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Volumn 11, Issue 6, 2014, Pages 608-622

Selective acetyl- and butyrylcholinesterase inhibitors reduce amyloid-β ex vivo activation of peripheral chemo-cytokines from Alzheimer's disease subjects: Exploring the cholinergic anti-inflammatory pathway

Author keywords

Acetylcholinesterase (AChE); Alzheimer's disease; Amyloid peptide (A ); Butyrylcholinesterase (BuChE); Cholinesterase inhibitors; Cytokines; IL 10; IL 1 ; IL 6; Inflammation; MCP 1; Phenserine, cymserine, bisnorcymserine, phytohaemagglutinin (PHA) THP 1 cells, peripheral blood mononuclear cells (PBMCs); TNF

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 MORPHOLINO 8 PHENYLCHROMONE; 4 (4 FLUOROPHENYL) 2 (4 HYDROXYPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; ACETYLCHOLINESTERASE; AMYLOID BETA PROTEIN; BISNORCYMSERINE; CHOLINESTERASE; CHOLINESTERASE INHIBITOR; CYMESERINE; CYTOKINE; INTERLEUKIN 10; INTERLEUKIN 1BETA; MONOCYTE CHEMOTACTIC PROTEIN 1; PHENETHYLCYMSERINE; PHENSERINE; PHYTOHEMAGGLUTININ; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; CCL2 PROTEIN, HUMAN; CHEMOKINE; IL10 PROTEIN, HUMAN; IL1B PROTEIN, HUMAN; IL6 PROTEIN, HUMAN; INTERLEUKIN 6; MESSENGER RNA;

EID: 84904754895     PISSN: 15672050     EISSN: 18755828     Source Type: Journal    
DOI: 10.2174/1567205010666131212113218     Document Type: Article
Times cited : (47)

References (113)
  • 1
    • 70350110000 scopus 로고    scopus 로고
    • Epidemiology of Alzheimer's
    • Prince M. Epidemiology of Alzheimer's. Psychiatry 3: 11-13 (2004)
    • (2004) Psychiatry , vol.3 , pp. 11-13
    • Prince, M.1
  • 2
    • 84863542098 scopus 로고    scopus 로고
    • Longitudinal epidemiologic clinicalpathologic studies of aging and Alzheimer's disease
    • Bennett DA, Launer LJ. Longitudinal epidemiologic clinicalpathologic studies of aging and Alzheimer's disease. Curr Alzheimer Res 9(6): 617-20 (2012).
    • (2012) Curr Alzheimer Res , vol.9 , Issue.6 , pp. 617-620
    • Bennett, D.A.1    Launer, L.J.2
  • 3
    • 33645829653 scopus 로고    scopus 로고
    • Has the amyloid cascade hypothesis for Alzheimer's disease been proved?
    • Hardy J. Has the amyloid cascade hypothesis for Alzheimer's disease been proved? Curr Alzheimer Res (1): 71-3 (2006).
    • (2006) Curr Alzheimer Res , Issue.1 , pp. 71-73
    • Hardy, J.1
  • 4
    • 33645846948 scopus 로고    scopus 로고
    • A partial failure of membrane protein turnover may cause Alzheimer's disease: A new hypothesis
    • Sambamurti K, Suram A, Venugopal C, Prakasam A, Zhou Y, Lahiri DK, et al. A partial failure of membrane protein turnover may cause Alzheimer's disease: a new hypothesis. Curr Alzheimer Res 3(1): 81-90 (2006).
    • (2006) Curr Alzheimer Res , vol.3 , Issue.1 , pp. 81-90
    • Sambamurti, K.1    Suram, A.2    Venugopal, C.3    Prakasam, A.4    Zhou, Y.5    Lahiri, D.K.6
  • 6
    • 45249102680 scopus 로고    scopus 로고
    • Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders
    • Rahimi F, Shanmugam A, Bitan G. Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders. Curr Alzheimer Res 5(3): 319-41 (2008).
    • (2008) Curr Alzheimer Res , vol.5 , Issue.3 , pp. 319-341
    • Rahimi, F.1    Shanmugam, A.2    Bitan, G.3
  • 7
    • 34548726106 scopus 로고    scopus 로고
    • TNF-alpha inhibition as a treatment strategy for neurodegenerative disorders: New drug candidates and targets
    • Tweedie D, Sambamurti K, Greig NH. TNF-alpha inhibition as a treatment strategy for neurodegenerative disorders: new drug candidates and targets. Curr Alzheimer Res 4(4): 378-85 (2007).
    • (2007) Curr Alzheimer Res , vol.4 , Issue.4 , pp. 378-385
    • Tweedie, D.1    Sambamurti, K.2    Greig, N.H.3
  • 8
    • 73949103253 scopus 로고    scopus 로고
    • Microglial activation in Alzheimer's disease
    • Schlachetzki JC, Hüll M. Microglial activation in Alzheimer's disease. Curr Alzheimer Res 6(6): 554-63, 2009.
    • (2009) Curr Alzheimer Res , vol.6 , Issue.6 , pp. 554-563
    • Schlachetzki, J.C.1    Hüll, M.2
  • 9
    • 77953179867 scopus 로고    scopus 로고
    • Neuroinflammation and tumor necrosis factor signaling in the pathophysiology of Alzheimer's disease
    • McAlpine FE, Tansey MG. Neuroinflammation and tumor necrosis factor signaling in the pathophysiology of Alzheimer's disease. J Inflamm Res 1:29-39 (2008).
    • (2008) J Inflamm Res , vol.1 , pp. 29-39
    • McAlpine, F.E.1    Tansey, M.G.2
  • 10
    • 84875655895 scopus 로고    scopus 로고
    • Inflammation in Alzheimer disease-a brief review of the basic science and clinical literature
    • Wyss-Coray T, Rogers J. Inflammation in Alzheimer disease-a brief review of the basic science and clinical literature. Cold Spring Harb Perspect Med 2(1): a006346 (2012).
    • (2012) Cold Spring Harb Perspect Med , vol.2 , Issue.1
    • Wyss-Coray, T.1    Rogers, J.2
  • 11
    • 79954486783 scopus 로고    scopus 로고
    • Does a pro-inflammatory process precede Alzheimer's disease and mild cognitive impairment?
    • Ferretti MT, Cuello AC. Does a pro-inflammatory process precede Alzheimer's disease and mild cognitive impairment? Curr Alzheimer Res 8(2): 164-74 (2011).
    • (2011) Curr Alzheimer Res , vol.8 , Issue.2 , pp. 164-174
    • Ferretti, M.T.1    Cuello, A.C.2
  • 12
    • 70349570588 scopus 로고    scopus 로고
    • Systemic inflammation and disease progression in Alzheimer disease
    • Holmes C, Cunningham C, Zotova E, Woolford J, Dean C, Kerr S, et al. Systemic inflammation and disease progression in Alzheimer disease. Neurology 73(10):768-74 (2009).
    • (2009) Neurology , vol.73 , Issue.10 , pp. 768-774
    • Holmes, C.1    Cunningham, C.2    Zotova, E.3    Woolford, J.4    Dean, C.5    Kerr, S.6
  • 13
    • 79960887486 scopus 로고    scopus 로고
    • Systemic inflammation and Alzheimer's disease
    • Holmes C, Butchart J. Systemic inflammation and Alzheimer's disease. Biochem Soc Trans 39(4): 898-901 (2011).
