naslund, J.1    Haroutunian, V.2    Mohs, R.3    Davis, K.L.4    Davies, P.5    Greengard, P.6    Buxbaum, J.D.7
  • 79
    • 0026476297 scopus 로고
    • Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors
    • Nitsch R.M., Slack B.E., Wurtman R.J., Growdon J.H. Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors. Science 1992, 258:304-307.
    • (1992) Science , vol.258 , pp. 304-307
    • Nitsch, R.M.1    Slack, B.E.2    Wurtman, R.J.3    Growdon, J.H.4
  • 80
    • 38349046973 scopus 로고    scopus 로고
    • Autophagy, amyloidogenesis and Alzheimer disease
    • Nixon R.A. Autophagy, amyloidogenesis and Alzheimer disease. J.Cell Sci. 2007, 120:4081-4091.
    • (2007) J.Cell Sci. , vol.120 , pp. 4081-4091
    • Nixon, R.A.1
  • 81
  • 82
    • 48249103491 scopus 로고    scopus 로고
    • Neurodegenerative lysosomal disorders: a continuum from development to late age
    • Nixon R.A., Yang D.S., Lee J.H. Neurodegenerative lysosomal disorders: a continuum from development to late age. Autophagy 2008, 4:590-599.
    • (2008) Autophagy , vol.4 , pp. 590-599
    • Nixon, R.A.1    Yang, D.S.2    Lee, J.H.3
  • 83
    • 4043167747 scopus 로고    scopus 로고
    • Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • Oddo S., Billings L., Kesslak J.P., Cribbs D.H., LaFerla F.M. Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 2004, 43:321-332.
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 84
    • 84863998590 scopus 로고    scopus 로고
    • Intrinsic voltage dynamics govern the diversity of spontaneous firing profiles in basal forebrain noncholinergic neurons
    • Ovsepian S.V., Dolly J.O., Zaborszky L. Intrinsic voltage dynamics govern the diversity of spontaneous firing profiles in basal forebrain noncholinergic neurons. J.Neurophysiol. 2012, 108:406-418.
    • (2012) J.Neurophysiol. , vol.108 , pp. 406-418
    • Ovsepian, S.V.1    Dolly, J.O.2    Zaborszky, L.3
  • 85
    • 85027952447 scopus 로고    scopus 로고
    • The neurotrophin receptor p75 mediates the uptake of the amyloid beta peptide, guiding it to lysosomes for degradation in basal forebrain cholinergic neurons
    • in press.
    • Ovsepian, S.V., Antyborzec, I., O'Leary, V.B., Zaborszky, L., Herms, J., and Dolly, J.O., 2013. The neurotrophin receptor p75 mediates the uptake of the amyloid beta peptide, guiding it to lysosomes for degradation in basal forebrain cholinergic neurons. Brain Structure and Functions, in press.
    • (2013) Brain Structure and Functions
    • Ovsepian, S.V.1    Antyborzec, I.2    O'Leary, V.B.3    Zaborszky, L.4    Herms, J.5    Dolly, J.O.6
  • 86
    • 0037698096 scopus 로고    scopus 로고
    • Presenilin-1, nicastrin, amyloid precursor protein, and gamma-secretase activity are co-localized in the lysosomal membrane
    • Pasternak S.H., Bagshaw R.D., Guiral M., Zhang S., Ackerley C.A., Pak B.J., Callahan J.W., Mahuran D.J. Presenilin-1, nicastrin, amyloid precursor protein, and gamma-secretase activity are co-localized in the lysosomal membrane. J.Biol. Chem. 2003, 278:26687-26694.
    • (2003) J.Biol. Chem. , vol.278 , pp. 26687-26694
    • Pasternak, S.H.1    Bagshaw, R.D.2    Guiral, M.3    Zhang, S.4    Ackerley, C.A.5    Pak, B.J.6    Callahan, J.W.7    Mahuran, D.J.8
  • 88
    • 0036239115 scopus 로고    scopus 로고
    • Endocytosis via caveolae
    • Pelkmans L., Helenius A. Endocytosis via caveolae. Traffic 2002, 3:311-320.
    • (2002) Traffic , vol.3 , pp. 311-320
    • Pelkmans, L.1    Helenius, A.2
  • 89
    • 0036534870 scopus 로고    scopus 로고
    • Role of p75 neurotrophin receptor in the neurotoxicity by beta-amyloid peptides and synergistic effect of inflammatory cytokines
    • Perini G., Della-Bianca V., Politi V., Della Valle G., Dal-Pra I., Rossi F., Armato U. Role of p75 neurotrophin receptor in the neurotoxicity by beta-amyloid peptides and synergistic effect of inflammatory cytokines. J.Exp. Med. 2002, 195:907-918.
