메뉴 건너뛰기




Volumn 116, Issue 5, 2011, Pages 742-746

Membrane targeting, shedding and protein interactions of brain acetylcholinesterase

Author keywords

acetylcholinesterase; Alzheimer disease; amyloid; lipid rafts; PRiMA; secretase; shedding

Indexed keywords

ACETYLCHOLINESTERASE; AMYLOID PRECURSOR PROTEIN; BUNGAROTOXIN RECEPTOR; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN;

EID: 79851507143     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2010.07032.x     Document Type: Article
Times cited : (34)

References (36)
  • 2
    • 0026447003 scopus 로고
    • Secreted acetylcholinesterase: Non-classical aspects of a classical enzyme
    • Appleyard M. E., (1992) Secreted acetylcholinesterase: non-classical aspects of a classical enzyme. Trends Neurosci. 15, 485-490.
    • (1992) Trends Neurosci. , vol.15 , pp. 485-490
    • Appleyard, M.E.1
  • 3
    • 0023608683 scopus 로고
    • Spontaneous and carbachol-evoked in vivo secretion of acetylcholinesterase from the hippocampus of the rat
    • DOI 10.1016/0197-0186(87)90029-5
    • Appleyard M. E., and, Smith A. D., (1987) Spontaneous and carbachol-evoked in vivo secretion of acetylcholinesterase from the hippocampus of the rat. Neurochem. Int. 11, 397-406. (Pubitemid 18017274)
    • (1987) Neurochemistry International , vol.11 , Issue.4 , pp. 397-406
    • Appleyard, M.E.1    Smith, A.D.2
  • 4
    • 58049089518 scopus 로고    scopus 로고
    • Neprilysin gene expression requires binding of the amyloid precursor protein intracellular domain to its promoter: Implications for Alzheimer disease
    • Belyaev N. D., Nalivaeva N. N., Makova N. Z., and, Turner A. J., (2009) Neprilysin gene expression requires binding of the amyloid precursor protein intracellular domain to its promoter: implications for Alzheimer disease. EMBO Rep. 10, 94-100.
    • (2009) EMBO Rep. , vol.10 , pp. 94-100
    • Belyaev, N.D.1    Nalivaeva, N.N.2    Makova, N.Z.3    Turner, A.J.4
  • 6
    • 33645299023 scopus 로고    scopus 로고
    • The involvement of lipid rafts in Alzheimer's disease
    • Cordy J. M., Hooper N. M., and, Turner A. J., (2006) The involvement of lipid rafts in Alzheimer's disease. Mol. Membr. Biol. 23, 111-122.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 111-122
    • Cordy, J.M.1    Hooper, N.M.2    Turner, A.J.3
  • 7
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts
    • DOI 10.1083/jcb.200207113
    • Ehehalt R., Keller P., Haass C., Thiele C., and, Simons K., (2003) Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts. J. Cell Biol. 160, 113-123. (Pubitemid 36091721)
    • (2003) Journal of Cell Biology , vol.160 , Issue.1 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 8
    • 0024417125 scopus 로고
    • Special properties of cholinesterases in the cerebral cortex of Alzheimer's disease
    • DOI 10.1016/0006-8993(89)90419-8
    • Geula C., and, Mesulam M., (1989) Special properties of cholinesterases in the cerebral cortex of Alzheimer's disease. Brain Res. 498, 185-189. (Pubitemid 19228181)
    • (1989) Brain Research , vol.498 , Issue.1 , pp. 185-189
    • Geula, C.1    Mesulam, M.2
  • 10
    • 38549159882 scopus 로고    scopus 로고
    • Non-hydrolytic functions of acetylcholinesterase: The significance of C-terminal peptides
    • DOI 10.1111/j.1742-4658.2007.06235.x
    • Greenfield S. A., Zimmermann M., and, Bond C. E., (2008) Non-hydrolytic functions of acetylcholinesterase. The significance of C-terminal peptides. FEBS J. 275, 604-611. (Pubitemid 351160966)
    • (2008) FEBS Journal , vol.275 , Issue.4 , pp. 604-611
    • Greenfield, S.A.1    Zimmermann, M.2    Bond, C.E.3
  • 11
    • 0033568704 scopus 로고    scopus 로고
    • Structural roles of acetylcholinesterase variants in biology and pathology
    • DOI 10.1046/j.1432-1327.1999.00693.x
    • Grisaru D., Sternfeld M., Eldor A., Glick D., and, Soreq H., (1999) Structural roles of acetylcholinesterase variants in biology and pathology. Eur. J. Biochem. 264, 672-686. (Pubitemid 29437196)
    • (1999) European Journal of Biochemistry , vol.264 , Issue.3 , pp. 672-686