    • (2011) Biochem Soc Trans , vol.39 , Issue.4 , pp. 898-901
    • Holmes, C.1    Butchart, J.2
  • 14
    • 84860501544 scopus 로고    scopus 로고
    • Relationship between inflammatory mediators, A β levels and ApoE genotype in Alzheimer disease
    • Reale M, Kamal MA, Velluto L, Gambi D, Di Nicola M, Greig NH. Relationship between inflammatory mediators, A β levels and ApoE genotype in Alzheimer disease. Curr Alzheimer Res 9(4): 447-57 (2012).
    • (2012) Curr Alzheimer Res , vol.9 , Issue.4 , pp. 447-457
    • Reale, M.1    Kamal, M.A.2    Velluto, L.3    Gambi, D.4    Di Nicola, M.5    Greig, N.H.6
  • 15
    • 33748371203 scopus 로고    scopus 로고
    • An internally controlled peripheral biomarker for Alzheimer's disease: Erk1 and Erk2 responses to the inflammatory signal bradykinin
    • Khan TK, Alkon DL. An internally controlled peripheral biomarker for Alzheimer's disease: Erk1 and Erk2 responses to the inflammatory signal bradykinin. Proc Natl Acad Sci USA 103(35): 13203-7 (2006).
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.35 , pp. 13203-13207
    • Khan, T.K.1    Alkon, D.L.2
  • 16
    • 0031985192 scopus 로고    scopus 로고
    • Peripheral markers in testing pathophysiological hypotheses and diagnosing Alzheimer's disease
    • Gasparin L, Racchi M, Binetti G, Trabucchi M, Solerte SB, Alkon D, et al. Peripheral markers in testing pathophysiological hypotheses and diagnosing Alzheimer's disease. FASEB J 12(1): 17-34 (1998).
    • (1998) FASEB J , vol.12 , Issue.1 , pp. 17-34
    • Gasparin, L.1    Racchi, M.2    Binetti, G.3    Trabucchi, M.4    Solerte, S.B.5    Alkon, D.6
  • 17
    • 4043061467 scopus 로고    scopus 로고
    • LRP/amyloid beta-peptide interaction mediates differential brain efflux of Abeta isoforms
    • Deane R, Wu Z, Sagare A, Davis J, Du Yan S, Hamm K, et al. LRP/amyloid beta-peptide interaction mediates differential brain efflux of Abeta isoforms. Neuron 43(3): 333-44 (2004).
    • (2004) Neuron , vol.43 , Issue.3 , pp. 333-344
    • Deane, R.1    Wu, Z.2    Sagare, A.3    Davis, J.4    Du Yan, S.5    Hamm, K.6
  • 18
    • 0034521392 scopus 로고    scopus 로고
    • Clearance of Alzheimer's amyloid-ss(1-40) peptide from brain by LDL receptor-related protein-1 at the blood-brain barrier
    • Shibata M, Yamada S, Kumar SR, Calero M, Bading J, Frangione B, et al. Clearance of Alzheimer's amyloid-ss(1-40) peptide from brain by LDL receptor-related protein-1 at the blood-brain barrier. J Clin Invest 106(12):1489-99 (2000).
    • (2000) J Clin Invest , vol.106 , Issue.12 , pp. 1489-1499
    • Shibata, M.1    Yamada, S.2    Kumar, S.R.3    Calero, M.4    Bading, J.5    Frangione, B.6
  • 19
    • 0037703255 scopus 로고    scopus 로고
    • RAGE mediates amyloid-beta peptide transport across the blood-brain barrier and accumulation in brain
    • Deane R, Du Yan S, Submamaryan RK, LaRue B, Jovanovic S, Hogg E, et al. RAGE mediates amyloid-beta peptide transport across the blood-brain barrier and accumulation in brain. Nat Med 9(7): 907-13 (2003).
    • (2003) Nat Med , vol.9 , Issue.7 , pp. 907-913
    • Deane, R.1    Du Yan, S.2    Submamaryan, R.K.3    LaRue, B.4    Jovanovic, S.5    Hogg, E.6
  • 20
    • 0035902619 scopus 로고    scopus 로고
    • Peripheral anti-A beta antibody alters CNS and plasma A beta clearance and decreases brain A beta burden in a mouse model of Alzheimer's disease
    • DeMattos RB, Bales KR, Cummins DJ, Dodart JC, Paul SM, Holtzman DM. Peripheral anti-A beta antibody alters CNS and plasma A beta clearance and decreases brain A beta burden in a mouse model of Alzheimer's disease. Proc Natl Acad Sci USA 98(15): 8850-5 (2001).
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.15 , pp. 8850-8855
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Dodart, J.C.4    Paul, S.M.5    Holtzman, D.M.6
  • 21
    • 0030891163 scopus 로고    scopus 로고
    • Hematopoietic cells differentiate into both microglia and macroglia in the brains of adult mice
    • Eglitis MA, Mezey E. Hematopoietic cells differentiate into both microglia and macroglia in the brains of adult mice. Proc Natl Acad Sci USA 94(8): 4080-5 (1997).
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.8 , pp. 4080-4085
    • Eglitis, M.A.1    Mezey, E.2
  • 22
    • 0037883685 scopus 로고    scopus 로고
    • Amyloid peptide-induced cytokine and chemokine expression in THP-1 monocytes is blocked by small inhibitory RNA duplexes for early growth response-1 messenger RNA
    • Giri RK, Selvaraj SK, Kalra VK. Amyloid peptide-induced cytokine and chemokine expression in THP-1 monocytes is blocked by small inhibitory RNA duplexes for early growth response-1 messenger RNA. J Immunol 170(10): 5281-94 (2003).
    • (2003) J Immunol , vol.170 , Issue.10 , pp. 5281-5294
    • Giri, R.K.1    Selvaraj, S.K.2    Kalra, V.K.3
  • 23
    • 7344246592 scopus 로고    scopus 로고
    • Amyloid-beta induces chemokine secretion and monocyte migration across a human blood--brain barrier model
    • Fiala M, Zhang L, Gan X, Sherry B, Taub D, Graves MC, et al. Amyloid-beta induces chemokine secretion and monocyte migration across a human blood--brain barrier model. Mol Med 4(7): 480-9 (1998).
    • (1998) Mol Med , vol.4 , Issue.7 , pp. 480-489
    • Fiala, M.1    Zhang, L.2    Gan, X.3    Sherry, B.4    Taub, D.5    Graves, M.C.6
  • 24
    • 0019972810 scopus 로고
    • The cholinergic hypothesis of geriatric memory dysfunction
    • Bartus RT, Dean RL 3rd, Beer B, Lippa AS. The cholinergic hypothesis of geriatric memory dysfunction. Science 217(4558): 408-14 (1982).
    • (1982) Science , vol.217 , Issue.4558 , pp. 408-414
    • Bartus, R.T.1    Dean III, R.L.2    Beer, B.3    Lippa, A.S.4
  • 25
    • 0036370776 scopus 로고    scopus 로고
    • Advances in the cellular and molecular biology of the beta-amyloid protein in Alzheimer's disease
    • Sambamurti K, Greig NH, Lahiri DK. Advances in the cellular and molecular biology of the beta-amyloid protein in Alzheimer's disease. Neuromolecular Med 1(1): 1-31 (2002).
