메뉴 건너뛰기




Volumn 493, Issue 1, 2017, Pages 158-163

Memantine inhibits β-amyloid aggregation and disassembles preformed β-amyloid aggregates

Author keywords

Alzheimer's disease; A aggregation; Memantine; amyloid

Indexed keywords

AMANTADINE; AMYLOID; AMYLOID BETA PROTEIN[1-42]; MEMANTINE; THIOFLAVINE; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT; PROTEIN BINDING;

EID: 85029525450     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2017.09.058     Document Type: Article
Times cited : (24)

References (38)
  • 1
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics
    • Selkoe, D.J., Schenk, D., Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics. Annu. Rev. Pharmacol. Toxicol. 43 (2003), 545–584.
    • (2003) Annu. Rev. Pharmacol. Toxicol. , vol.43 , pp. 545-584
    • Selkoe, D.J.1    Schenk, D.2
  • 2
    • 84963520567 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease at 25 years
    • Selkoe, D.J., Hardy, J., The amyloid hypothesis of Alzheimer's disease at 25 years. EMBO Mol. Med. 8 (2016), 595–608.
    • (2016) EMBO Mol. Med. , vol.8 , pp. 595-608
    • Selkoe, D.J.1    Hardy, J.2
  • 3
    • 85009204333 scopus 로고    scopus 로고
    • Aberrant proteolytic processing and therapeutic strategies in Alzheimer disease
    • Tomita, T., Aberrant proteolytic processing and therapeutic strategies in Alzheimer disease. Adv. Biol. Regul. 64 (2017), 33–38.
    • (2017) Adv. Biol. Regul. , vol.64 , pp. 33-38
    • Tomita, T.1
  • 4
    • 85020437815 scopus 로고    scopus 로고
    • Dysregulated metabolism of the amyloid-β protein and therapeutic approaches in Alzheimer disease
    • in press
    • Kikuchi, K., Kidana, K., Tatebe, T., et al. Dysregulated metabolism of the amyloid-β protein and therapeutic approaches in Alzheimer disease. J. Cell Biochem., 2017 in press.
    • (2017) J. Cell Biochem.
    • Kikuchi, K.1    Kidana, K.2    Tatebe, T.3
  • 5
    • 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., et al. 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 13 (1994), 45–53.
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3
  • 6
    • 12644258498 scopus 로고    scopus 로고
    • The presenilin 2 mutation (N141I) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid beta protein ending at the 42nd (or 43rd) residue
    • Tomita, T., Maruyama, K., Saido, T.C., et al. The presenilin 2 mutation (N141I) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid beta protein ending at the 42nd (or 43rd) residue. Proc. Natl. Acad. Sci. U. S. A. 94 (1997), 2025–2030.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2025-2030
    • Tomita, T.1    Maruyama, K.2    Saido, T.C.3
  • 7
    • 0028973637 scopus 로고
    • Amyloid β-protein ending at Thr43 is a minor component of some diffuse plaques in the Alzheimer's disease brain, but is not found in cerebrovascular amyloid
    • Iizuka, T., Shoji, M., Harigaya, Y., et al. Amyloid β-protein ending at Thr43 is a minor component of some diffuse plaques in the Alzheimer's disease brain, but is not found in cerebrovascular amyloid. Brain Res. 702 (1995), 275–278.
    • (1995) Brain Res. , vol.702 , pp. 275-278
    • Iizuka, T.1    Shoji, M.2    Harigaya, Y.3
  • 8
    • 0034747316 scopus 로고    scopus 로고
    • Correlation between Aßx-40-, Aßx-42- and Aßx-43-containing amyloid plaques and cognitive decline
    • Parvathy, S., Davies, P., Haroutunian, V., et al. Correlation between Aßx-40-, Aßx-42- and Aßx-43-containing amyloid plaques and cognitive decline. Arch. Neurol. 58 (2001), 2025–2032.