    • Grisaru, D.1    Sternfeld, M.2    Eldor, A.3    Glick, D.4    Soreq, H.5
  • 12
    • 0019495297 scopus 로고
    • A projection from acetylcholinesterase-containing neurones in the diagonal band to the occipital cortex of the rat
    • DOI 10.1016/0306-4522(81)90072-5
    • Henderson Z., (1981) A projection from acetylcholinesterase-containing neurones in the diagonal band to the occipital cortex of the rat. Neuroscience 6, 1081-1088. (Pubitemid 11064212)
    • (1981) Neuroscience , vol.6 , Issue.6 , pp. 1081-1088
    • Henderson, Z.1
  • 13
    • 0024493994 scopus 로고
    • Acetylcholinesterase on the dendrites of central cholinergic neurons: An electronmicroscopical study in the ferret
    • DOI 10.1016/0306-4522(89)90235-2
    • Henderson Z., (1989) Acetylcholinesterase on the dendrites of central cholinergic neurons: an electron microscopical study in the ferret. Neuroscience 28, 95-108. (Pubitemid 19026746)
    • (1989) Neuroscience , vol.28 , Issue.1 , pp. 95-108
    • Henderson, Z.1
  • 14
    • 13444292473 scopus 로고    scopus 로고
    • Somato-dendritic nicotinic receptor responses recorded in vitro from the medial septal diagonal band complex of the rodent
    • DOI 10.1113/jphysiol.2004.070300
    • Henderson Z., Boros A., Janzso G., Westwood A. J., Monyer H., and, Halasy K., (2005) Somato-dendritic nicotinic receptor responses recorded in vitro from the medial septal diagonal band complex of the rodent. J. Physiol. 562, 165-182. (Pubitemid 40207794)
    • (2005) Journal of Physiology , vol.562 , Issue.1 , pp. 165-182
    • Henderson, Z.1    Boros, A.2    Janzso, G.3    Westwood, A.J.4    Monyer, H.5    Halasy, K.6
  • 15
    • 77953916706 scopus 로고    scopus 로고
    • Co-localization of PRiMA with acetylcholinesterase in cholinergic neurons of rat brain: An immunocytochemical study
    • Henderson Z., Matto N., John D., Nalivaeva N. N., and, Turner A. J., (2010) Co-localization of PRiMA with acetylcholinesterase in cholinergic neurons of rat brain: an immunocytochemical study. Brain Res. 1344, 34-42.
    • (2010) Brain Res. , vol.1344 , pp. 34-42
    • Henderson, Z.1    Matto, N.2    John, D.3    Nalivaeva, N.N.4    Turner, A.J.5
  • 16
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme
    • DOI 10.1016/S0896-6273(00)80108-7
    • Inestrosa N. C., Alvarez A., Pérez C. A., Moreno R. D., Vicente M., Linker C., Casanueva O. I., Soto C., and, Garrido J., (1996) Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron 16, 881-891. (Pubitemid 26124065)
    • (1996) Neuron , vol.16 , Issue.4 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Perez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6    Casanueva, O.I.7    Soto, C.8    Garrido, J.9
  • 17
    • 77955510036 scopus 로고    scopus 로고
    • Acetylcholine as a possible signaling molecule in embryonic stem cells: Studies on survival, proliferation and death
    • Landgraf D., Barth M., Layer P. G., and, Sperling L. E., (2010) Acetylcholine as a possible signaling molecule in embryonic stem cells: studies on survival, proliferation and death. Chem. Biol. Interact. 187, 115-119.
    • (2010) Chem. Biol. Interact. , vol.187 , pp. 115-119
    • Landgraf, D.1    Barth, M.2    Layer, P.G.3    Sperling, L.E.4
  • 19
    • 0027257971 scopus 로고
    • Cholinergic enzymes in spinal cord infarction: Biochemical and histochemical changes
    • Malatová Z., and, Marsala J., (1993) Cholinergic enzymes in spinal cord infarction. Biochemical and histochemical changes. Mol. Chem. Neuropathol. 19, 283-296. (Pubitemid 23241851)
    • (1993) Molecular and Chemical Neuropathology , vol.19 , Issue.3 , pp. 283-296
    • Malatova, Z.1    Marsala, J.2
  • 20
    • 28744432658 scopus 로고    scopus 로고
    • The C-terminal peptides of acetylcholinesterase: Cellular trafficking, oligomerization and functional anchoring
    • DOI 10.1016/j.cbi.2005.10.002, PII S0009279705002425
    • Massoulié J., Bon S., Perrier N., and, Falasca C., (2005) The C-terminal peptides of acetylcholinesterase: cellular trafficking, oligomerization and functional anchoring. Chem. Biol. Interact. 157-158, 3-14. (Pubitemid 41757627)
