메뉴 건너뛰기




Volumn 11, Issue 4, 2000, Pages 329-382

Mechanisms of β-amyloid neurotoxicity: Perspectives of pharmacotherapy

Author keywords

amyloid; Anti amyloid peptide; Calcium; Drug delivery; Excitotoxicity; Oxidative stress

Indexed keywords

2 DIPROPYLAMINO 8 HYDROXYTETRALIN; ACETYLCHOLINESTERASE; ADENOSINE A1 RECEPTOR AGONIST; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN ANTIBODY; AMYLOID PRECURSOR PROTEIN; CALCIUM CHANNEL BLOCKING AGENT; CHOLINE ACETYLTRANSFERASE; CORTICOSTERONE; GLUCOCORTICOID; IFENPRODIL; N [2 [4 (2 METHOXYPHENYL) 1 PIPERAZINYL]ETHYL] N (2 PYRIDYL)CYCLOHEXANECARBOXAMIDE; N METHYL DEXTRO ASPARTIC ACID; NORADRENALIN; PROPENTOFYLLINE; PROPIONYLISOLEUCYLISOLEUCYLGLYCYLLEUCINE; PROTEIN ANTIBODY; REPINOTAN; SEROTONIN 1A AGONIST; TETRAPEPTIDE; UNCLASSIFIED DRUG;

EID: 0033740610     PISSN: 03341763     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (116)

