Brain amyloid-β oligomers in ageing and Alzheimer’s disease
Alzheimer’s disease begins about two decades before the onset of symptoms or neuron death, and is believed to be caused by pathogenic amyloid-β aggregates that initiate a cascade of molecular events culminating in widespread neurodegeneration. The microtubule binding protein tau may mediate the effe...
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| Published in | Brain (London, England : 1878) Vol. 136; no. 5; pp. 1383 - 1398 |
|---|---|
| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Oxford
Oxford University Press
01.05.2013
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Alzheimer’s disease begins about two decades before the onset of symptoms or neuron death, and is believed to be caused by pathogenic amyloid-β aggregates that initiate a cascade of molecular events culminating in widespread neurodegeneration. The microtubule binding protein tau may mediate the effects of amyloid-β in this cascade. Amyloid plaques comprised of insoluble, fibrillar amyloid-β aggregates are the most characteristic feature of Alzheimer’s disease. However, the correspondence between the distribution of plaques and the pattern of neurodegeneration is tenuous. This discrepancy has stimulated the investigation of other amyloid-β aggregates, including soluble amyloid-β oligomers. Different soluble amyloid-β oligomers have been studied in several mouse models, but not systematically in humans. Here, we measured three amyloid-β oligomers previously described in mouse models—amyloid-β trimers, Aβ*56 and amyloid-β dimers—in brain tissue from 75 cognitively intact individuals, ranging from young children to the elderly, and 58 impaired subjects with mild cognitive impairment or probable Alzheimer’s disease. As in mouse models, where amyloid-β trimers appear to be the fundamental amyloid-β assembly unit of Aβ*56 and are present in young mice prior to memory decline, amyloid-β trimers in humans were present in children and adolescents; their levels rose gradually with age and were significantly above baseline in subjects in their 70s. Aβ*56 levels were negligible in children and young adults, rose significantly above baseline in subjects in their 40s and increased steadily thereafter. Amyloid-β dimers were undetectable until subjects were in their 60s; their levels then increased sharply and correlated with plaque load. Remarkably, in cognitively intact individuals we found strong positive correlations between Aβ*56 and two pathological forms of soluble tau (tau-CP13 and tau-Alz50), and negative correlations between Aβ*56 and two postsynaptic proteins (drebrin and fyn kinase), but none between amyloid-β dimers or amyloid-β trimers and tau or synaptic proteins. Comparing impaired with age-matched unimpaired subjects, we found the highest levels of amyloid-β dimers, but the lowest levels of Aβ*56 and amyloid-β trimers, in subjects with probable Alzheimer’s disease. In conclusion, in cognitively normal adults Aβ*56 increased ahead of amyloid-β dimers or amyloid-β trimers, and pathological tau proteins and postsynaptic proteins correlated with Aβ*56, but not amyloid-β dimers or amyloid-β trimers. We propose that Aβ*56 may play a pathogenic role very early in the pathogenesis of Alzheimer’s disease. |
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| AbstractList | Alzheimer's disease begins about two decades before the onset of symptoms or neuron death, and is believed to be caused by pathogenic amyloid-β aggregates that initiate a cascade of molecular events culminating in widespread neurodegeneration. The microtubule binding protein tau may mediate the effects of amyloid-β in this cascade. Amyloid plaques comprised of insoluble, fibrillar amyloid-β aggregates are the most characteristic feature of Alzheimer's disease. However, the correspondence between the distribution of plaques and the pattern of neurodegeneration is tenuous. This discrepancy has stimulated the investigation of other amyloid-β aggregates, including soluble amyloid-β oligomers. Different soluble amyloid-β oligomers have been studied in several mouse models, but not