    • (2001) Arch. Neurol. , vol.58 , pp. 2025-2032
    • Parvathy, S.1    Davies, P.2    Haroutunian, V.3
  • 9
    • 67649488309 scopus 로고    scopus 로고
    • Aβ43 is more frequent than Aβ40 in amyloid plaque cores from Alzheimer disease brains
    • Welander, H., Frånberg, J., Graff, C., et al. Aβ43 is more frequent than Aβ40 in amyloid plaque cores from Alzheimer disease brains. J. Neurochem. 110 (2009), 697–706.
    • (2009) J. Neurochem. , vol.110 , pp. 697-706
    • Welander, H.1    Frånberg, J.2    Graff, C.3
  • 10
    • 79960819248 scopus 로고    scopus 로고
    • Potent amyloidogenicity and pathogenicity of Aβ43
    • Saito, T., Suemoto, T., Brouwers, N., et al. Potent amyloidogenicity and pathogenicity of Aβ43. Nat. Neurosci. 14 (2011), 1023–1032.
    • (2011) Nat. Neurosci. , vol.14 , pp. 1023-1032
    • Saito, T.1    Suemoto, T.2    Brouwers, N.3
  • 11
    • 0028855851 scopus 로고
    • Dominant and differential deposition of distinct beta-amyloid peptide species, A beta N3(pE), in senile plaques
    • Saido, T.C., Iwatsubo, T., Mann, D.M., et al. Dominant and differential deposition of distinct beta-amyloid peptide species, A beta N3(pE), in senile plaques. Neuron 14 (1995), 457–466.
    • (1995) Neuron , vol.14 , pp. 457-466
    • Saido, T.C.1    Iwatsubo, T.2    Mann, D.M.3
  • 12
    • 0026879650 scopus 로고
    • Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the beta-amyloid precursor protein gene
    • Hendriks, L., van Duijn, C.M., Cras, P., et al. Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the beta-amyloid precursor protein gene. Nat. Genet. 1 (1992), 218–221.
    • (1992) Nat. Genet. , vol.1 , pp. 218-221
    • Hendriks, L.1    van Duijn, C.M.2    Cras, P.3
  • 13
    • 8644275574 scopus 로고    scopus 로고
    • Hemorrhage is uncommon in new Alzheimer family with Flemish amyloid precursor protein mutation
    • Brooks, W.S., Kwok, J.B., Halliday, G.M., et al. Hemorrhage is uncommon in new Alzheimer family with Flemish amyloid precursor protein mutation. Neurology 9 (2004), 1613–1617.
    • (2004) Neurology , vol.9 , pp. 1613-1617
    • Brooks, W.S.1    Kwok, J.B.2    Halliday, G.M.3
  • 14
    • 76249118271 scopus 로고    scopus 로고
    • An APP inhibitory domain containing the Flemish mutation residue modulates gamma-secretase activity for Abeta production
    • Tian, Y., Bassit, B., Chau, D., et al. An APP inhibitory domain containing the Flemish mutation residue modulates gamma-secretase activity for Abeta production. Nat. Struct. Mol. Biol. 17 (2010), 151–158.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 151-158
    • Tian, Y.1    Bassit, B.2    Chau, D.3
  • 15
    • 0037469171 scopus 로고    scopus 로고
    • Early onset familial Alzheimer's disease: mutation frequency in 31 families
    • Janssen, J.C., Beck, J.A., Campbell, T.A., et al. Early onset familial Alzheimer's disease: mutation frequency in 31 families. Neurology 28 (2003), 235–239.
    • (2003) Neurology , vol.28 , pp. 235-239
    • Janssen, J.C.1    Beck, J.A.2    Campbell, T.A.3
  • 16
    • 33947505097 scopus 로고    scopus 로고
    • The Tottori (D7N) and English (H6R) familial Alzheimer disease mutations accelerate Abeta fibril formation without increasing protofibril formation
    • Hori, Y., Hashimoto, T., Wakutani, Y., et al. The Tottori (D7N) and English (H6R) familial Alzheimer disease mutations accelerate Abeta fibril formation without increasing protofibril formation. J. Biol. Chem. 16 (2007), 4916–4923.