    • (2002) J.Exp. Med. , vol.195 , pp. 907-918
    • Perini, G.1    Della-Bianca, V.2    Politi, V.3    Della Valle, G.4    Dal-Pra, I.5    Rossi, F.6    Armato, U.7
  • 92
    • 28644437291 scopus 로고    scopus 로고
    • The amyloid-beta precursor protein: integrating structure with biological function
    • Reinhard C., Hebert S.S., De Strooper B. The amyloid-beta precursor protein: integrating structure with biological function. EMBO J. 2005, 24:3996-4006.
    • (2005) EMBO J. , vol.24 , pp. 3996-4006
    • Reinhard, C.1    Hebert, S.S.2    De Strooper, B.3
  • 93
    • 0028832215 scopus 로고
    • Structural and immunocytochemical features of olivopontocerebellar atrophy caused by the spinocerebellar ataxia type 1 (SCA-1) mutation define a unique phenotype
    • Robitaille Y., Schut L., Kish S.J. Structural and immunocytochemical features of olivopontocerebellar atrophy caused by the spinocerebellar ataxia type 1 (SCA-1) mutation define a unique phenotype. Acta Neuropathol. 1995, 90:572-581.
    • (1995) Acta Neuropathol. , vol.90 , pp. 572-581
    • Robitaille, Y.1    Schut, L.2    Kish, S.J.3
  • 95
    • 0036523031 scopus 로고    scopus 로고
    • Inhibition of intracellular cholesterol transport alters presenilin localization and amyloid precursor protein processing in neuronal cells
    • Runz H., Rietdorf J., Tomic I., de Bernard M., Beyreuther K., Pepperkok R., Hartmann T. Inhibition of intracellular cholesterol transport alters presenilin localization and amyloid precursor protein processing in neuronal cells. J.Neurosci. 2002, 22:1679-1689.
    • (2002) J.Neurosci. , vol.22 , pp. 1679-1689
    • Runz, H.1    Rietdorf, J.2    Tomic, I.3    de Bernard, M.4    Beyreuther, K.5    Pepperkok, R.6    Hartmann, T.7
  • 96
    • 33745902844 scopus 로고    scopus 로고
    • Molecular mechanisms of late endosome morphology, identity and sorting
    • Russell M.R., Nickerson D.P., Odorizzi G. Molecular mechanisms of late endosome morphology, identity and sorting. Curr. Opin. Cell Biol. 2006, 18:422-428.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 422-428
    • Russell, M.R.1    Nickerson, D.P.2    Odorizzi, G.3
  • 97
    • 37249062072 scopus 로고    scopus 로고
    • Internalization of beta-amyloid peptide by primary neurons in the absence of apolipoprotein E
    • Saavedra L., Mohamed A., Ma V., Kar S., de Chaves E.P. Internalization of beta-amyloid peptide by primary neurons in the absence of apolipoprotein E. J.Biol .Chem. 2007, 282:35722-35732.
    • (2007) J.Biol .Chem. , vol.282 , pp. 35722-35732
    • Saavedra, L.1    Mohamed, A.2    Ma, V.3    Kar, S.4    de Chaves, E.P.5
  • 98
    • 0034054499 scopus 로고    scopus 로고
    • P75 neurotrophin receptor in the nucleus basalis of meynert in relation to age, sex, and Alzheimer's disease
    • Salehi A., Ocampo M., Verhaagen J., Swaab D.F. P75 neurotrophin receptor in the nucleus basalis of meynert in relation to age, sex, and Alzheimer's disease. Exp. Neurol. 2000, 161:245-258.
    • (2000) Exp. Neurol. , vol.161 , pp. 245-258
    • Salehi, A.1    Ocampo, M.2    Verhaagen, J.3    Swaab, D.F.4
  • 99
    • 26244437738 scopus 로고    scopus 로고
    • Basal forebrain cholinergic dysfunction in Alzheimer's disease-interrelationship with beta-amyloid, inflammation and neurotrophin signaling
    • Schliebs R. Basal forebrain cholinergic dysfunction in Alzheimer's disease-interrelationship with beta-amyloid, inflammation and neurotrophin signaling. Neurochem. Res. 2005, 30:895-908.
    • (2005) Neurochem. Res. , vol.30 , pp. 895-908
    • Schliebs, R.1
  • 100
    • 79955727727 scopus 로고    scopus 로고
    • The cholinergic system in aging and neuronal degeneration
    • Schliebs R., Arendt T. The cholinergic system in aging and neuronal degeneration. Behav. Brain Res. 2011, 221:555-563.
