메뉴 건너뛰기




Volumn 178, Issue 1, 2011, Pages 140-149

Actions of β-amyloid protein on human neurons are expressed through the amylin receptor

Author keywords

[No Author keywords available]

Indexed keywords

AC253; AMYLIN; AMYLOID BETA PROTEIN[1-42]; CASPASE 6; CASPASE 9; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 79251473696     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.1016/j.ajpath.2010.11.022     Document Type: Article
Times cited : (75)

References (47)
  • 1
    • 56349116391 scopus 로고    scopus 로고
    • Molecular genetics of Alzheimer's disease: An update
    • Brouwers N, Sleegers K, Van Broeckhoven C: Molecular genetics of Alzheimer's disease: an update. Ann Med 2008, 40:562-583
    • (2008) Ann Med , vol.40 , pp. 562-583
    • Brouwers, N.1    Sleegers, K.2    Van Broeckhoven, C.3
  • 2
    • 64149132721 scopus 로고    scopus 로고
    • Amyloid beta-protein toxicity and the pathogenesis of Alzheimer disease
    • Yankner BA, Lu T: Amyloid beta-protein toxicity and the pathogenesis of Alzheimer disease. J Biol Chem 2009, 284:4755-4759
    • (2009) J Biol Chem , vol.284 , pp. 4755-4759
    • Yankner, B.A.1    Lu, T.2
  • 4
    • 38349143353 scopus 로고    scopus 로고
    • RAGE: A potential target for Abeta-mediated cellular perturbation in Alzheimer's disease
    • Chen X, Walker DG, Schmidt AM, Arancio O, Lue LF, Yan SD: RAGE: a potential target for Abeta-mediated cellular perturbation in Alzheimer's disease. Curr Mol Med 2007, 7:735-742
    • (2007) Curr Mol Med , vol.7 , pp. 735-742
    • Chen, X.1    Walker, D.G.2    Schmidt, A.M.3    Arancio, O.4    Lue, L.F.5    Yan, S.D.6
  • 5
    • 61349088546 scopus 로고    scopus 로고
    • Inflammation in Alzheimer's disease: Amyloid-beta oligomers trigger innate immunity defence via pattern recognition receptors
    • Salminen A, Ojala J, Kauppinen A, Kaarniranta K, Suuronen T: Inflammation in Alzheimer's disease: amyloid-beta oligomers trigger innate immunity defence via pattern recognition receptors. Prog Neurobiol 2009, 87:181-194
    • (2009) Prog Neurobiol , vol.87 , pp. 181-194
    • Salminen, A.1    Ojala, J.2    Kauppinen, A.3    Kaarniranta, K.4    Suuronen, T.5
  • 7
    • 77949681543 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor interaction with beta-amyloid: Molecular, cellular, and physiological consequences
    • Parri RH, Dineley TK: Nicotinic acetylcholine receptor interaction with beta-amyloid: molecular, cellular, and physiological consequences. Curr Alzheimer Res 2010, 7:27-39
    • (2010) Curr Alzheimer Res , vol.7 , pp. 27-39
    • Parri, R.H.1    Dineley, T.K.2
  • 8
    • 65549084830 scopus 로고    scopus 로고
    • Defining pre-synaptic nicotinic receptors regulated by beta amyloid in mouse cortex and hippocampus with receptor null mutants
    • Mehta TK, Dougherty JJ, Wu J, Choi CH, Khan GM, Nichols RA: Defining pre-synaptic nicotinic receptors regulated by beta amyloid in mouse cortex and hippocampus with receptor null mutants. J Neurochem 2009, 109:1452-1458
    • (2009) J Neurochem , vol.109 , pp. 1452-1458
    • Mehta, T.K.1    Dougherty, J.J.2    Wu, J.3    Choi, C.H.4    Khan, G.M.5    Nichols, R.A.6
  • 9
    • 33747104566 scopus 로고    scopus 로고
    • Links between Alzheimer's disease and diabetes
    • (Barc)
    • Sun MK, Alkon DL: Links between Alzheimer's disease and diabetes. Drugs Today (Barc) 2006, 42:481-489
    • (2006) Drugs Today , vol.42 , pp. 481-489
    • Sun, M.K.1    Alkon, D.L.2
  • 10
    • 34147173277 scopus 로고    scopus 로고