systematically in humans. Here, we measured three amyloid-β oligomers previously described in mouse models-amyloid-β trimers, Aβ*56 and amyloid-β dimers-in brain tissue from 75 cognitively intact individuals, ranging from young children to the elderly, and 58 impaired subjects with mild cognitive impairment or probable Alzheimer's disease. As in mouse models, where amyloid-β trimers appear to be the fundamental amyloid-β assembly unit of Aβ*56 and are present in young mice prior to memory decline, amyloid-β trimers in humans were present in children and adolescents; their levels rose gradually with age and were significantly above baseline in subjects in their 70s. Aβ*56 levels were negligible in children and young adults, rose significantly above baseline in subjects in their 40s and increased steadily thereafter. Amyloid-β dimers were undetectable until subjects were in their 60s; their levels then increased sharply and correlated with plaque load. Remarkably, in cognitively intact individuals we found strong positive correlations between Aβ*56 and two pathological forms of soluble tau (tau-CP13 and tau-Alz50), and negative correlations between Aβ*56 and two postsynaptic proteins (drebrin and fyn kinase), but none between amyloid-β dimers or amyloid-β trimers and tau or synaptic proteins. Comparing impaired with age-matched unimpaired subjects, we found the highest levels of amyloid-β dimers, but the lowest levels of Aβ*56 and amyloid-β trimers, in subjects with probable Alzheimer's disease. In conclusion, in cognitively normal adults Aβ*56 increased ahead of amyloid-β dimers or amyloid-β trimers, and pathological tau proteins and postsynaptic proteins correlated with Aβ*56, but not amyloid-β dimers or amyloid-β trimers. We propose that Aβ*56 may play a pathogenic role very early in the pathogenesis of Alzheimer's disease.Alzheimer's disease begins about two decades before the onset of symptoms or neuron death, and is believed to be caused by pathogenic amyloid-β aggregates that initiate a cascade of molecular events culminating in widespread neurodegeneration. The microtubule binding protein tau may mediate the effects of amyloid-β in this cascade. Amyloid plaques comprised of insoluble, fibrillar amyloid-β aggregates are the most characteristic feature of Alzheimer's disease. However, the correspondence between the distribution of plaques and the pattern of neurodegeneration is tenuous. This discrepancy has stimulated the investigation of other amyloid-β aggregates, including soluble amyloid-β oligomers. Different soluble amyloid-β oligomers have been studied in several mouse models, but not systematically in humans. Here, we measured three amyloid-β oligomers previously described in mouse models-amyloid-β trimers, Aβ*56 and amyloid-β dimers-in brain tissue from 75 cognitively intact individuals, ranging from young children to the elderly, and 58 impaired subjects with mild cognitive impairment or probable Alzheimer's disease. As in mouse models, where amyloid-β trimers appear to be the fundamental amyloid-β assembly unit of Aβ*56 and are present in young mice prior to memory decline, amyloid-β trimers in humans were present in children and adolescents; their levels rose gradually with age and were significantly above baseline in subjects in their 70s. Aβ*56 levels were negligible in children and young adults, rose significantly above baseline in subjects in their 40s and increased steadily thereafter. Amyloid-β dimers were undetectable until subjects were in their 60s; their levels then increased sharply and correlated with plaque load. Remarkably, in cognitively intact individuals we found strong positive correlations between Aβ*56 and two pathological forms of soluble tau (tau-CP13 and tau-Alz50), and negative correlations between Aβ*56 and two postsynaptic proteins (drebrin and fyn kinase), but none between amyloid-β dimers or amyloid-β trimers and tau or synaptic proteins. Comparing impaired with age-matched unimpaired subjects, we found the highest levels of amyloid-β dimers, but the lowest levels of Aβ*56 and amyloid-β trimers, in subjects with probable Alzheimer's disease. In