    • (2007) J. Biol. Chem. , vol.16 , pp. 4916-4923
    • Hori, Y.1    Hashimoto, T.2    Wakutani, Y.3
  • 17
    • 0242580170 scopus 로고    scopus 로고
    • Neurotoxicity and physicochemical properties of Abeta mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease
    • Murakami, K., Irie, K., Morimoto, A., et al. Neurotoxicity and physicochemical properties of Abeta mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease. J. Biol. Chem. 278 (2003), 46179–46187.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46179-46187
    • Murakami, K.1    Irie, K.2    Morimoto, A.3
  • 18
    • 17944368176 scopus 로고    scopus 로고
    • The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation
    • Nilsberth, C., Westlind-Danielsson, A., Eckman, C.B., et al. The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation. Nat. Neurosci. 4 (2001), 887–893.
    • (2001) Nat. Neurosci. , vol.4 , pp. 887-893
    • Nilsberth, C.1    Westlind-Danielsson, A.2    Eckman, C.B.3
  • 19
    • 0025296269 scopus 로고
    • Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type
    • Levy, E., Carman, M.D., Fernandez-Madrid, I.J., et al. Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type. Science 248 (1990), 1124–1126.
    • (1990) Science , vol.248 , pp. 1124-1126
    • Levy, E.1    Carman, M.D.2    Fernandez-Madrid, I.J.3
  • 20
    • 0019979780 scopus 로고
    • Familial cerebral amyloid angiopathy presenting as recurrent cerebral haemorrhage
    • Wattendorff, A.R., Bots, G.T., Went, L.N., et al. Familial cerebral amyloid angiopathy presenting as recurrent cerebral haemorrhage. J. Neurol. Sci. 55 (1982), 121–135.
    • (1982) J. Neurol. Sci. , vol.55 , pp. 121-135
    • Wattendorff, A.R.1    Bots, G.T.2    Went, L.N.3
  • 21
    • 0025720097 scopus 로고
    • Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine for glutamic acid substitution have accelerated amyloid fibril formation
    • Wisniewski, T., Ghiso, J., Frangione, B., Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine for glutamic acid substitution have accelerated amyloid fibril formation. Biochem. Biophys. Res. Commun., 180, 1991, 1528.
    • (1991) Biochem. Biophys. Res. Commun. , vol.180 , pp. 1528
    • Wisniewski, T.1    Ghiso, J.2    Frangione, B.3
  • 22
    • 0034982951 scopus 로고    scopus 로고
    • Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy
    • Grabowski, T.J., Cho, H.S., Vonsattel, J.P., et al. Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy. Ann. Neurol. 49 (2001), 697–705.
    • (2001) Ann. Neurol. , vol.49 , pp. 697-705
    • Grabowski, T.J.1    Cho, H.S.2    Vonsattel, J.P.3
  • 23
    • 0036447753 scopus 로고    scopus 로고
    • Pathogenic effects of cerebral amyloid angiopathy mutations in the amyloid beta-protein precursor
    • Van Nostrand, W.E., Melchor, J.P., Romanov, G., et al. Pathogenic effects of cerebral amyloid angiopathy mutations in the amyloid beta-protein precursor. Ann. N. Y. Acad. Sci. 977 (2002), 258–265.
    • (2002) Ann. N. Y. Acad. Sci. , vol.977 , pp. 258-265
    • Van Nostrand, W.E.1    Melchor, J.P.2    Romanov, G.3
  • 24
    • 0002329070 scopus 로고    scopus 로고
    • A new βPP mutation related to hereditary cerebral haemorrhage
    • Tagliavini, F., Rossi, G., Padovani, A., et al. A new βPP mutation related to hereditary cerebral haemorrhage. Alzheimer's Rep., 2, 1999, S28.