    • (2005) Chemico-Biological Interactions , vol.157-158 , pp. 3-14
    • Massoulie, J.1    Bon, S.2    Perrier, N.3    Falasca, C.4
  • 21
    • 77954956652 scopus 로고    scopus 로고
    • The levels of both lipid rafts and raft-located acetylcholinesterase dimers increase in muscle of mice with muscular dystrophy by merosin deficiency
    • Moral-Naranjo M. T., Montenegro M. F., Muñoz-Delgado E., Campoy F. J., and, Vidal C. J., (2010) The levels of both lipid rafts and raft-located acetylcholinesterase dimers increase in muscle of mice with muscular dystrophy by merosin deficiency. Biochim. Biophys. Acta 1802, 754-764.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 754-764
    • Moral-Naranjo, M.T.1    Montenegro, M.F.2    Muñoz-Delgado, E.3    Campoy, F.J.4    Vidal, C.J.5
  • 22
    • 0032860873 scopus 로고    scopus 로고
    • Does acetylcholinesterase secretion involve an ADAMs-like metallosecretase?
    • Nalivaeva N. N., and, Turner A. J., (1999) Does acetylcholinesterase secretion involve an ADAMs-like metallosecretase? Lett. Peptide Sci. 6, 343-348. (Pubitemid 29462952)
    • (1999) Letters in Peptide Science , vol.6 , Issue.5-6 , pp. 343-348
    • Nalivaeva, N.N.1    Turner, A.J.2
  • 23
    • 0034005582 scopus 로고    scopus 로고
    • Hydrophobic protein that copurifies with human brain acetylcholinesterase: Amino acid sequence, genomic organization, and chromosomal localization
    • DOI 10.1046/j.1471-4159.2000.0742146.x
    • Navaratnam D. S., Fernando F. S., Priddle J. D., Giles K., Clegg S. M., Pappin D. J., Craig I., and, Smith A. D., (2000) Hydrophobic protein that copurifies with human brain acetylcholinesterase: amino acid sequence, genomic organization, and chromosomal localization. J. Neurochem. 74, 2146-2153. (Pubitemid 30217672)
    • (2000) Journal of Neurochemistry , vol.74 , Issue.5 , pp. 2146-2153
    • Navaratnam, D.S.1    Fernando, F.S.2    Priddle, J.D.3    Giles, K.4    Clegg, S.M.5    Pappin, D.J.6    Craig, I.7    Smith, A.D.8
  • 24
    • 0035196471 scopus 로고    scopus 로고
    • Reversible and irreversible acetylcholinesterase inhibitors cause changes in neuronal amyloid precursor protein processing and protein kinase C level in vitro
    • Pakaski M., Rakonczay Z., and, Kasa P., (2001) Reversible and irreversible acetylcholinesterase inhibitors cause changes in neuronal amyloid precursor protein processing and protein kinase C level in vitro. Neurochem. Int. 38, 219-226.
    • (2001) Neurochem. Int. , vol.38 , pp. 219-226
    • Pakaski, M.1    Rakonczay, Z.2    Kasa, P.3
  • 25
    • 0037122918 scopus 로고    scopus 로고
    • PRiMA: The membrane anchor of acetylcholinesterase in the brain
    • DOI 10.1016/S0896-6273(01)00584-0
    • Perrier A. L., Massoulié J., and, Krejci E., (2002) PRiMA: the membrane anchor of acetylcholinesterase in the brain. Neuron 33, 275-285. (Pubitemid 34127759)
    • (2002) Neuron , vol.33 , Issue.2 , pp. 275-285
    • Perrier, A.L.1    Massoulie, J.2    Krejci, E.3
  • 27
    • 0344542055 scopus 로고    scopus 로고
    • Motor neurone acetylcholinesterase release precedes neurotoxicity caused by systemic administration of excitatory amino acids and strychnine
    • DOI 10.1016/S0022-510X(98)00204-4, PII S0022510X98002044
    • Rodríguez-Ithurralde D., Maruri A., and, Rodríguez X., (1998) Motor neurone acetylcholinesterase release precedes neurotoxicity caused by systemic administration of excitatory amino acids and strychnine. J. Neurol. Sci. 160 (Suppl. 1), S80-S86. (Pubitemid 28522524)
    • (1998) Journal of the Neurological Sciences , vol.160 , Issue.SUPPL. 1
    • Rodriguez-Ithurralde, D.1    Maruri, A.2    Rodriguez, X.3
  • 28
    • 57349173045 scopus 로고    scopus 로고
    • Nicotine relieves anxiogenic-like behavior in mice that overexpress the read-through variant of acetylcholinesterase but not in wild-type mice
    • Salas R., Main A., Gangitano D. A., Zimmerman G., Ben-Ari S., Soreq H., and, De Biasi M., (2008) Nicotine relieves anxiogenic-like behavior in mice that overexpress the read-through variant of acetylcholinesterase but not in wild-type mice. Mol. Pharmacol. 74, 1641-1648.