References (448)
  • 13
    • 0028980467 scopus 로고
    • β-Amyloid peptide fragment 25-35 potentiates the calcium-dependent release of excitatory amino acids from depolarized hippocampal slices
    • (1995) J Neurosci Res , vol.41 , pp. 561-566
    • Arias, C.1    Arrieta, I.2    Tapia, R.3
  • 21
    • 0025779179 scopus 로고
    • Solution structures of β peptide and its constituent fragments: Relation to amyloid deposition
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 22
    • 0030271381 scopus 로고    scopus 로고
    • Combination therapy with MK-801 and α-tert-butyl-nitrone enhances protection against ischemic neuronal damage in organotypic hippocampal slice cultures
    • (1996) Exp Neurol , vol.141 , pp. 330-336
    • Barth, A.1    Barth, L.2    Newell, D.W.3
  • 24
    • 0030728765 scopus 로고    scopus 로고
    • Amyloid β-protein toxicity and oxidative stress in Alzheimer's disease
    • (1997) Cell Tissue Res , vol.290 , pp. 471-480
    • Behl, C.1
  • 25
    • 0032418502 scopus 로고    scopus 로고
    • Effects of glucocorticoids on oxidative stree-induced hippocampal cell death: Implications for the pathogenesis of Alzheimer's disease
    • (1998) Exp Gerontol , vol.33 , pp. 689-696
    • Behl, C.1
  • 26
    • 0032890439 scopus 로고    scopus 로고
    • Alzheimer's disease and oxidative stress: Implications for novel therapeutic approaches
    • (1999) Prog Neurobiol , vol.57 , pp. 301-323
    • Behl, C.1
  • 34
    • 0031593606 scopus 로고    scopus 로고
    • Simulation of cortical cholinergic deficits - A novel experimental approach to study pathogenetic aspects of Alzheimer's disease
    • (1998) J Neural Transm , vol.54 , Issue.SUPPL. , pp. 237-247
    • Bigl, V.1    Schliebs, R.2
  • 41
    • 0032450937 scopus 로고    scopus 로고
    • Age-related toxicity to lactate, glutamate and β-amyloid in cultured adult neurons
    • (1998) Neurobiol Aging , vol.19 , pp. 561-568
    • Brewer, G.J.1
  • 45
    • 0019497412 scopus 로고
    • A possible role of zinc in the pathology of dementia
    • (1981) Lancet , vol.1 , pp. 186-188
    • Burnet, F.M.1
  • 60
    • 0029379605 scopus 로고
    • Processing of the β-amyloid precursor protein and its regulation in Alzheimer's disease
    • (1995) J Neurochem , vol.65 , pp. 1431-1444
    • Checler, F.1
  • 61
    • 0032872131 scopus 로고    scopus 로고
    • Presenilins: Structural aspects and post-translational events
    • (1999) Mol Neurobiol , vol.19 , pp. 255-265
    • Checler, F.1
  • 63
    • 0024093449 scopus 로고
    • Glutamate neurotoxicity and diseases of the nervous system
    • (1988) Neuron , vol.1 , pp. 623-634
    • Choi, D.W.1
  • 64
    • 0030581107 scopus 로고    scopus 로고
    • Amyloidogenic processing of Alzheimer's amyloid precursor protein in vitro and its modulation by metal ions and tacrine
    • (1996) Life Sci , vol.59 , pp. 545-557
    • Chong, Y.H.1    Suh, Y.H.2
  • 75
    • 0028989045 scopus 로고
    • β-Amyloid peptides enhance binding of the calcium mobilising second messengers, inositol-(1,4,5)trisphosphate and inositol-(1,3,4,5)tetrakisphosphate to their receptor sites in rat cortical membranes
    • (1995) Neurosci Lett , vol.191 , pp. 31-34
    • Cowburn, R.F.1    Wiehager, B.2    Sundstrom, E.3
  • 76
    • 0030817292 scopus 로고    scopus 로고
    • Effects of β-amyloid-(25-35) peptides on radioligand binding to excitatory amino acid receptors and voltage-dependent calcium channels: Evidence for a selective affinity for the glutamate and glycine recognition sites of the NMDA receptor
    • (1997) Neurochem Res , vol.22 , pp. 1437-1442
    • Cowburn, R.F.1    Wiehager, B.2    Trief, E.3    Li-Li, M.4    Sundstrom, E.5
  • 82
    • 0032911170 scopus 로고    scopus 로고
    • Alzheimer's disease: Seeking new ways to preserve brain function
    • (1999) Geriatrics , vol.54 , pp. 42-47
    • Davis, K.L.1
  • 92
    • 0032589298 scopus 로고    scopus 로고
    • Sodium salicylate and 17β-estradiol attenuate nuclear transcription factor NF-κB translocation in cultured rat astroglial cultures following exposure to amyloid Aβ(1-42) and lipopolysaccharides
    • (1999) J Neurochem , vol.73 , pp. 1453-1460
    • Dodel, R.C.1    Du, Y.2    Bales, K.R.3    Gao, F.4    Paul, S.M.5
  • 94
    • 0033535629 scopus 로고    scopus 로고
    • Stimulation of the 5-HT(1A) receptor selectively suppresses NMDA receptor-mediated synaptic excitation in the rat visual cortex
    • (1999) Brain Res , vol.827 , pp. 225-228
    • Edagawa, Y.1    Saito, H.2    Abe, K.3
  • 96
    • 0007250753 scopus 로고    scopus 로고
    • Gene induction and neuronal apoptosis