conclusion, in cognitively normal adults Aβ*56 increased ahead of amyloid-β dimers or amyloid-β trimers, and pathological tau proteins and postsynaptic proteins correlated with Aβ*56, but not amyloid-β dimers or amyloid-β trimers. We propose that Aβ*56 may play a pathogenic role very early in the pathogenesis of Alzheimer's disease. Alzheimer’s disease begins about two decades before the onset of symptoms or neuron death, and is believed to be caused by pathogenic amyloid-β aggregates that initiate a cascade of molecular events culminating in widespread neurodegeneration. The microtubule binding protein tau may mediate the effects of amyloid-β in this cascade. Amyloid plaques comprised of insoluble, fibrillar amyloid-β aggregates are the most characteristic feature of Alzheimer’s disease. However, the correspondence between the distribution of plaques and the pattern of neurodegeneration is tenuous. This discrepancy has stimulated the investigation of other amyloid-β aggregates, including soluble amyloid-β oligomers. Different soluble amyloid-β oligomers have been studied in several mouse models, but not systematically in humans. Here, we measured three amyloid-β oligomers previously described in mouse models—amyloid-β trimers, Aβ*56 and amyloid-β dimers—in brain tissue from 75 cognitively intact individuals, ranging from young children to the elderly, and 58 impaired subjects with mild cognitive impairment or probable Alzheimer’s disease. As in mouse models, where amyloid-β trimers appear to be the fundamental amyloid-β assembly unit of Aβ*56 and are present in young mice prior to memory decline, amyloid-β trimers in humans were present in children and adolescents; their levels rose gradually with age and were significantly above baseline in subjects in their 70s. Aβ*56 levels were negligible in children and young adults, rose significantly above baseline in subjects in their 40s and increased steadily thereafter. Amyloid-β dimers were undetectable until subjects were in their 60s; their levels then increased sharply and correlated with plaque load. Remarkably, in cognitively intact individuals we found strong positive correlations between Aβ*56 and two pathological forms of soluble tau (tau-CP13 and tau-Alz50), and negative correlations between Aβ*56 and two postsynaptic proteins (drebrin and fyn kinase), but none between amyloid-β dimers or amyloid-β trimers and tau or synaptic proteins. Comparing impaired with age-matched unimpaired subjects, we found the highest levels of amyloid-β dimers, but the lowest levels of Aβ*56 and amyloid-β trimers, in subjects with probable Alzheimer’s disease. In conclusion, in cognitively normal adults Aβ*56 increased ahead of amyloid-β dimers or amyloid-β trimers, and pathological tau proteins and postsynaptic proteins correlated with Aβ*56, but not amyloid-β dimers or amyloid-β trimers. We propose that Aβ*56 may play a pathogenic role very early in the pathogenesis of Alzheimer’s disease. Alzheimer's disease begins about two decades before the onset of symptoms or neuron death, and is believed to be caused by pathogenic amyloid- beta aggregates that initiate a cascade of molecular events culminating in widespread neurodegeneration. The microtubule binding protein tau may mediate the effects of amyloid- beta in this cascade. Amyloid plaques comprised of insoluble, fibrillar amyloid- beta aggregates are the most characteristic feature of Alzheimer's disease. However, the correspondence between the distribution of plaques and the pattern of neurodegeneration is tenuous. This discrepancy has stimulated the investigation of other amyloid- beta aggregates, including soluble amyloid- beta oligomers. Different soluble amyloid- beta oligomers have been studied in several mouse models, but not systematically in humans. Here, we measured three amyloid- beta oligomers previously described in mouse models-amyloid- beta trimers, A beta *56 and amyloid- beta dimers-in brain tissue from 75 cognitively intact individuals, ranging from young children to the elderly, and 58 impaired subjects with mild cognitive impairment or probable Alzheimer's disease. As in mouse