    • (2002) Neuromolecular Med , vol.1 , Issue.1 , pp. 1-31
    • Sambamurti, K.1    Greig, N.H.2    Lahiri, D.K.3
  • 26
    • 0028197477 scopus 로고
    • Tacrine alters the processing of beta-amyloid precursor protein in different cell lines
    • Lahiri DK, Lewis S, Farlow MR. Tacrine alters the processing of beta-amyloid precursor protein in different cell lines. J Neurosci Res 37: 777-87 (1994).
    • (1994) J Neurosci Res , vol.37 , pp. 777-787
    • Lahiri, D.K.1    Lewis, S.2    Farlow, M.R.3
  • 27
    • 0030663142 scopus 로고    scopus 로고
    • Effects of cholinesterase inhibitors on the secretion of beta-amyloid precursor protein in cell cultures
    • Lahiri DK, Farlow MR, Nurnberger JI, Jr., Greig NH. Effects of cholinesterase inhibitors on the secretion of beta-amyloid precursor protein in cell cultures. Ann NY Acad Sci 826: 416-21 (1997).
    • (1997) Ann NY Acad Sci , vol.826 , pp. 416-421
    • Lahiri, D.K.1    Farlow, M.R.2    Nurnberger Jr., J.I.3    Greig, N.H.4
  • 28
    • 0032569990 scopus 로고    scopus 로고
    • The secretion of amyloid beta-peptides is inhibited in the tacrine-treated human neuroblastoma cells
    • Lahiri DK, Farlow MR, Sambamurti K. The secretion of amyloid beta-peptides is inhibited in the tacrine-treated human neuroblastoma cells. Mol Brain Res 62: 131-40 (1998).
    • (1998) Mol Brain Res , vol.62 , pp. 131-140
    • Lahiri, D.K.1    Farlow, M.R.2    Sambamurti, K.3
  • 29
    • 0035912825 scopus 로고    scopus 로고
    • Phenserine regulates translation of beta-amyloid precursor protein mRNA by a putative interleukin-1 responsive element, a target for drug development
    • Shaw KT, Utsuki T, Rogers J, Yu QS, Sambamurti K, Brossi A, Ge YW, et al. Phenserine regulates translation of beta-amyloid precursor protein mRNA by a putative interleukin-1 responsive element, a target for drug development. Proc Natl Acad Sci USA 98(13): 7605-10 (2001).
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.13 , pp. 7605-7610
    • Shaw, K.T.1    Utsuki, T.2    Rogers, J.3    Yu, Q.S.4    Sambamurti, K.5    Brossi, A.6    Ge, Y.W.7
  • 31
    • 45249108473 scopus 로고    scopus 로고
    • Structure-function implications in Alzheimer's disease: Effect of Abeta oligomers at central synapses
    • Cerpa W, Dinamarca MC, Inestrosa NC. Structure-function implications in Alzheimer's disease: effect of Abeta oligomers at central synapses. Curr Alzheimer Res 5(3): 233-43 (2008).
    • (2008) Curr Alzheimer Res , vol.5 , Issue.3 , pp. 233-243
    • Cerpa, W.1    Dinamarca, M.C.2    Inestrosa, N.C.3
  • 32
    • 22144436584 scopus 로고    scopus 로고
    • Memory deficits correlating with acetylcholinesterase splice shift and amyloid burden in doubly transgenic mice
    • Rees TM, Berson A, Sklan EH, Younkin L, Younkin S, Brimijoin S, et al. Memory deficits correlating with acetylcholinesterase splice shift and amyloid burden in doubly transgenic mice. Curr Alzheimer Res 2(3): 291-300 (2005).
    • (2005) Curr Alzheimer Res , vol.2 , Issue.3 , pp. 291-300
    • Rees, T.M.1    Berson, A.2    Sklan, E.H.3    Younkin, L.4    Younkin, S.5    Brimijoin, S.6
  • 33
    • 0037817311 scopus 로고    scopus 로고
    • Amyloid-beta increases acetylcholinesterase expression in neuroblastoma cells by reducing enzyme degradation
    • HuW, Gray NW, Brimijoin S. Amyloid-beta increases acetylcholinesterase expression in neuroblastoma cells by reducing enzyme degradation. J Neurochem 86(2): 470-78 (2003).
    • (2003) J Neurochem , vol.86 , Issue.2 , pp. 470-478
    • Hu, W.1    Gray, N.W.2    Brimijoin, S.3
  • 34
    • 84872769020 scopus 로고    scopus 로고
    • The non-neuronal cholinergic system: Basic science, therapeutic implications and new perspectives
    • Grando SA, Kawashima K, Kirkpatrick CJ, Meurs H, Wessler I. The non-neuronal cholinergic system: basic science, therapeutic implications and new perspectives. Life Sci 91(21-22): 969-72 (2012).
    • (2012) Life Sci , vol.91 , Issue.21-22 , pp. 969-972
    • Grando, S.A.1    Kawashima, K.2    Kirkpatrick, C.J.3    Meurs, H.4    Wessler, I.5
  • 35
    • 0037470612 scopus 로고    scopus 로고
    • The lymphocytic cholinergic system and its biological function
    • Kawashima K, Fujii T. The lymphocytic cholinergic system and its biological function. Life Sci 72: 2101-9 (2003).
    • (2003) Life Sci , vol.72 , pp. 2101-2109
    • Kawashima, K.1    Fujii, T.2
  • 36
    • 0344255794 scopus 로고    scopus 로고
    • The lymphocytic cholinergic system and its contribution to the regulation of immune activity
    • Kawashima K, Fujii T. The lymphocytic cholinergic system and its contribution to the regulation of immune activity. Life Sci 74: 675-96 (2003).
    • (2003) Life Sci , vol.74 , pp. 675-696
    • Kawashima, K.1    Fujii, T.2
  • 37
    • 84872775951 scopus 로고    scopus 로고
    • Regulatory mechanisms of acetylcholine synthesis and release by T cells
    • Fujii T, Takada-Takatori Y, Kawashima K. Regulatory mechanisms of acetylcholine synthesis and release by T cells. Life Sci 91(21-22): 981-5 (2012)
    • (2012) Life Sci , vol.91 , Issue.21-22 , pp. 981-985
    • Fujii, T.1    Takada-Takatori, Y.2    Kawashima, K.3
  • 38
    • 20644439539 scopus 로고    scopus 로고
    • Regulation of CD8+ cytolytic T lymphocyte differentiation by a cholinergic pathway
    • Zimring JC, Kapp LM, Yamada M, Wess J, Kapp JA. Regulation of CD8+ cytolytic T lymphocyte differentiation by a cholinergic pathway. J Neuroimmunol 164(1-2): 66-75 (2005).
    • (2005) J Neuroimmunol , vol.164 , Issue.1-2 , pp. 66-75
    • Zimring, J.C.1    Kapp, L.M.2    Yamada, M.3    Wess, J.4    Kapp, J.A.5
  • 39
    • 2942530300 scopus 로고    scopus 로고
    • Acetylcholinesterase and its inhibition in Alzheimer disease
    • Lane RM, Kivipelto M, Greig NH. Acetylcholinesterase and its inhibition in Alzheimer disease. Clin Neuropharmacol 27(3):141-9 (2004).