    • Insulin resistance and Alzheimer's disease pathogenesis: Potential mechanisms and implications for treatment
    • Craft S: Insulin resistance and Alzheimer's disease pathogenesis: potential mechanisms and implications for treatment. Curr Alzheimer Res 2007, 4:147-152
    • (2007) Curr Alzheimer Res , vol.4 , pp. 147-152
    • Craft, S.1
  • 11
    • 36448936053 scopus 로고    scopus 로고
    • Common pathological processes in Alzheimer disease and type 2 diabetes: A review
    • Lin L, Hölscher C: Common pathological processes in Alzheimer disease and type 2 diabetes: a review. Brain Res Rev 2007, 56:384-402
    • (2007) Brain Res Rev , vol.56 , pp. 384-402
    • Lin, L.1    Hölscher, C.2
  • 12
    • 0023579739 scopus 로고
    • Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients
    • Cooper GJ, Willis AC, Clark A, Turner RC, Sim RB, Reid KB: Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc Natl Acad Sci USA 1987, 84:8628-8632
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8628-8632
    • Cooper, G.J.1    Willis, A.C.2    Clark, A.3    Turner, R.C.4    Sim, R.B.5    Reid, K.B.6
  • 13
    • 0027490362 scopus 로고
    • Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membrane
    • Arispe N, Pollard HB, Rojas E: Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membrane. Proc Natl Acad Sci USA 1993, 90:10573-10577
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10573-10577
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 14
    • 0027434987 scopus 로고
    • Neurotoxicity of human amylin in rat primary hippocampal cultures: Similarity to Alzheimer's disease amyloid- Beta neurotoxicity
    • May PC, Boggs LN, Fuson KS: Neurotoxicity of human amylin in rat primary hippocampal cultures: similarity to Alzheimer's disease amyloid- beta neurotoxicity. J Neurochem 1993, 61:2330-2333
    • (1993) J Neurochem , vol.61 , pp. 2330-2333
    • May, P.C.1    Boggs, L.N.2    Fuson, K.S.3
  • 15
    • 0031754613 scopus 로고    scopus 로고
    • Human amylin induces "apoptotic" pattern of gene expression concomitant with cortical neuronal atrophy
    • Tucker HM, Rydel RE, Wright S, Estus S: Human amylin induces "apoptotic" pattern of gene expression concomitant with cortical neuronal atrophy. J Neurochem 1998, 71:506-516
    • (1998) J Neurochem , vol.71 , pp. 506-516
    • Tucker, H.M.1    Rydel, R.E.2    Wright, S.3    Estus, S.4
  • 16
    • 0034843660 scopus 로고    scopus 로고
    • Cellular mechanisms for amyloid-beta protein activation of rat cholinergic basal forebrain neurons
    • Jhamandas JH, Cho C, Jassar B, Harris K, MacTavish D, Easaw J: Cellular mechanisms for amyloid-beta protein activation of rat cholinergic basal forebrain neurons. J Neurophysiol 2001, 86:1312-1320
    • (2001) J Neurophysiol , vol.86 , pp. 1312-1320
    • Jhamandas, J.H.1    Cho, C.2    Jassar, B.3    Harris, K.4    MacTavish, D.5    Easaw, J.6
  • 17
    • 3042511642 scopus 로고    scopus 로고
    • Human amylin actions on rat cholinergic basal forebrain neurons: Antagonism of beta-amyloid effects
    • Jhamandas JH, Harris KH, Cho C, Fu W, MacTavish D: Human amylin actions on rat cholinergic basal forebrain neurons: antagonism of beta-amyloid effects. J Neurophysiol 2003, 90:3130-3136
    • (2003) J Neurophysiol , vol.90 , pp. 3130-3136
    • Jhamandas, J.H.1    Harris, K.H.2    Cho, C.3    Fu, W.4    MacTavish, D.5
  • 18
    • 44749083630 scopus 로고    scopus 로고
    • Human but not rat amylin shares neurotoxic properties with Abeta42 in long-term hippocampal and cortical cultures