models, where amyloid- beta trimers appear to be the fundamental amyloid- beta assembly unit of A beta *56 and are present in young mice prior to memory decline, amyloid- beta trimers in humans were present in children and adolescents; their levels rose gradually with age and were significantly above baseline in subjects in their 70s. A beta *56 levels were negligible in children and young adults, rose significantly above baseline in subjects in their 40s and increased steadily thereafter. Amyloid- beta dimers were undetectable until subjects were in their 60s; their levels then increased sharply and correlated with plaque load. Remarkably, in cognitively intact individuals we found strong positive correlations between A beta *56 and two pathological forms of soluble tau (tau-CP13 and tau-Alz50), and negative correlations between A beta *56 and two postsynaptic proteins (drebrin and fyn kinase), but none between amyloid- beta dimers or amyloid- beta trimers and tau or synaptic proteins. Comparing impaired with age-matched unimpaired subjects, we found the highest levels of amyloid- beta dimers, but the lowest levels of A beta *56 and amyloid- beta trimers, in subjects with probable Alzheimer's disease. In conclusion, in cognitively normal adults A beta *56 increased ahead of amyloid- beta dimers or amyloid- beta trimers, and pathological tau proteins and postsynaptic proteins correlated with A beta *56, but not amyloid- beta dimers or amyloid- beta trimers. We propose that A beta *56 may play a pathogenic role very early in the pathogenesis of Alzheimer's disease. |
| Author | Schneider, Julie A. Lesné, Sylvain E. Grant, Marianne Kuskowski, Michael Bennett, David A. Sherman, Mathew A. Ashe, Karen H. |
| AuthorAffiliation | 2 N. Bud Grossman Centre for Memory Research and Care, University of Minnesota, Minneapolis, MN 55455 USA 5 Rush Alzheimer’s Disease Centre, Rush University Medical Centre, Chicago, IL 60612 USA 4 Department of Neurology, University of Minnesota, Minneapolis, MN 55455 USA 3 Institute for Translational Neuroscience, University of Minnesota, Minneapolis, MN 55455 USA 6 Geriatric Research Education Clinical Centre, VA Medical Centre, Minneapolis, MN 55417 USA 1 Department of Neuroscience, University of Minnesota, Minneapolis, MN 55455 USA |
| AuthorAffiliation_xml | – name: 6 Geriatric Research Education Clinical Centre, VA Medical Centre, Minneapolis, MN 55417 USA – name: 3 Institute for Translational Neuroscience, University of Minnesota, Minneapolis, MN 55455 USA – name: 1 Department of Neuroscience, University of Minnesota, Minneapolis, MN 55455 USA – name: 4 Department of Neurology, University of Minnesota, Minneapolis, MN 55455 USA – name: 5 Rush Alzheimer’s Disease Centre, Rush University Medical Centre, Chicago, IL 60612 USA – name: 2 N. Bud Grossman Centre for Memory Research and Care, University of Minnesota, Minneapolis, MN 55455 USA |
| Author_xml | – sequence: 1 givenname: Sylvain E. surname: Lesné fullname: Lesné, Sylvain E. – sequence: 2 givenname: Mathew A. surname: Sherman fullname: Sherman, Mathew A. – sequence: 3 givenname: Marianne surname: Grant fullname: Grant, Marianne – sequence: 4 givenname: Michael surname: Kuskowski fullname: Kuskowski, Michael – sequence: 5 givenname: Julie A. surname: Schneider fullname: Schneider, Julie A. – sequence: 6 givenname: David A. surname: Bennett fullname: Bennett, David A. – sequence: 7 givenname: Karen H. surname: Ashe fullname: Ashe, Karen H. |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=27302159$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/23576130$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1016/j.cell.2010.06.036 10.1212/01.WNL.0000152982.47274.9E 10.1001/jamaneurol.2013.48 10.1073/pnas.090106797 10.3233/JAD-2011-101995 10.1523/JNEUROSCI.5543-03.2004 10.1111/j.1471-4159.2011.07478.x 10.1212/01.WNL.0000063311.58879.01 10.1038/6374 10.1523/JNEUROSCI.0172-12.2012 10.1016/j.neurobiolaging.2009.11.007 10.1007/BF00308809 10.1126/science.1079469 10.1016/j.jalz.2010.11.002 10.1126/science.3083509 10.1016/S1474-4422(09)70299-6 10.1126/science.274.5284.99 10.1073/pnas.0409336102 10.1523/JNEUROSCI.5161-07.2008 