    • (2011) Behav. Brain Res. , vol.221 , pp. 555-563
    • Schliebs, R.1    Arendt, T.2
  • 102
    • 0031127975 scopus 로고    scopus 로고
    • Cholinergic synapses in human cerebral cortex: an ultrastructural study in serial sections
    • Smiley J.F., Morrell F., Mesulam M.M. Cholinergic synapses in human cerebral cortex: an ultrastructural study in serial sections. Exp. Neurol. 1997, 144:361-368.
    • (1997) Exp. Neurol. , vol.144 , pp. 361-368
    • Smiley, J.F.1    Morrell, F.2    Mesulam, M.M.3
  • 106
    • 0014193263 scopus 로고
    • Fine structural localization of acid phosphatase in senile plaques in Alzheimer's presenile dementia
    • Suzuki K., Terry R.D. Fine structural localization of acid phosphatase in senile plaques in Alzheimer's presenile dementia. Acta Neuropathol. 1967, 8:276-284.
    • (1967) Acta Neuropathol. , vol.8 , pp. 276-284
    • Suzuki, K.1    Terry, R.D.2
  • 107
    • 1842732209 scopus 로고    scopus 로고
    • Oligomerization of Alzheimer's beta-amyloid within processes and synapses of cultured neurons and brain
    • Takahashi R.H., Almeida C.G., Kearney P.F., Yu F., Lin M.T., Milner T.A., Gouras G.K. Oligomerization of Alzheimer's beta-amyloid within processes and synapses of cultured neurons and brain. J.Neurosci. 2004, 24:3592-3599.
    • (2004) J.Neurosci. , vol.24 , pp. 3592-3599
    • Takahashi, R.H.1    Almeida, C.G.2    Kearney, P.F.3    Yu, F.4    Lin, M.T.5    Milner, T.A.6    Gouras, G.K.7
  • 109
    • 0036165129 scopus 로고    scopus 로고
    • Alzheimer beta-amyloid peptides: normal and abnormal localization
    • Takahashi R.H., Nam E.E., Edgar M., Gouras G.K. Alzheimer beta-amyloid peptides: normal and abnormal localization. Histol. Histopathol. 2002, 17:239-246.
    • (2002) Histol. Histopathol. , vol.17 , pp. 239-246
    • Takahashi, R.H.1    Nam, E.E.2    Edgar, M.3    Gouras, G.K.4
  • 111
    • 0037172826 scopus 로고    scopus 로고
    • Phases of A beta-deposition in the human brain and its relevance for the development of AD
    • Thal D.R., Rub U., Orantes M., Braak H. Phases of A beta-deposition in the human brain and its relevance for the development of AD. Neurology 2002, 58:1791-1800.
    • (2002) Neurology , vol.58 , pp. 1791-1800
    • Thal, D.R.1    Rub, U.2    Orantes, M.3    Braak, H.4
  • 112
    • 57649221135 scopus 로고    scopus 로고
    • Amyloid precursor protein trafficking, processing, and function
    • Thinakaran G., Koo E.H. Amyloid precursor protein trafficking, processing, and function. J.Biol. Chem. 2008, 283:29615-29619.
    • (2008) J.Biol. Chem. , vol.283 , pp. 29615-29619
    • Thinakaran, G.1    Koo, E.H.2
  • 113
    • 0347479327 scopus 로고    scopus 로고
    • Nerve growth factor: from animal models of cholinergic neuronal degeneration to gene therapy in Alzheimer's disease
    • Tuszynski M.H., Blesch A. Nerve growth factor: from animal models of cholinergic neuronal degeneration to gene therapy in Alzheimer's disease. Prog. Brain Res. 2004, 146:441-449.
    • (2004) Prog. Brain Res. , vol.146 , pp. 441-449
    • Tuszynski, M.H.1    Blesch, A.2
  • 115
    • 0036848549 scopus 로고    scopus 로고
    • Increased extracellular amyloid deposition and neurodegeneration in human amyloid precursor protein transgenic mice deficient in receptor-associated protein
    • Van Uden E., Mallory M., Veinbergs I., Alford M., Rockenstein E., Masliah E. Increased extracellular amyloid deposition and neurodegeneration in human amyloid precursor protein transgenic mice deficient in receptor-associated protein. J.Neurosci. 2002, 22:9298-9304.
    • (2002) J.Neurosci. , vol.22 , pp. 9298-9304
    • Van Uden, E.1    Mallory, M.2    Veinbergs, I.3    Alford, M.4    Rockenstein, E.5    Masliah, E.6
  • 116
    • 0034006944 scopus 로고    scopus 로고
    • Beta-amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology
    • Wang H.Y., Lee D.H., D'Andrea M.R., Peterson P.A., Shank R.P., Reitz A.B. Beta-amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology. J.Biol. Chem. 2000, 275:5626-5632.