    • Lim YA, Ittner LM, Lim YL, Götz J: Human but not rat amylin shares neurotoxic properties with Abeta42 in long-term hippocampal and cortical cultures. FEBS Lett 2008, 582:2188-2194
    • (2008) FEBS Lett , vol.582 , pp. 2188-2194
    • Lim, Y.A.1    Ittner, L.M.2    Lim, Y.L.3    Götz, J.4
  • 20
    • 0036266044 scopus 로고    scopus 로고
    • XXXII. The mammalian calcitonin gene-related peptides, adrenomedullin, amylin, and calcitonin receptors
    • International Union of Pharmacology.
    • Poyner DR, Sexton PM, Marshall I, Smith DM, Quirion R, Born W, Muff R, Fischer JA, Foord SM: International Union of Pharmacology. XXXII. The mammalian calcitonin gene-related peptides, adrenomedullin, amylin, and calcitonin receptors. Pharmacol Rev 2002, 54:233-246
    • (2002) Pharmacol Rev , vol.54 , pp. 233-246
    • Poyner, D.R.1    Sexton, P.M.2    Marshall, I.3    Smith, D.M.4    Quirion, R.5    Born, W.6    Muff, R.7    Fischer, J.A.8    Foord, S.M.9
  • 21
    • 33645221141 scopus 로고    scopus 로고
    • Receptor pharmacology
    • Young A: Receptor pharmacology. Adv Pharmacol 2005, 52:47-65
    • (2005) Adv Pharmacol , vol.52 , pp. 47-65
    • Young, A.1
  • 23
    • 17844365264 scopus 로고    scopus 로고
    • Pharmacological discrimination of calcitonin receptor: Receptor activity-modifying protein complexes
    • Hay DL, Christopoulos G, Christopoulos A, Poyner DR, Sexton PM: Pharmacological discrimination of calcitonin receptor: receptor activity-modifying protein complexes. Mol Pharmacol 2005, 67:1655-1665
    • (2005) Mol Pharmacol , vol.67 , pp. 1655-1665
    • Hay, D.L.1    Christopoulos, G.2    Christopoulos, A.3    Poyner, D.R.4    Sexton, P.M.5
  • 26
    • 3042593297 scopus 로고    scopus 로고
    • Antagonist of the amylin receptor blocks beta-amyloid toxicity in rat cholinergic basal forebrain neurons
    • Jhamandas JH, MacTavish D: Antagonist of the amylin receptor blocks beta-amyloid toxicity in rat cholinergic basal forebrain neurons. J Neurosci 2004, 24:5579-5584
    • (2004) J Neurosci , vol.24 , pp. 5579-5584
    • Jhamandas, J.H.1    MacTavish, D.2
  • 27
    • 0031690759 scopus 로고    scopus 로고
    • Neuronal death induced by brainderived human immunodeficiency virus type 1 envelope genes differs between demented and nondemented AIDS patients
    • Power C, McArthur JC, Nath A, Wehrly K, Mayne M, Nishio J, Langelier T, Johnson RT, Chesebro B: Neuronal death induced by brainderived human immunodeficiency virus type 1 envelope genes differs between demented and nondemented AIDS patients. J Virol 1998, 72:9045-9053
    • (1998) J Virol , vol.72 , pp. 9045-9053
    • Power, C.1    McArthur, J.C.2    Nath, A.3    Wehrly, K.4    Mayne, M.5    Nishio, J.6    Langelier, T.7    Johnson, R.T.8    Chesebro, B.9
  • 28
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis
    • Stine WB Jr, Dahlgren KN, Krafft GA, LaDu MJ: In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis. J Biol Chem 2003, 278:11612-11622
    • (2003) J Biol Chem , vol.278 , pp. 11612-11622
    • Stine Jr., W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    LaDu, M.J.4
  • 29
    • 14744283139 scopus 로고    scopus 로고
    • Differential effects of oligomeric and fibrillar amyloid-beta 1-42 on astrocyte-mediated inflammation
    • White JA, Manelli AM, Holmberg KH, Van Eldik LJ, Ladu MJ: Differential effects of oligomeric and fibrillar amyloid-beta 1-42 on astrocyte-mediated inflammation. Neurobiol Dis 2005, 18:459-465
    • (2005) Neurobiol Dis , vol.18 , pp. 459-465
    • White, J.A.1    Manelli, A.M.2    Holmberg, K.H.3    Van Eldik, L.J.4    Ladu, M.J.5