    • (2004) Clin Neuropharmacol , vol.27 , Issue.3 , pp. 141-149
    • Lane, R.M.1    Kivipelto, M.2    Greig, N.H.3
  • 40
    • 30344485665 scopus 로고    scopus 로고
    • Targeting acetylcholinesterase and butyrylcholinesterase in dementia
    • Lane RM, Potkin SG, Enz A. Targeting acetylcholinesterase and butyrylcholinesterase in dementia. Int J Neuropsychopharmacol 9(1):101-24 (2006).
    • (2006) Int J Neuropsychopharmacol , vol.9 , Issue.1 , pp. 101-124
    • Lane, R.M.1    Potkin, S.G.2    Enz, A.3
  • 41
    • 28044437122 scopus 로고    scopus 로고
    • Selective butyrylcholinesterase inhibition elevates brain acetylcholine, augments learning and lowers Alzheimer β-amyloid peptide in rodent
    • Greig NH, Utsuki T, Ingram DK, Wang Y, Pepeu G, Scali C, et al. Selective butyrylcholinesterase inhibition elevates brain acetylcholine, augments learning and lowers Alzheimer β-amyloid peptide in rodent. Proc Natl Acad Sci USA 102: 17213-8 (2005).
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17213-17218
    • Greig, N.H.1    Utsuki, T.2    Ingram, D.K.3    Wang, Y.4    Pepeu, G.5    Scali, C.6
  • 42
    • 0035661483 scopus 로고    scopus 로고
    • A new therapeutic target in Alzheimer's disease treatment: Attention to butyrylcholinesesterase
    • Greig NH, Utsuki T, Yu Q, Zhu X, Holloway HW, Perry T, et al. A new therapeutic target in Alzheimer's disease treatment: attention to butyrylcholinesesterase. Curr Med Res Opin 17(3): 1-7 (2001).
    • (2001) Curr Med Res Opin , vol.17 , Issue.3 , pp. 1-7
    • Greig, N.H.1    Utsuki, T.2    Yu, Q.3    Zhu, X.4    Holloway, H.W.5    Perry, T.6
  • 43
  • 44
  • 45
    • 34548779802 scopus 로고    scopus 로고
    • N1phenethyl-norcymserine, a selective butyrylcholinesterase inhibitor, increases acetylcholine release in rat cerebral cortex: A comparison with donepezil and rivastigmine
    • Cerbai F, Giovannini MG, Melani C, Enz A, Pepeu G. N1phenethyl-norcymserine, a selective butyrylcholinesterase inhibitor, increases acetylcholine release in rat cerebral cortex: a comparison with donepezil and rivastigmine. Eur J Pharmacol 572(2-3):142-50 (2007).
    • (2007) Eur J Pharmacol , vol.572 , Issue.2-3 , pp. 142-150
    • Cerbai, F.1    Giovannini, M.G.2    Melani, C.3    Enz, A.4    Pepeu, G.5
  • 46
    • 33846981174 scopus 로고    scopus 로고
    • Excessive levels of hippocampal acetylcholine in acetylcholinesterase-knockout mice are moderated by butyrylcholinesterase activity
    • Hartmann J, Kiewert C, Duysen EG, Lockridge O, Greig NH, Klein J. Excessive levels of hippocampal acetylcholine in acetylcholinesterase-knockout mice are moderated by butyrylcholinesterase activity. J Neurochem 100: 1421-8 (2007).
    • (2007) J Neurochem , vol.100 , pp. 1421-1428
    • Hartmann, J.1    Kiewert, C.2    Duysen, E.G.3    Lockridge, O.4    Greig, N.H.5    Klein, J.6
  • 50
    • 70450231676 scopus 로고    scopus 로고
    • Neuroprotective and neurotoxic effects of nicotine
    • Ferrea S, Winterer G. Neuroprotective and neurotoxic effects of nicotine. Pharmacopsychiatry 42(6): 255-65 (2009).
    • (2009) Pharmacopsychiatry , vol.42 , Issue.6 , pp. 255-265
    • Ferrea, S.1    Winterer, G.2
  • 51
    • 0036316642 scopus 로고    scopus 로고
    • Chronic nicotine treatment reduces beta-amyloidosis in the brain of a mouse model of Alzheimer's disease (APPsw)
    • Nordberg A, Hellström-Lindahl E, Lee M, Johnson M, Mousavi M, Hall R, et al. Chronic nicotine treatment reduces beta-amyloidosis in the brain of a mouse model of Alzheimer's disease (APPsw). J Neurochem 81(3): 655-8 (2002).
    • (2002) J Neurochem , vol.81 , Issue.3 , pp. 655-658
    • Nordberg, A.1    Hellström-Lindahl, E.2    Lee, M.3    Johnson, M.4    Mousavi, M.5    Hall, R.6
  • 52
    • 32844461888 scopus 로고    scopus 로고
    • Nicotinic effects on cognitive function: Behavioral characterization, pharmacological specification, and anatomic localization
    • Levin ED, McClernon FJ, Rezvani AH. Nicotinic effects on cognitive function: behavioral characterization, pharmacological specification, and anatomic localization. Psychopharmacol 184(3-4):523-39 (2006).
    • (2006) Psychopharmacol , vol.184 , Issue.3-4 , pp. 523-539
    • Levin, E.D.1    McClernon, F.J.2    Rezvani, A.H.3
  • 53
    • 0034713266 scopus 로고    scopus 로고
    • Vagus nerve stimulation attenuates the systemic inflammatory response to endotoxin
    • Borovikova LV, Ivanova S, Zhang M, Yang H, Botchkina GI, Watkins LR, et al. Vagus nerve stimulation attenuates the systemic inflammatory response to endotoxin. Nature 405(6785): 458-62 (2000).
    • (2000) Nature , vol.405 , Issue.6785 , pp. 458-462
    • Borovikova, L.V.1    Ivanova, S.2    Zhang, M.3    Yang, H.4    Botchkina, G.I.5    Watkins, L.R.6
  • 54
    • 0037461768 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor alpha7 subunit is an essential regulator of inflammation
    • Wang H, Yu M, Ochani M, Amella CA, Tanovic M, Susarla S. Nicotinic acetylcholine receptor alpha7 subunit is an essential regulator of inflammation. Nature 421: 384-388 (2003).
    • (2003) Nature , vol.421 , pp. 384-388
    • Wang, H.1    Yu, M.2    Ochani, M.3    Amella, C.A.4    Tanovic, M.5    Susarla, S.6
  • 55
    • 84879198267 scopus 로고    scopus 로고
    • Modulation of inflammatory pathways by the immune cholinergic system
    • Nizri E, Brenner T. Modulation of inflammatory pathways by the immune cholinergic system. Amino Acids 45(1): 73-85 (2013).
    • (2013) Amino Acids , vol.45 , Issue.1 , pp. 73-85
    • Nizri, E.1    Brenner, T.2
  • 56
    • 34547558959 scopus 로고    scopus 로고
    • The alpha7 nicotinic acetylcholine receptor as a pharmacological target for inflammation
    • de Jonge WJ, Ulloa L. The alpha7 nicotinic acetylcholine receptor as a pharmacological target for inflammation. Br J Pharmacol 151(7): 915-29 (2007).