    • (2000) J.Biol. Chem. , vol.275 , pp. 5626-5632
    • Wang, H.Y.1    Lee, D.H.2    D'Andrea, M.R.3    Peterson, P.A.4    Shank, R.P.5    Reitz, A.B.6
  • 118
    • 33748753481 scopus 로고    scopus 로고
    • Clearance of amyloid-beta in Alzheimer's disease: progress, problems and perspectives
    • Wang Y.J., Zhou H.D., Zhou X.F. Clearance of amyloid-beta in Alzheimer's disease: progress, problems and perspectives. Drug Discov. Today 2006, 11:931-938.
    • (2006) Drug Discov. Today , vol.11 , pp. 931-938
    • Wang, Y.J.1    Zhou, H.D.2    Zhou, X.F.3
  • 119
    • 0842290742 scopus 로고    scopus 로고
    • What is the importance of multivesicular bodies in retrograde axonal transport invivo?
    • Weible M.W., Hendry I.A. What is the importance of multivesicular bodies in retrograde axonal transport invivo?. J.Neurobiol. 2004, 58:230-243.
    • (2004) J.Neurobiol. , vol.58 , pp. 230-243
    • Weible, M.W.1    Hendry, I.A.2
  • 120
    • 0024576043 scopus 로고
    • The pontomesencephalotegmental cholinergic system does not degenerate in Alzheimer's disease
    • Woolf N.J., Jacobs R.W., Butcher L.L. The pontomesencephalotegmental cholinergic system does not degenerate in Alzheimer's disease. Neurosci. Lett. 1989, 96:277-282.
    • (1989) Neurosci. Lett. , vol.96 , pp. 277-282
    • Woolf, N.J.1    Jacobs, R.W.2    Butcher, L.L.3
  • 121
    • 0037040889 scopus 로고    scopus 로고
    • Amyloid beta binds trimers as well as monomers of the 75-kDa neurotrophin receptor and activates receptor signaling
    • Yaar M., Zhai S., Fine R.E., Eisenhauer P.B., Arble B.L., Stewart K.B., Gilchrest B.A. Amyloid beta binds trimers as well as monomers of the 75-kDa neurotrophin receptor and activates receptor signaling. J.Biol. Chem. 2002, 277:7720-7725.
    • (2002) J.Biol. Chem. , vol.277 , pp. 7720-7725
    • Yaar, M.1    Zhai, S.2    Fine, R.E.3    Eisenhauer, P.B.4    Arble, B.L.5    Stewart, K.B.6    Gilchrest, B.A.7
  • 122
    • 0030723983 scopus 로고    scopus 로고
    • Binding of beta-amyloid to the p75 neurotrophin receptor induces apoptosis. A possible mechanism for Alzheimer's disease
    • Yaar M., Zhai S., Pilch P.F., Doyle S.M., Eisenhauer P.B., Fine R.E., Gilchrest B.A. Binding of beta-amyloid to the p75 neurotrophin receptor induces apoptosis. A possible mechanism for Alzheimer's disease. J.Clin. Invest. 1997, 100:2333-2340.
    • (1997) J.Clin. Invest. , vol.100 , pp. 2333-2340
    • Yaar, M.1    Zhai, S.2    Pilch, P.F.3    Doyle, S.M.4    Eisenhauer, P.B.5    Fine, R.E.6    Gilchrest, B.A.7
  • 123
    • 22144444924 scopus 로고    scopus 로고
    • Alzheimer's disease: interactions between cholinergic functions and beta-amyloid
    • Yan Z., Feng J. Alzheimer's disease: interactions between cholinergic functions and beta-amyloid. Curr. Alzheimer Res. 2004, 1:241-248.
    • (2004) Curr. Alzheimer Res. , vol.1 , pp. 241-248
    • Yan, Z.1    Feng, J.2
  • 124
    • 0037337815 scopus 로고    scopus 로고
    • Neuronal loss is greater in the locus coeruleus than nucleus basalis and substantia nigra in Alzheimer and Parkinson diseases
    • Zarow C., Lyness S.A., Mortimer J.A., Chui H.C. Neuronal loss is greater in the locus coeruleus than nucleus basalis and substantia nigra in Alzheimer and Parkinson diseases. Arch. Neurol. 2003, 60:337-341.
    • (2003) Arch. Neurol. , vol.60 , pp. 337-341
    • Zarow, C.1    Lyness, S.A.2    Mortimer, J.A.3    Chui, H.C.4


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