10.1016/j.neuron.2010.04.031 10.1016/j.neuron.2010.11.030 10.1093/brain/awq065 10.1002/ana.21509 10.1523/JNEUROSCI.3432-04.2004 10.1212/01.WNL.0000042478.08543.F7 10.1001/archneur.61.3.378 10.1016/j.tins.2010.05.004 10.1038/nn.3028 10.1074/jbc.M808591200 10.1002/ana.410410106 10.1016/j.neuroscience.2007.10.054 10.1111/j.1742-4658.2010.07719.x 10.1073/pnas.2635903100 10.1038/nm1782 10.1016/j.jalz.2011.03.003 10.1080/01688639308402570 10.1212/01.wnl.0000228244.10416.20 10.1074/jbc.M701078200 10.1196/annals.1379.012 10.1074/jbc.M608485200 10.1126/science.1141736 10.2174/156720512801322573 10.1126/science.1113694 10.1038/nature04533 10.1523/JNEUROSCI.20-11-04050.2000 10.1074/jbc.M109.000208 10.1073/pnas.092136199 10.1007/978-1-60761-744-0_4 10.1016/j.neurobiolaging.2011.05.003 10.1126/science.1566067 10.1523/JNEUROSCI.5180-09.2010 10.1001/archneurol.2009.59 10.1159/000096129 10.1016/j.neuron.2011.01.002 10.1002/ana.22052 10.1056/NEJMoa1202753 |
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| References | Bennett (2024110407435006800_awt062-B8) 2005; 64 Sherman (2024110407435006800_awt062-B49) 2011; 670 Zahs (2024110407435006800_awt062-B55) 2010; 33 Klyubin (2024110407435006800_awt062-B56) 2008; 28 Reed (2024110407435006800_awt062-B43) 2011; 32 Bennett (2024110407435006800_awt062-B10) 2003; 60 Santacruz (2024110407435006800_awt062-B47) 2005; 309 Hoover (2024110407435006800_awt062-B25) 2010; 68 Cheng (2024110407435006800_awt062-B15) 2007; 282 Youngjohn (2024110407435006800_awt062-B54) 1993; 15 Handoko (2024110407435006800_awt062-B22) 2013 Sperling (2024110407435006800_awt062-B51) 2011; 7 Wolozin (2024110407435006800_awt062-B53) 1986; 232 Bao (2024110407435006800_awt062-B3) 2012; 33 Bateman (2024110407435006800_awt062-B4) 2012; 367 Mucke (2024110407435006800_awt062-B37) 2000; 20 Reiman (2024110407435006800_awt062-B44) 2004; 101 Hsiao (2024110407435006800_awt062-B26) 1996; 274 Boyle (2024110407435006800_awt062-B11) 2006; 67 Giannakopoulos (2024110407435006800_awt062-B19) 2003; 60 Bennett (2024110407435006800_awt062-B7) 2012; 9 Ittner (2024110407435006800_awt062-B27) 2010; 142 Jack (2024110407435006800_awt062-B28) 2010; 9 Braak (2024110407435006800_awt062-B12) 1991; 82 Rapoport (2024110407435006800_awt062-B42) 2002; 99 Pham (2024110407435006800_awt062-B41) 2010; 277 Golde (2024110407435006800_awt062-B20) 2011; 69 Bennett (2024110407435006800_awt062-B6) 2006; 27 Oddo (2024110407435006800_awt062-B39) 2006; 281 Larson (2024110407435006800_awt062-B33) 2012; 120 Noguchi (2024110407435006800_awt062-B38) 2009; 284 Georganopoulou (2024110407435006800_awt062-B18) 2005; 102 Villemagne (2024110407435006800_awt062-B52) 2010; 30 Gandy (2024110407435006800_awt062-B17) 2010; 68 Kayed (2024110407435006800_awt062-B30) 2003; 300 Chapman (2024110407435006800_awt062-B14) 1999; 2 Rocca (2024110407435006800_awt062-B46) 2011; 7 Ashe (2024110407435006800_awt062-B2) 2010; 66 Petrie (2024110407435006800_awt062-B40) 2009; 66 Kawarabayashi (2024110407435006800_awt062-B29) 2004; 24 Kayed (2024110407435006800_awt062-B31) 2009; 284 Hensley (2024110407435006800_awt062-B24) 2011; 24 Shankar (2024110407435006800_awt062-B48) 2008; 14 Chabrier (2024110407435006800_awt062-B13) 2012; 32 de Leon (2024110407435006800_awt062-B16) 2007; 1097 Lesne (2024110407435006800_awt062-B34) 2006; 440 Hardy (2024110407435006800_awt062-B23) 1992; 256 Mc Donald (2024110407435006800_awt062-B36) 2010; 133 Lacor (2024110407435006800_awt062-B32) 2004; 24 Roberson (2024110407435006800_awt062-B45) 2007; 316 Small (2024110407435006800_awt062-B50) 2000; 97 Benilova (2024110407435006800_awt062-B5) 2012; 15 Lesne (2024110407435006800_awt062-B35) 2008; 151 Amieva (2024110407435006800_awt062-B1) 2008; 64 Bennett (2024110407435006800_awt062-B9) 2004; 61 Gomez-Isla (2024110407435006800_awt062-B21) 1997; 41 35552385 - Brain. 2022 May 13 |