    • (2007) Br J Pharmacol , vol.151 , Issue.7 , pp. 915-929
    • de Jonge, W.J.1    Ulloa, L.2
  • 57
    • 14844311199 scopus 로고    scopus 로고
    • The amyloid-beta peptide suppresses transforming growth factor-beta1-induced matrix metalloproteinase-2 production via Smad7 expression in human monocytic THP-1 cells
    • Lee EO, Kang JL, Chong YH. The amyloid-beta peptide suppresses transforming growth factor-beta1-induced matrix metalloproteinase-2 production via Smad7 expression in human monocytic THP-1 cells. Biol Chem 280: 7845-53 (2005).
    • (2005) Biol Chem , vol.280 , pp. 7845-7853
    • Lee, E.O.1    Kang, J.L.2    Chong, Y.H.3
  • 58
    • 0033587026 scopus 로고    scopus 로고
    • Synthesis of novel phenserine-based-selective inhibitors of butyrylcholinesterase for Alzheimer's disease
    • Yu Q, Holloway HW, Utsuki T, Brossi A, Greig NH. Synthesis of novel phenserine-based-selective inhibitors of butyrylcholinesterase for Alzheimer's disease. J Med Chem 42(10): 1855-61 (1999).
    • (1999) J Med Chem , vol.42 , Issue.10 , pp. 1855-1861
    • Yu, Q.1    Holloway, H.W.2    Utsuki, T.3    Brossi, A.4    Greig, N.H.5
  • 59
    • 0028894072 scopus 로고
    • Phenserine and ring-C hetero-analogues: Drug candidates for the treatment of Alzheimer's disease
    • Greig NH, Pei X-F, Soncrant T, Ingram D, Brossi A. Phenserine and ring-C hetero-analogues: drug candidates for the treatment of Alzheimer's disease. Med Chem Rev 15: 3-31 (1995).
    • (1995) Med Chem Rev , vol.15 , pp. 3-31
    • Greig, N.H.1    Pei, X.-F.2    Soncrant, T.3    Ingram, D.4    Brossi, A.5
  • 60
    • 0021271971 scopus 로고
    • Clinical diagnosis of Alzheimer's disease: Report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Service Task Force on Alzheimer's Disease
    • McKhann G, Drachman D, Folstein M, Katzman R, Price D, Stadlan EM. Clinical diagnosis of Alzheimer's disease: report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Service Task Force on Alzheimer's Disease. Neurology 34: 939-944 (1984).
    • (1984) Neurology , vol.34 , pp. 939-944
    • McKhann, G.1    Drachman, D.2    Folstein, M.3    Katzman, R.4    Price, D.5    Stadlan, E.M.6
  • 64
    • 0033982028 scopus 로고    scopus 로고
    • Amyloid beta and amylin fibrils induce increases in proinflammatory cytokine and chemokine production by THP-1 cells and murine microglia
    • Yates SL, Burgess LH, Kocsis-Angle J, Antal JM, Dority MD, Embury PB, et al. Amyloid beta and amylin fibrils induce increases in proinflammatory cytokine and chemokine production by THP-1 cells and murine microglia. J Neurochem 74(3):1017-25 (2000).
    • (2000) J Neurochem , vol.74 , Issue.3 , pp. 1017-1025
    • Yates, S.L.1    Burgess, L.H.2    Kocsis-Angle, J.3    Antal, J.M.4    Dority, M.D.5    Embury, P.B.6
  • 65
    • 0034813586 scopus 로고    scopus 로고
    • Regulation of betaamyloid stimulated proinflammatory responses by peroxisome proliferator-activated receptor alpha
    • Combs CK, Bates P, Karlo JC, Landreth GE. Regulation of betaamyloid stimulated proinflammatory responses by peroxisome proliferator-activated receptor alpha. Neurochem Int 39(5-6): 449-57 (2001).
    • (2001) Neurochem Int , vol.39 , Issue.5-6 , pp. 449-457
    • Combs, C.K.1    Bates, P.2    Karlo, J.C.3    Landreth, G.E.4
  • 66
    • 54149085909 scopus 로고    scopus 로고
    • All-or-nothing type biphasic cytokine production of human lymphocytes after exposure to Alzheimer's beta-amyloid peptide
    • Teixeira AL, Reis HJ, Coelho FM, Carneiro DS, Teixeira MM, Vieira LB, et al. All-or-nothing type biphasic cytokine production of human lymphocytes after exposure to Alzheimer's beta-amyloid peptide. Biol Psychiatry 64(10): 891-5 (2008).
    • (2008) Biol Psychiatry , vol.64 , Issue.10 , pp. 891-895
    • Teixeira, A.L.1    Reis, H.J.2    Coelho, F.M.3    Carneiro, D.S.4    Teixeira, M.M.5    Vieira, L.B.6
  • 67
    • 22144494112 scopus 로고    scopus 로고
    • An overview of phenserine tartrate, a novel acetylcholinesterase inhibitor for the treatment of Alzheimer's disease
    • Greig NH, Sambamurti K, Yu QS, Brossi A, Bruinsma GB, Lahiri DK. An overview of phenserine tartrate, a novel acetylcholinesterase inhibitor for the treatment of Alzheimer's disease. Curr Alzheimer Res 2: 281-90 (2005).
    • (2005) Curr Alzheimer Res , vol.2 , pp. 281-290
    • Greig, N.H.1    Sambamurti, K.2    Yu, Q.S.3    Brossi, A.4    Bruinsma, G.B.5    Lahiri, D.K.6
  • 68
    • 84155166859 scopus 로고    scopus 로고
    • Peripheral blood mono-nuclear cells derived from Alzheimer's disease patients show elevated baseline levels of secreted cytokines but resist stimulation with β-amyloid peptide
    • Rocha NP, Teixeira AL, Coelho FM, Caramelli P, Guimarães HC, Barbosa IG, et al. Peripheral blood mono-nuclear cells derived from Alzheimer's disease patients show elevated baseline levels of secreted cytokines but resist stimulation with β-amyloid peptide. Mol Cell Neurosci 49(1):77-84 (2012).
    • (2012) Mol Cell Neurosci , vol.49 , Issue.1 , pp. 77-84
    • Rocha, N.P.1    Teixeira, A.L.2    Coelho, F.M.3    Caramelli, P.4    Guimarães, H.C.5    Barbosa, I.G.6
  • 70
    • 77952542382 scopus 로고    scopus 로고
    • Biological markers of amyloid beta-related mechanisms in Alzheimer's disease
    • Hampel H, Shen Y, Walsh DM, Aisen P, Shaw LM, Zetterberg H, et al. Biological markers of amyloid beta-related mechanisms in Alzheimer's disease. Exp Neurol 223(2): 334-46 (2010).
    • (2010) Exp Neurol , vol.223 , Issue.2 , pp. 334-346
    • Hampel, H.1    Shen, Y.2    Walsh, D.M.3    Aisen, P.4    Shaw, L.M.5    Zetterberg, H.6
  • 71
    • 84876850027 scopus 로고    scopus 로고
    • Pathogenesis of Abetaoligomers in synaptic failure
    • Sivanesan S, Tan A, Rajadas J. Pathogenesis of Abetaoligomers in synaptic failure. Curr Alzheimer Res 10(3): 316-23 (2013).