    • Mattson MP, ed. Neuroprotective Signal Transduction. Totowa, NJ: Humana Press
    • (1998) , pp. 83-94
    • Estus, S.1
  • 117
    • 0018868515 scopus 로고
    • Amyloid deposits and amyloidosis. The β-fibrilloses (Part I and II)
    • (1980) N Engl J Med , vol.302 , pp. 1333-1343
    • Glenner, G.G.1
  • 121
    • 0030050677 scopus 로고    scopus 로고
    • + channel openers protect hippocampal neurons against oxidative injury and amyloid β-peptide toxicity
    • (1996) Brain Res , vol.706 , pp. 328-332
    • Goodman, Y.1    Mattson, M.P.2
  • 126
    • 0031555397 scopus 로고    scopus 로고
    • Low concentrations of estradiol reduce β-amyloid(25-35)-induced toxicity, lipid peroxidation and glucose utilization in human SK-N-SH neuroblastoma cells
    • (1997) Brain Res , vol.778 , pp. 158-165
    • Gridley, K.E.1    Green, P.S.2    Simpkins, J.W.3
  • 134
    • 0027333557 scopus 로고
    • Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Haass, C.1    Selkoe, D.J.2
  • 137
    • 0032876784 scopus 로고    scopus 로고
    • Activation of cascapse-3 in β-amyloid-induced apoptosis of cultured rat cortical neurons
    • (1999) Brain Res , vol.842 , pp. 311-323
    • Harada, J.1    Sugimoto, M.2
  • 149
    • 0034117262 scopus 로고    scopus 로고
    • β-Amyloid excitotoxicity in rat magnocellular nucleus basalis: Effect of cortical deafferentation on cerebral blood flow regulation and implications for Alzheimer's disease
    • (2000) Ann NY Acad Sci , vol.903 , pp. 374-386
    • Harkany, T.1    Penke, B.2    Luiten, P.G.M.3
  • 150
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • (1997) Ann Rev Neurosci , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury P.T., Jr.2
  • 163
    • 0344936729 scopus 로고    scopus 로고
    • Possible causes of Alzheimer's disease: Amyloid fragments, free radicals and calcium homeostasis
    • (1998) Neurobiol Dis , vol.5 , pp. 129-141
    • Holscher, C.1
  • 182
    • 0027006436 scopus 로고
    • Amyloid fibril formation requires a chemically discriminating nucleation event: Studies of an amyloidogenic sequence from the bacterial protein OsmB
    • (1992) Biochemistry , vol.31 , pp. 12345-12352
    • Jarrett, J.T.1    Lansbury P.T., Jr.2
  • 183
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, J.R.2
  • 198
    • 0031840571 scopus 로고    scopus 로고
    • Roles of lipid peroxidation in modulation of cellular signaling pathways, cell dysfunction, and death in the nervous system
    • (1998) Rev Neurosci , vol.9 , pp. 105-116
    • Keller, J.N.1    Mattson, M.P.2
  • 201
    • 0030583638 scopus 로고    scopus 로고
    • Mechanisms underlying the vascular activity of β-amyloid fragment (βA(4)25-35) at the level of skin vasculature
    • (1996) Brain Res , vol.736 , pp. 206-216
    • Khalil, Z.1    Chen, H.2    Helme, R.D.3
  • 220
    • 0028247579 scopus 로고
    • The role of glucocorticoids in brain ageing and Alzheimer's disease: An integrative physiological hypothesis
    • (1994) Exp Gerontol , vol.29 , pp. 3-11
    • Landfield, P.W.1
  • 222
    • 0007178807 scopus 로고    scopus 로고
    • 25-35 induced neurite outgrowth inhibition in vitro
    • (1998) Alz Rep , vol.1 , pp. 55-60
    • Larner, A.J.1
  • 223
    • 0032815498 scopus 로고    scopus 로고
    • Hypothesis: Amyloid β-peptides truncated at the N-terminus contribute to the pathogenesis of Alzheimer's disease
    • (1999) Neurobiol Aging , pp. 65-69
    • Larner, A.J.1
  • 228
    • 0032553350 scopus 로고    scopus 로고
    • Chronic elevation of amyloid precursor protein expression in the neocortex and hippocampus of rats with selective cholinergic lesions
    • (1998) Neurosci Lett , vol.257 , pp. 53-56
    • Leanza, G.1
  • 257
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of β-amyloid precursor protein and its soluble and fibrillogenic derivatives
    • (1997) Physiol Rev , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 258
    • 0032007328 scopus 로고    scopus 로고
    • Modification of ion homeostasis by lipid peroxidation: Roles in neuronal degeneration and adaptive plasticity
    • (1998) Trends Neurosci , vol.21 , pp. 53-57
    • Mattson, M.P.1
  • 261
    • 0030611750 scopus 로고    scopus 로고
    • Activation of NF-κB protects hippocampal neurons against oxidative stress-induced apoptosis: Evidence for induction of manganese superoxide dismutase and suppression of peroxynitrite production and protein tyrosine nitration
    • (1997) J Neurosci Res , vol.49 , pp. 681-697
    • Mattson, M.P.1    Goodman, Y.2    Luo, H.3    Fu, W.4    Furukawa, K.5
  • 273
    • 0033430085 scopus 로고    scopus 로고