  • 30
    • 30744448642 scopus 로고    scopus 로고
    • Galanin attenuates betaamyloid (Abeta) toxicity in rat cholinergic basal forebrain neurons
    • Ding X, MacTavish D, Kar S, Jhamandas JH: Galanin attenuates betaamyloid (Abeta) toxicity in rat cholinergic basal forebrain neurons. Neurobiol Dis 2006, 21:413-420
    • (2006) Neurobiol Dis , vol.21 , pp. 413-420
    • Ding, X.1    MacTavish, D.2    Kar, S.3    Jhamandas, J.H.4
  • 31
    • 0033052957 scopus 로고    scopus 로고
    • Actions of amylin on subfornical organ neurons and on drinking behaviour in rats
    • Riediger T, Rauch M, Schmid HA: Actions of amylin on subfornical organ neurons and on drinking behaviour in rats. Am J Physiol 1999, 276:R514-521
    • (1999) Am J Physiol , vol.276
    • Riediger, T.1    Rauch, M.2    Schmid, H.A.3
  • 32
    • 0026570528 scopus 로고
    • Beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson MP, Cheng B, Davis D, Bryant K, Lieberburg I, Rydel RE: beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J Neurosci 1992, 12:376-389
    • (1992) J Neurosci , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 36
    • 0034641936 scopus 로고    scopus 로고
    • Apoptosis in the nervous system
    • Yuan J, Yankner BA: Apoptosis in the nervous system. Nature 2000, 407:802-809
    • (2000) Nature , vol.407 , pp. 802-809
    • Yuan, J.1    Yankner, B.A.2
  • 37
    • 2442621492 scopus 로고    scopus 로고
    • Role of AIF in caspase-dependent and caspase-independent cell death
    • Cregan SP, Dawson VL, Slack RS: Role of AIF in caspase-dependent and caspase-independent cell death. Oncogene 2004, 23: 2785-2796
    • (2004) Oncogene , vol.23 , pp. 2785-2796
    • Cregan, S.P.1    Dawson, V.L.2    Slack, R.S.3
  • 39
    • 33750292972 scopus 로고    scopus 로고
    • Cell death in the nervous system
    • Bredesen DE, Rao RV, Mehlen P: Cell death in the nervous system. Nature 2006, 443:796-802
    • (2006) Nature , vol.443 , pp. 796-802
    • Bredesen, D.E.1    Rao, R.V.2    Mehlen, P.3
  • 40
    • 33847134493 scopus 로고    scopus 로고
    • Apoptosis-inducing factor: A matter of neuron life and death
    • Krantic S, Mechawar N, Reix S, Quirion R: Apoptosis-inducing factor: a matter of neuron life and death. Prog Neurobiol 2007, 81:179-196
    • (2007) Prog Neurobiol , vol.81 , pp. 179-196
    • Krantic, S.1    Mechawar, N.2    Reix, S.3    Quirion, R.4
  • 42
    • 67349112388 scopus 로고    scopus 로고
    • Common features between diabetes mellitus and Alzheimer's disease
    • Götz J, Ittner LM, Lim YA: Common features between diabetes mellitus and Alzheimer's disease. Cell Mol Life Sci 2009, 66:1321-1325
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1321-1325
    • Götz, J.1    Ittner, L.M.2    Lim, Y.A.3
  • 44
    • 0142026832 scopus 로고    scopus 로고
    • Potential roles of insulin and IGF-1 in Alzheimer's disease
    • Gasparini L, Xu H: Potential roles of insulin and IGF-1 in Alzheimer's disease. Trends Neurosci 2003, 26:404-406
    • (2003) Trends Neurosci , vol.26 , pp. 404-406
    • Gasparini, L.1    Xu, H.2
  • 47
    • 0028065142 scopus 로고
    • Analysis of microtubule-associated protein tau glycation in paired helical filaments
    • Ledesma MD, Bonay P, Colaço C, Avila J: Analysis of microtubule-associated protein tau glycation in paired helical filaments. J Biol Chem 1994, 269:21614-21619 (Pubitemid 24274797)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.34 , pp. 21614-21619
    • Ledesma, M.D.1    Bonay, P.2    Colaco, C.3    Avila, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.