    • (2013) Curr Alzheimer Res , vol.10 , Issue.3 , pp. 316-323
    • Sivanesan, S.1    Tan, A.2    Rajadas, J.3
  • 72
    • 0028971069 scopus 로고
    • Vector-mediated delivery of 125I-labeled beta-amyloid peptide A beta 1-40 through the blood-brain barrier and binding to Alzheimer disease amyloid of the A beta 1-40/vector complex
    • Saito Y, Buciak J, Yang J, Pardridge WM. Vector-mediated delivery of 125I-labeled beta-amyloid peptide A beta 1-40 through the blood-brain barrier and binding to Alzheimer disease amyloid of the A beta 1-40/vector complex. Proc Natl Acad Sci USA 92: 10227-31 (1995)
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10227-10231
    • Saito, Y.1    Buciak, J.2    Yang, J.3    Pardridge, W.M.4
  • 73
    • 0031961832 scopus 로고    scopus 로고
    • Cerebrovascular accumulation and increased blood-brain barrier permeability to circulating Alzheimer's amyloid beta peptide in aged squirrel monkey with cerebral amyloid angiopathy
    • Mackic JB, Weiss MH, Miao W, Kirkman E, Ghiso J, Calero M, et al. Cerebrovascular accumulation and increased blood-brain barrier permeability to circulating Alzheimer's amyloid beta peptide in aged squirrel monkey with cerebral amyloid angiopathy. J Neurochem 70: 210-15 (1998).
    • (1998) J Neurochem , vol.70 , pp. 210-215
    • Mackic, J.B.1    Weiss, M.H.2    Miao, W.3    Kirkman, E.4    Ghiso, J.5    Calero, M.6
  • 74
    • 65649105035 scopus 로고    scopus 로고
    • Clearance of amyloidbeta peptide across the blood-brain barrier: Implication for therapies in Alzheimer's disease
    • Deane R, Bell RD, Sagare A, Zlokovic BV. Clearance of amyloidbeta peptide across the blood-brain barrier: implication for therapies in Alzheimer's disease. CNS Neurol Disord Drug Targets 8(1):16-30 (2009).
    • (2009) CNS Neurol Disord Drug Targets , vol.8 , Issue.1 , pp. 16-30
    • Deane, R.1    Bell, R.D.2    Sagare, A.3    Zlokovic, B.V.4
  • 75
    • 80053129900 scopus 로고    scopus 로고
    • The molecular assembly of amyloid abeta controls its neurotoxicity and binding to cellular proteins
    • Manzoni C, Colombo L, Bigini P, Diana V, Cagnotto A, et al. The molecular assembly of amyloid abeta controls its neurotoxicity and binding to cellular proteins. PLoS One 6: e24909 (2011).
    • (2011) PLoS One , vol.6
    • Manzoni, C.1    Colombo, L.2    Bigini, P.3    Diana, V.4    Cagnotto, A.5
  • 76
    • 42649084052 scopus 로고    scopus 로고
    • The role of interleukin-1 in neuroinflammation and Alzheimer disease: An evolving perspective
    • Shaftel SS, Griffin WS, O'Banion MK. The role of interleukin-1 in neuroinflammation and Alzheimer disease: an evolving perspective. J Neuroinflammation 5: 7 (2008).
    • (2008) J Neuroinflammation , vol.5 , pp. 7
    • Shaftel, S.S.1    Griffin, W.S.2    O'Banion, M.K.3
  • 77
    • 84861473274 scopus 로고    scopus 로고
    • Tumor necrosis factor-α synthesis inhibitor 3,6'-dithiothalidomide attenuates markers of inflammation, Alzheimer pathology and behavioral deficits in animal models of neuroinflammation and Alzheimer's disease
    • Tweedie D, Ferguson RA, Fishman K, Frankola KA, Van Praag H, Holloway HW, et al. Tumor necrosis factor-α synthesis inhibitor 3,6'-dithiothalidomide attenuates markers of inflammation, Alzheimer pathology and behavioral deficits in animal models of neuroinflammation and Alzheimer's disease. J Neuroinflammation 9: 106 (2012).
    • (2012) J Neuroinflammation , vol.9 , pp. 106
    • Tweedie, D.1    Ferguson, R.A.2    Fishman, K.3    Frankola, K.A.4    Van Praag, H.5    Holloway, H.W.6
  • 78
    • 79951701971 scopus 로고    scopus 로고
    • Targeting TNF-α to elucidate and ameliorate neuroinflammation in neurodegenerative diseases
    • Frankola KA, Greig NH, Luo W, Tweedie D. Targeting TNF-α to elucidate and ameliorate neuroinflammation in neurodegenerative diseases. CNS Neurol Disord Drug Targets 10(3): 391-403 (2011).
    • (2011) CNS Neurol Disord Drug Targets , vol.10 , Issue.3 , pp. 391-403
    • Frankola, K.A.1    Greig, N.H.2    Luo, W.3    Tweedie, D.4
  • 79
    • 84870038215 scopus 로고    scopus 로고
    • The vagus nerve and the inflammatory reflex--linking immunity and metabolism
    • Pavlov VA, Tracey KJ. The vagus nerve and the inflammatory reflex--linking immunity and metabolism. Nat Rev Endocrinol 8(12): 743-54 (2012).
    • (2012) Nat Rev Endocrinol , vol.8 , Issue.12 , pp. 743-754
    • Pavlov, V.A.1    Tracey, K.J.2
  • 80
    • 0035866060 scopus 로고    scopus 로고
    • Beta-Amyloid stimulation of microglia and monocytes results in TNFalpha-dependent expression of inducible nitric oxide synthase and neuronal apoptosis
    • Combs CK, Karlo JC, Kao SC, Landreth GE. beta-Amyloid stimulation of microglia and monocytes results in TNFalpha-dependent expression of inducible nitric oxide synthase and neuronal apoptosis. J Neurosci 21(4): 1179-88 (2001).
    • (2001) J Neurosci , vol.21 , Issue.4 , pp. 1179-1188
    • Combs, C.K.1    Karlo, J.C.2    Kao, S.C.3    Landreth, G.E.4
  • 81
    • 79955738773 scopus 로고    scopus 로고
    • The history of the cholinergic hypothesis
    • Contestabile A. The history of the cholinergic hypothesis. Behav Brain Res 221(2): 334-40 (2011).
    • (2011) Behav Brain Res , vol.221 , Issue.2 , pp. 334-340
    • Contestabile, A.1
  • 83
    • 0028174977 scopus 로고
    • The cholinesterases: From genes to proteins
    • Taylor P, Radic Z. The cholinesterases: from genes to proteins. Ann Rev Pharmacol Toxicol 34: 281-320 (1994).
    • (1994) Ann Rev Pharmacol Toxicol , vol.34 , pp. 281-320
    • Taylor, P.1    Radic, Z.2
  • 86
    • 84865654979 scopus 로고    scopus 로고
    • α7 nicotinic acetylcholine receptor (α7nAChR) expression in bone marrow-derived non-T cells is required for the inflammatory reflex
    • Olofsson PS, Katz DA, Rosas-Ballina M, Levine YA, Ochani M, Valdés-Ferrer SI, et al. α7 nicotinic acetylcholine receptor (α7nAChR) expression in bone marrow-derived non-T cells is required for the inflammatory reflex. Mol Med 18: 539-43 (2012).