    • (1999) Alzheimer's Rep. , vol.2 , pp. S28
    • Tagliavini, F.1    Rossi, G.2    Padovani, A.3
  • 25
    • 0032892343 scopus 로고
    • Memantine is a clinically well tolerated N-methyl-D-aspartate (NMDA) receptor antagonist—a review of preclinical data
    • Parsons, C.G., Danysz, W., Quack, G., Memantine is a clinically well tolerated N-methyl-D-aspartate (NMDA) receptor antagonist—a review of preclinical data. Neuropharmacology 38 (1993), 735–767.
    • (1993) Neuropharmacology , vol.38 , pp. 735-767
    • Parsons, C.G.1    Danysz, W.2    Quack, G.3
  • 26
    • 33748775469 scopus 로고    scopus 로고
    • Cognitive dysfunction induced by sequential injection of amyloid-beta and ibotenate into the bilateral hippocampus; protection by memantine and MK-801
    • Nakamura, S., Murayama, N., Noshita, T., et al. Cognitive dysfunction induced by sequential injection of amyloid-beta and ibotenate into the bilateral hippocampus; protection by memantine and MK-801. Eur. J. Pharmacol. 548 (2006), 115–122.
    • (2006) Eur. J. Pharmacol. , vol.548 , pp. 115-122
    • Nakamura, S.1    Murayama, N.2    Noshita, T.3
  • 27
    • 79955746908 scopus 로고    scopus 로고
    • The basal forebrain cholinergic system in aging and dementia. Rescuing cholinergic neurons from neurotoxic amyloid-β42 with memantine
    • Nyakas, C., Granic, I., Halmy, L.G., et al. The basal forebrain cholinergic system in aging and dementia. Rescuing cholinergic neurons from neurotoxic amyloid-β42 with memantine. Behav. Brain Res. 221 (2011), 594–603.
    • (2011) Behav. Brain Res. , vol.221 , pp. 594-603
    • Nyakas, C.1    Granic, I.2    Halmy, L.G.3
  • 28
    • 57049085109 scopus 로고    scopus 로고
    • Memantine leads to behavioral improvement and amyloid reduction in Alzheimer's-disease-model transgenic mice shown as by micromagnetic resonance imaging
    • Scholtzova, H., Wadghiri, Y.Z., Douadi, M., et al. Memantine leads to behavioral improvement and amyloid reduction in Alzheimer's-disease-model transgenic mice shown as by micromagnetic resonance imaging. J. Neurosci. Res. 86 (2008), 2784–2791.
    • (2008) J. Neurosci. Res. , vol.86 , pp. 2784-2791
    • Scholtzova, H.1    Wadghiri, Y.Z.2    Douadi, M.3
  • 29
    • 73949151820 scopus 로고    scopus 로고
    • Memantine lowers amyloid-beta peptide levels in neuronal cultures and in APP/PS1 transgenic mice
    • Alley, G.M., Bailey, J.A., Chen, D., et al. Memantine lowers amyloid-beta peptide levels in neuronal cultures and in APP/PS1 transgenic mice. J. Neurosci. Res. 88 (2010), 143–154.
    • (2010) J. Neurosci. Res. , vol.88 , pp. 143-154
    • Alley, G.M.1    Bailey, J.A.2    Chen, D.3
  • 30
    • 57349119307 scopus 로고    scopus 로고
    • Effects of memantine on neuronal structure and conditioned fear in the Tg2576 mouse model of Alzheimer's disease
    • Dong, H., Yuede, C.M., Coughlan, C., et al. Effects of memantine on neuronal structure and conditioned fear in the Tg2576 mouse model of Alzheimer's disease. Neuropsychopharmacology 33 (2008), 3226–3236.
    • (2008) Neuropsychopharmacology , vol.33 , pp. 3226-3236
    • Dong, H.1    Yuede, C.M.2    Coughlan, C.3
  • 31
    • 76149120867 scopus 로고    scopus 로고
    • Memantine improves cognition and reduces Alzheimer's-like neuropathology in transgenic mice
    • Martinez-Coria, H., Green, K.N., Billings, L.M., et al. Memantine improves cognition and reduces Alzheimer's-like neuropathology in transgenic mice. Am. J. Pathol. 176 (2010), 870–880.