    • Amyloid-β binds catalase with high affinity and inhibits hydrogen peroxide breakdown
    • (1999) Biochem J , vol.344 , pp. 293-296
    • Milton, N.G.1
  • 288
    • 0032730839 scopus 로고    scopus 로고
    • Reduction in somatostatin and substance P levels and choline acetyltransferase activity in the cortex and hippocampus of the rat after chronic intracerebrovascular infusion of β-amyloid(1-40)
    • (1999) Brain Res Bull , vol.50 , pp. 251-262
    • Nag, S.1    Yee, B.K.2    Tang, F.3
  • 321
    • 0032997908 scopus 로고    scopus 로고
    • Estrogen modulates neuronal Bcl-xL expression and β-amyloid-induced apoptosis: Relevance to Alzheimer's disease
    • (1999) J Neurochem , vol.71 , pp. 1552-1563
    • Pike, C.J.1
  • 334
    • 0027198067 scopus 로고
    • Overlapping binding sites of two different transcription factors in the promoter of the human gene for the Alzheimer amyloid precursor protein
    • (1993) Biochem Biophys Res Commun , vol.190 , pp. 637-647
    • Pollwein, P.1
  • 349
    • 0002229641 scopus 로고
    • Reactive oxygen intermediates in microglial cells differentiating into brain macrophages: Depression by propentofylline and relation to adenozine action
    • Krieglstein J, Oberpichler H, eds. Pharmacology of Cerebral Ischemia. Stuttgart: Wiss. Verl. Ges.
    • (1992) , pp. 461-467
    • Schubert, P.1    Banati, R.2    Dux, E.3    Gehrmann, J.4    Rudolphi, K.5    Kreutzberg, G.W.6
  • 352
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 353
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 355
    • 0030986545 scopus 로고    scopus 로고
    • β-Amyloid and ionophore A23187 evoke τ hyperphosphorylation by distinct intracellular pathways: Differential involvement of the calpain/protein kinase C system
    • (1997) J Neurosci Res , vol.49 , pp. 759-768
    • Shea, T.B.1    Prabhakar, S.2    Ekinci, F.J.3
  • 365
    • 0031243561 scopus 로고    scopus 로고
    • Melatonin alters the metabolism of the β-amyloid precursor protein in the neuroendocrine cell line PC12
    • (1997) J Mol Neurosci , vol.9 , pp. 75-92
    • Song, W.1    Lahiri, D.K.2
  • 366
    • 0033044804 scopus 로고    scopus 로고
    • Alzheimer's and prion disease as disorders of protein conformation: Implications for the design of novel therapeutic approaches
    • (1999) J Mol Med , vol.77 , pp. 412-418
    • Soto, C.1
  • 367
    • 0032839878 scopus 로고    scopus 로고
    • Plaque busters: Strategies to inhibit amyloid formation in Alzheimer's disease
    • (1999) Mol Med Today , vol.5 , pp. 343-350
    • Soto, C.1
  • 386
    • 0033358871 scopus 로고    scopus 로고
    • Caspases land on APP: One small step for apoptosis, one giant leap for amyloidosis?
    • (1999) Nat Neurosci , vol.2 , pp. 585-586
    • Tanzi, R.E.1
  • 411
    • 0033593574 scopus 로고    scopus 로고
    • Expression of calbindin-D28k in C6 glial cells stabilizes intracellular calcium levels and protects against apoptosis induced by calcium ionophore and amyloid β-peptide
    • (1999) Mol Brain Res , vol.64 , pp. 69-79
    • Wernyj, R.P.1    Mattson, M.P.2    Christakos, C.3
  • 423
    • 0001216824 scopus 로고    scopus 로고
    • Reorganization of cholinergic terminals in the cerebral cortex and hippocampus in transgenic mice carrying mutated presenilin-1 and amyloid precursor protein transgenes
    • (1999) J Neurosci , vol.19 , pp. 2706-2716
    • Wong, T.P.1    Debeir, T.2    Duff, K.3    Cuello, A.C.4
  • 441
    • 0032936688 scopus 로고    scopus 로고
    • The antioxidant vitamin E modulates amyloid β-peptide-induced creatine kinase activity inhibition and increased protein oxidation: Implications for the free radical hypothesis of Alzheimer's disease
    • (1999) Neurochem Res , vol.24 , pp. 427-435
    • Yatin, S.M.1    Aksenov, M.2    Butterfield, D.A.3
  • 444
    • 0033015485 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: Suppression of oxidative stress and stabilization of calcium homeostasis
    • (1999) Exp Neurol , vol.155 , pp. 302-314
    • Yu, Z.1    Luo, H.2    Fu, W.3    Mattson, M.P.4
  • 445
    • 0026631361 scopus 로고
    • NMR studies of amyloid β-peptides: Proton assignments, secondary structure, and mechanism of an α-helix-β-sheet conversion for a homologous, 28-residue, N-terminal fragment
    • (1992) Biochemistry , vol.31 , pp. 5621-5631
    • Zagorski, M.G.1    Barrow, C.J.2
  • 446
    • 0032053686 scopus 로고    scopus 로고
    • Involvement of cytokines in normal CNS development and neurological diseases: Recent progress and perspectives
    • (1998) J Neurosci Res , vol.52 , pp. 7-16
    • Zhao, B.1    Schwartz, J.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.