    • (2012) Mol Med , vol.18 , pp. 539-543
    • Olofsson, P.S.1    Katz, D.A.2    Rosas-Ballina, M.3    Levine, Y.A.4    Ochani, M.5    Valdés-Ferrer, S.I.6
  • 87
    • 11144355227 scopus 로고    scopus 로고
    • Cholinergic modulation of microglia activation by a 7 nicotinic receptors
    • Shytle RD, Mori T, Townsend K, Vendrame M, Sun M, Zeng J, et al. Cholinergic modulation of microglia activation by a 7 nicotinic receptors. J. Neurochem 89: 337-43 (2004).
    • (2004) J Neurochem , vol.89 , pp. 337-343
    • Shytle, R.D.1    Mori, T.2    Townsend, K.3    Vendrame, M.4    Sun, M.5    Zeng, J.6
  • 88
    • 84859354765 scopus 로고    scopus 로고
    • Association between butyrylcholinesterase activity and low-grade systemic inflammation
    • Lampón N, Hermida-Cadahia EF, Riveiro A, Tutor JC. Association between butyrylcholinesterase activity and low-grade systemic inflammation. Ann Hepatol 11(3): 356-63 (2012).
    • (2012) Ann Hepatol , vol.11 , Issue.3 , pp. 356-363
    • Lampón, N.1    Hermida-Cadahia, E.F.2    Riveiro, A.3    Tutor, J.C.4
  • 89
    • 58549098084 scopus 로고    scopus 로고
    • Blood-brain barrier: Ageing and microvascular disease--systematic review and meta-analysis
    • Farrall AJ, Wardlaw JM. Blood-brain barrier: ageing and microvascular disease--systematic review and meta-analysis. Neurobiol Aging 30: 337-52 (2009).
    • (2009) Neurobiol Aging , vol.30 , pp. 337-352
    • Farrall, A.J.1    Wardlaw, J.M.2
  • 90
    • 47849132772 scopus 로고    scopus 로고
    • Peripheral chemokine receptors, their ligands, cytokines and Alzheimer's disease
    • Reale M, Iarlori C, Feliciani C, Gambi D. Peripheral chemokine receptors, their ligands, cytokines and Alzheimer's disease. J Alzheimers Dis 14(2):147-59 (2008).
    • (2008) J Alzheimers Dis , vol.14 , Issue.2 , pp. 147-159
    • Reale, M.1    Iarlori, C.2    Feliciani, C.3    Gambi, D.4
  • 91
    • 33645227116 scopus 로고    scopus 로고
    • The acetylcholinesterase inhibitor, Donepezil, regulates a Th2 bias in Alzheimer's disease patients
    • Reale M, Iarlori C, Gambi F, Feliciani C, Isabella L, Gambi D. The acetylcholinesterase inhibitor, Donepezil, regulates a Th2 bias in Alzheimer's disease patients. Neuropharmacol 50(5): 606-13 (2006).
    • (2006) Neuropharmacol , vol.50 , Issue.5 , pp. 606-613
    • Reale, M.1    Iarlori, C.2    Gambi, F.3    Feliciani, C.4    Isabella, L.5    Gambi, D.6
  • 92
    • 35448954937 scopus 로고    scopus 로고
    • Elevated butyrylcholinesterase and acetylcholinesterase may predict the development of type 2 diabetes mellitus and Alzheimer's disease
    • Rao AA, Sridhar GR, Das UN. Elevated butyrylcholinesterase and acetylcholinesterase may predict the development of type 2 diabetes mellitus and Alzheimer's disease. Med Hypotheses 69(6):1272-6 (2007).
    • (2007) Med Hypotheses , vol.69 , Issue.6 , pp. 1272-1276
    • Rao, A.A.1    Sridhar, G.R.2    Das, U.N.3
  • 93
    • 0030879686 scopus 로고    scopus 로고
    • Selective phosphorylation of adult tau isoforms in mature hippocampal neurons exposed to fibrillar A beta
    • Ferreira A, Lu Q, Orecchio L, Kosik KS. Selective phosphorylation of adult tau isoforms in mature hippocampal neurons exposed to fibrillar A beta. Mol Cell Neurosci 9(3): 220-34 (1997).
    • (1997) Mol Cell Neurosci , vol.9 , Issue.3 , pp. 220-234
    • Ferreira, A.1    Lu, Q.2    Orecchio, L.3    Kosik, K.S.4
  • 94
    • 0033957692 scopus 로고    scopus 로고
    • PD98059 prevents neurite degeneration induced by fibrillar beta-amyloid in mature hippocampal neurons
    • Rapoport M, Ferreira A. PD98059 prevents neurite degeneration induced by fibrillar beta-amyloid in mature hippocampal neurons J Neurochem 74(1): 125-33 (2000).
    • (2000) J Neurochem , vol.74 , Issue.1 , pp. 125-133
    • Rapoport, M.1    Ferreira, A.2
  • 95
    • 0034730892 scopus 로고    scopus 로고
    • Amyloid beta neurotoxicity not mediated by the mitogen-activated protein kinase cascade in cultured rat hippocampal and cortical neurons
    • Abe K, Saito H. Amyloid beta neurotoxicity not mediated by the mitogen-activated protein kinase cascade in cultured rat hippocampal and cortical neurons. Neurosci Lett 292(1): 1-4 (2000).
    • (2000) Neurosci Lett , vol.2 , Issue.1 , pp. 1-4
    • Abe, K.1    Saito, H.2
  • 96
    • 0037352702 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is involved in Toll-like receptor 4-mediated cytokine expression in mouse macrophages
    • Ojaniemi M, Glumoff V, Harju K, Liljeroos M, Vuori K, Hallman M. Phosphatidylinositol 3-kinase is involved in Toll-like receptor 4-mediated cytokine expression in mouse macrophages. Eur J Immunol 33:597-605 (2003).
    • (2003) Eur J Immunol , vol.33 , pp. 597-605
    • Ojaniemi, M.1    Glumoff, V.2    Harju, K.3    Liljeroos, M.4    Vuori, K.5    Hallman, M.6
  • 97
    • 19344365340 scopus 로고    scopus 로고
    • LY294002 inhibits LPSinduced NO production through a inhibition of NF-kappaB activation: Independent mechanism of phosphatidylinositol 3-kinase
    • Kim YH, Choi KH, Park JW, Kwon TK. LY294002 inhibits LPSinduced NO production through a inhibition of NF-kappaB activation: independent mechanism of phosphatidylinositol 3-kinase. Immunol Lett 99: 45-50 (2005).
    • (2005) Immunol Lett , vol.99 , pp. 45-50
    • Kim, Y.H.1    Choi, K.H.2    Park, J.W.3    Kwon, T.K.4
  • 99
    • 0346103719 scopus 로고    scopus 로고
    • Modulation of the phosphoinositide 3-kinase pathway alters innate resistance to polymicrobial sepsis
    • Williams DL, Li C, Ha T, Ozment-Skelton T, Kalbfleisch JH, Preiszner J, et al. Modulation of the phosphoinositide 3-kinase pathway alters innate resistance to polymicrobial sepsis. J Immunol 172: 449-56 (2004).
    • (2004) J Immunol , vol.172 , pp. 449-456
    • Williams, D.L.1    Li, C.2    Ha, T.3    Ozment-Skelton, T.4    Kalbfleisch, J.H.5    Preiszner, J.6
  • 101
    • 0038705106 scopus 로고    scopus 로고
    • Role of cytokines in the gene expression of amyloid ß-protein precursor: Identification of a 5'-UTR-binding nuclear factor and its implications in Alzheimer's disease
    • Lahiri DK, Chen D, Vivien D, Ge Y-W, Greig, NH, Rogers JT. Role of cytokines in the gene expression of amyloid ß-protein precursor: identification of a 5'-UTR-binding nuclear factor and its implications in Alzheimer's disease. J Alzheimers Dis 5(2): 81-90 (2003).