    • (2010) Am. J. Pathol. , vol.176 , pp. 870-880
    • Martinez-Coria, H.1    Green, K.N.2    Billings, L.M.3
  • 32
    • 85012113377 scopus 로고    scopus 로고
    • Memantine reduces the production of amyloid-β peptides through modulation of amyloid precursor protein trafficking
    • Ito, K., Tatebe, T., Suzuki, K., et al. Memantine reduces the production of amyloid-β peptides through modulation of amyloid precursor protein trafficking. Eur. J. Pharmacol. 798 (2017), 16–25.
    • (2017) Eur. J. Pharmacol. , vol.798 , pp. 16-25
    • Ito, K.1    Tatebe, T.2    Suzuki, K.3
  • 33
    • 78649474332 scopus 로고    scopus 로고
    • Monoclonal antibody against the turn of the 42-residue amyloid β-protein at positions 22 and 23
    • Murakami, K., Horikoshi-Sakuraba, Y., Murata, N., et al. Monoclonal antibody against the turn of the 42-residue amyloid β-protein at positions 22 and 23. ACS Chem. Neurosci. 1 (2010), 747–756.
    • (2010) ACS Chem. Neurosci. , vol.1 , pp. 747-756
    • Murakami, K.1    Horikoshi-Sakuraba, Y.2    Murata, N.3
  • 34
    • 84969443567 scopus 로고    scopus 로고
    • Intracellular amyloid β oligomers impair organelle transport and induce dendritic spine loss in primary neurons
    • Umeda, T., Ramser, E.M., Yamashita, M., et al. Intracellular amyloid β oligomers impair organelle transport and induce dendritic spine loss in primary neurons. Acta Neuropathol. Commun., 3, 2015, 51.
    • (2015) Acta Neuropathol. Commun. , vol.3 , pp. 51
    • Umeda, T.1    Ramser, E.M.2    Yamashita, M.3
  • 35
    • 14844303721 scopus 로고    scopus 로고
    • Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins
    • Taniguchi, S., Suzuki, N., Masuda, M., et al. Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins. J. Biol. Chem. 280 (2005), 7614–7623.
    • (2005) J. Biol. Chem. , vol.280 , pp. 7614-7623
    • Taniguchi, S.1    Suzuki, N.2    Masuda, M.3
  • 36
    • 0029085113 scopus 로고
    • Cerebrospinal fluid and serum concentrations of the N-methyl-D-aspartate (NMDA) receptor antagonist memantine in man
    • Kornhuber, J., Quack, G., Cerebrospinal fluid and serum concentrations of the N-methyl-D-aspartate (NMDA) receptor antagonist memantine in man. Neurosci. Lett. 195 (1995), 137–139.
    • (1995) Neurosci. Lett. , vol.195 , pp. 137-139
    • Kornhuber, J.1    Quack, G.2
  • 37
    • 84865529158 scopus 로고    scopus 로고
    • Clinical and biomarker changes in dominantly inherited Alzheimer's disease
    • Bateman, R.J., Xiong, C., Benzinger, T.L., et al. Clinical and biomarker changes in dominantly inherited Alzheimer's disease. N. Engl. J. Med. 367 (2012), 795–804.
    • (2012) N. Engl. J. Med. , vol.367 , pp. 795-804
    • Bateman, R.J.1    Xiong, C.2    Benzinger, T.L.3
  • 38
    • 84888201046 scopus 로고    scopus 로고
    • Longitudinal change in CSF Tau and Aβ biomarkers for up to 48 months in ADNI
    • Toledo, J.B., Xie, S.X., Trojanowski, J.Q., et al. Longitudinal change in CSF Tau and Aβ biomarkers for up to 48 months in ADNI. Acta Neuropathol. 126 (2013), 659–670.
    • (2013) Acta Neuropathol. , vol.126 , pp. 659-670
    • Toledo, J.B.1    Xie, S.X.2    Trojanowski, J.Q.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.