    • (2008) Mol. Pharmacol. , vol.74 , pp. 1641-1648
    • Salas, R.1    Main, A.2    Gangitano, D.A.3    Zimmerman, G.4    Ben-Ari, S.5    Soreq, H.6    De Biasi, M.7
  • 29
    • 33750445930 scopus 로고    scopus 로고
    • The significance of the cholinergic system in the brain during aging and in Alzheimer's disease
    • DOI 10.1007/s00702-006-0579-2, 100 Years of Alzheimer's Disease
    • Schliebs R., and, Arendt T., (2006) The significance of the cholinergic system in the brain during aging and in Alzheimer's disease. J. Neural Transm. 113, 1625-1644. (Pubitemid 44657659)
    • (2006) Journal of Neural Transmission , vol.113 , Issue.11 , pp. 1625-1644
    • Schliebs, R.1    Arendt, T.2
  • 30
    • 0027491242 scopus 로고
    • Regulated and constitutive secretion of distinct molecular forms of acetylcholinesterase from PC12 cells
    • Schweitzer E. S., (1993) Regulated and constitutive secretion of distinct molecular forms of acetylcholinesterase from PC12 cells. J. Cell Sci. 106, 731-740. (Pubitemid 23346786)
    • (1993) Journal of Cell Science , vol.106 , Issue.3 , pp. 731-740
    • Schweitzer, E.S.1
  • 31
    • 0029897490 scopus 로고    scopus 로고
    • Non-classical actions of cholinesterases: Role in cellular differentiation, tumorigenesis and Alzheimer's disease
    • DOI 10.1016/0197-0186(95)00099-2
    • Small D. H., Michaelson S., and, Sberna G., (1996) Non-classical actions of cholinesterases: role in cellular differentiation, tumorigenesis and Alzheimer's disease. Neurochem. Int. 28, 453-483. (Pubitemid 26161318)
    • (1996) Neurochemistry International , vol.28 , Issue.5-6 , pp. 453-483
    • Small, D.H.1    Michaelson, S.2    Sberna, G.3
  • 33
    • 77953280950 scopus 로고    scopus 로고
    • Membrane rafts in Alzheimer's disease β-amyloid production
    • Vetrivel K. S., and, Thinakaran G., (2010) Membrane rafts in Alzheimer's disease β-amyloid production. Biochim. Biophys. Acta 1801, 860-867.
    • (2010) Biochim. Biophys. Acta , vol.1801 , pp. 860-867
    • Vetrivel, K.S.1    Thinakaran, G.2
  • 34
    • 0033624509 scopus 로고    scopus 로고
    • 1-42 binds selectively and with picomolar affinity to α7 nicotinic acetylcholine receptors
    • DOI 10.1046/j.1471-4159.2000.0751155.x
    • Wang H. Y., Lee D. H., Davis C. B., and, Shank R. P., (2000) Amyloid peptide Aβ(1-42) binds selectively and with picomolar affinity to α7 nicotinic acetylcholine receptors. J. Neurochem. 75, 1155-1161. (Pubitemid 30660505)
    • (2000) Journal of Neurochemistry , vol.75 , Issue.3 , pp. 1155-1161
    • Wang, H.-Y.1    Lee, D.H.S.2    Davis, C.B.3    Shank, R.P.4
  • 35
    • 62949143141 scopus 로고    scopus 로고
    • Transcriptional regulation of proline-rich membrane anchor (PRiMA) of globular form acetylcholinesterase in neuron: An inductive effect of neuron differentiation
    • Xie H. Q., Choi R. C., Leung K. W., Chen V. P., Chu G. K., and, Tsim K. W., (2009) Transcriptional regulation of proline-rich membrane anchor (PRiMA) of globular form acetylcholinesterase in neuron: an inductive effect of neuron differentiation. Brain Res. 1265, 13-23.
    • (2009) Brain Res. , vol.1265 , pp. 13-23
    • Xie, H.Q.1    Choi, R.C.2    Leung, K.W.3    Chen, V.P.4    Chu, G.K.5    Tsim, K.W.6
  • 36
    • 77951234310 scopus 로고    scopus 로고
    • Targeting acetylcholinesterase to membrane rafts: A function mediated by the proline-rich membrane anchor (PRiMA) in neurons
    • Xie H. Q., Liang D., Leung K. W., Chen V. P., Zhu K. Y., Chan W. K., Choi R. C., Massoulié J., and, Tsim K. W., (2010) Targeting acetylcholinesterase to membrane rafts: a function mediated by the proline-rich membrane anchor (PRiMA) in neurons. J. Biol. Chem. 285, 11537-11546.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11537-11546
    • Xie, H.Q.1    Liang, D.2    Leung, K.W.3    Chen, V.P.4    Zhu, K.Y.5    Chan, W.K.6    Choi, R.C.7    Massoulié, J.8    Tsim, K.W.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.