    • (2003) J Alzheimers Dis , vol.5 , Issue.2 , pp. 81-90
    • Lahiri, D.K.1    Chen, D.2    Vivien, D.3    Ge, Y.-W.4    Greig, N.H.5    Rogers, J.T.6
  • 102
    • 0038719725 scopus 로고    scopus 로고
    • Transforming growth factor-beta 1 potentiates amyloid-beta generation in astrocytes and in transgenic mice
    • Lesné S, Docagne F, Gabriel C, Liot G, Lahiri DK, Buée L, et al. Transforming growth factor-beta 1 potentiates amyloid-beta generation in astrocytes and in transgenic mice. J Biol Chem 278(20): 18408-18 (2003).
    • (2003) J Biol Chem , vol.278 , Issue.20 , pp. 18408-18418
    • Lesné, S.1    Docagne, F.2    Gabriel, C.3    Liot, G.4    Lahiri, D.K.5    Buée, L.6
  • 103
    • 70349782469 scopus 로고    scopus 로고
    • Amyloid-beta(1-42) fibrillar precursors are optimal for inducing tumor necrosis factoralpha production in the THP-1 human monocytic cell line
    • Ajit D, Udan ML, Paranjape G, Nichols MR. Amyloid-beta(1-42) fibrillar precursors are optimal for inducing tumor necrosis factoralpha production in the THP-1 human monocytic cell line. Biochemistry 48(38): 9011-21 (2009).
    • (2009) Biochemistry , vol.48 , Issue.38 , pp. 9011-9021
    • Ajit, D.1    Udan, M.L.2    Paranjape, G.3    Nichols, M.R.4
  • 104
    • 0031056029 scopus 로고    scopus 로고
    • Interaction of Alzheimer beta-amyloid peptide with the human monocytic cell line THP-1 results in a protein kinase C-dependent secretion of tumor necrosis factor-alpha
    • Klegeris A, Walker DG, McGeer PL. Interaction of Alzheimer beta-amyloid peptide with the human monocytic cell line THP-1 results in a protein kinase C-dependent secretion of tumor necrosis factor-alpha. Brain Res 747(1): 114-21 (1997).
    • (1997) Brain Res , vol.747 , Issue.1 , pp. 114-121
    • Klegeris, A.1    Walker, D.G.2    McGeer, P.L.3
  • 105
    • 22144489808 scopus 로고    scopus 로고
    • Non-steroidal anti-inflammatory drugs (NSAIDs) and other anti-inflammatory agents in the treatment of neurodegenerative disease
    • Klegeris A, McGeer PL. Non-steroidal anti-inflammatory drugs (NSAIDs) and other anti-inflammatory agents in the treatment of neurodegenerative disease. Curr Alzheimer Res 2(3): 355-65 (2005).
    • (2005) Curr Alzheimer Res , vol.2 , Issue.3 , pp. 355-365
    • Klegeris, A.1    McGeer, P.L.2
  • 106
    • 80053385335 scopus 로고    scopus 로고
    • The Alzheimer's amyloid-β peptide (Aβ)binds a specific DNA Abeta-interacting domain (AβID) in the APP, BACE1, and APOE promoters in a sequence-specific manner: Characterizing a new regulatory motif
    • Maloney B, Lahiri DK. The Alzheimer's amyloid-β peptide (Aβ)binds a specific DNA Abeta-interacting domain (AβID) in the APP, BACE1, and APOE promoters in a sequence-specific manner: characterizing a new regulatory motif. Gene 488(1-2): 1-12 (2011).
    • (2011) Gene , vol.488 , Issue.1-2 , pp. 1-12
    • Maloney, B.1    Lahiri, D.K.2
  • 107
    • 80053384785 scopus 로고    scopus 로고
    • Functional activity of the novel Alzheimer's amyloid-βpeptide interacting domain (AβID) in the APP and BACE1 promoter sequences and implications in activating apoptotic genes and in amyloidogenesis
    • Bailey JA, Maloney B, Ge Y-W, Lahiri, DK. Functional activity of the novel Alzheimer's amyloid-βpeptide interacting domain (AβID) in the APP and BACE1 promoter sequences and implications in activating apoptotic genes and in amyloidogenesis. Gene 488(1-2): 13-22 (2011).
    • (2011) Gene , vol.488 , Issue.1-2 , pp. 13-22
    • Bailey, J.A.1    Maloney, B.2    Ge, Y.-W.3    Lahiri, D.K.4
  • 108
    • 4544295150 scopus 로고    scopus 로고
    • Rationale for the development of cholinesterase inhibitors as anti-Alzheimer agents
    • Lahiri DK, Rogers JT, Greig NH, Sambamurti K. Rationale for the development of cholinesterase inhibitors as anti-Alzheimer agents. Curr Pharm Des 10: 3111-9 (2004).
    • (2004) Curr Pharm Des , vol.10 , pp. 3111-3119
    • Lahiri, D.K.1    Rogers, J.T.2    Greig, N.H.3    Sambamurti, K.4
  • 109
  • 110
    • 70349306585 scopus 로고    scopus 로고
    • Cholinesterase inhibition: Is there evidence for disease-modifying effects?
    • Shanks M, Kivipelto M, Bullock R, Lane R. Cholinesterase inhibition: is there evidence for disease-modifying effects? Curr Med Res Opin 25(10): 2439-46 (2009).
    • (2009) Curr Med Res Opin 2 , vol.5 , Issue.10 , pp. 2439-2446
    • Shanks, M.1    Kivipelto, M.2    Bullock, R.3    Lane, R.4
  • 111
    • 84859070489 scopus 로고    scopus 로고
    • Neuronal receptors as targets for the action of amyloid-beta protein (Aβ) in the brain
    • Patel AN, Jhamandas JH. Neuronal receptors as targets for the action of amyloid-beta protein (Aβ) in the brain. Expert Rev Mol Med 14: e2 (2012).
    • (2012) Expert Rev Mol Med , vol.14
    • Patel, A.N.1    Jhamandas, J.H.2
  • 112
    • 84655164275 scopus 로고    scopus 로고
    • Cholinergic modulation of amyloid precursor protein processing with emphasis on M1 muscarinic receptor: Perspectives and challenges in treatment of Alzheimer's disease
    • Fisher A. Cholinergic modulation of amyloid precursor protein processing with emphasis on M1 muscarinic receptor: perspectives and challenges in treatment of Alzheimer's disease. J Neurochem 120(1): 22-33 (2012).
    • (2012) J Neurochem , vol.120 , Issue.1 , pp. 22-33
    • Fisher, A.1
  • 113
    • 33745402341 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibitors for Alzheimer's disease: Anti-inflammatories in acetylcholine clothing!
    • Tabet N. Acetylcholinesterase inhibitors for Alzheimer's disease: anti-inflammatories in acetylcholine clothing! Age Ageing 35(4): 336-8 (2006).
    • (2006) Age Ageing , vol.35 , Issue.4 , pp. 336-338
    • Tabet, N.1


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