| References_xml | – volume: 142 start-page: 387 year: 2010 ident: 2024110407435006800_awt062-B27 article-title: Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models publication-title: Cell doi: 10.1016/j.cell.2010.06.036 – volume: 64 start-page: 834 year: 2005 ident: 2024110407435006800_awt062-B8 article-title: Mild cognitive impairment is related to Alzheimer disease pathology and cerebral infarctions publication-title: Neurology doi: 10.1212/01.WNL.0000152982.47274.9E – year: 2013 ident: 2024110407435006800_awt062-B22 article-title: Specific amyloid-β oligomers, but not amyloid-β(1-42), correlate with tau in cerebrospinal fluid from cognitively normal older adults publication-title: JAMA Neurol doi: 10.1001/jamaneurol.2013.48 – volume: 97 start-page: 6037 year: 2000 ident: 2024110407435006800_awt062-B50 article-title: Cerebral metabolic and cognitive decline in persons at genetic risk for Alzheimer's disease publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.090106797 – volume: 24 start-page: 767 year: 2011 ident: 2024110407435006800_awt062-B24 article-title: Analysis of postmortem ventricular cerebrospinal fluid from patients with and without dementia indicates association of vitamin E with neuritic plaques and specific measures of cognitive performance publication-title: J Alzheimers Dis doi: 10.3233/JAD-2011-101995 – volume: 24 start-page: 3801 year: 2004 ident: 2024110407435006800_awt062-B29 article-title: Dimeric amyloid beta protein rapidly accumulates in lipid rafts followed by apolipoprotein E and phosphorylated tau accumulation in the Tg2576 mouse model of Alzheimer's disease publication-title: J Neurosci doi: 10.1523/JNEUROSCI.5543-03.2004 – volume: 120 start-page: 125 year: 2012 ident: 2024110407435006800_awt062-B33 article-title: Soluble Abeta oligomer production and toxicity publication-title: J Neurochem doi: 10.1111/j.1471-4159.2011.07478.x – volume: 60 start-page: 1495 year: 2003 ident: 2024110407435006800_awt062-B19 article-title: Tangle and neuron numbers, but not amyloid load, predict cognitive status in Alzheimer's disease publication-title: Neurology doi: 10.1212/01.WNL.0000063311.58879.01 – volume: 2 start-page: 271 year: 1999 ident: 2024110407435006800_awt062-B14 article-title: Impaired synaptic plasticity and learning in aged amyloid precursor protein transgenic mice publication-title: Nat Neurosci doi: 10.1038/6374 – volume: 32 start-page: 17345 year: 2012 ident: 2024110407435006800_awt062-B13 article-title: Soluble abeta promotes wild-type tau pathology in vivo publication-title: J Neurosci doi: 10.1523/JNEUROSCI.0172-12.2012 – volume: 32 start-page: 1784 year: 2011 ident: 2024110407435006800_awt062-B43 article-title: Cognitive effects of cell-derived and synthetically derived Abeta oligomers publication-title: Neurobiol Aging doi: 10.1016/j.neurobiolaging.2009.11.007 – volume: 82 start-page: 239 year: 1991 ident: 2024110407435006800_awt062-B12 article-title: Neuropathological stageing of Alzheimer-related changes publication-title: Acta Neuropathol doi: 10.1007/BF00308809 – volume: 300 start-page: 486 year: 2003 ident: 2024110407435006800_awt062-B30 article-title: Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis publication-title: Science doi: 10.1126/science.1079469 – volume: 7 start-page: 80 year: 2011 ident: 2024110407435006800_awt062-B46 article-title: Trends in the incidence and prevalence of Alzheimer's disease, dementia, and cognitive impairment in the United States publication-title: Alzheimers Dement doi: 10.1016/j.jalz.2010.11.002 – volume: 232 start-page: 648 year: 1986 ident: 2024110407435006800_awt062-B53 article-title: A neuronal antigen in the brains of Alzheimer patients publication-title: Science doi: 10.1126/science.3083509 – volume: 9 start-page: 119 year: 2010 ident: 2024110407435006800_awt062-B28 article-title: Hypothetical model of dynamic biomarkers of the Alzheimer's pathological cascade publication-title: Lancet Neurol doi: 10.1016/S1474-4422(09)70299-6 – volume: 274 start-page: 99 year: 1996 ident: 2024110407435006800_awt062-B26 article-title: Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice publication-title: Science doi: 10.1126/science.274.5284.99 – volume: 102 start-page: 2273 year: 2005 ident: 2024110407435006800_awt062-B18 article-title: Nanoparticle-based detection in cerebral spinal fluid of a soluble pathogenic biomarker for Alzheimer's disease publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.0409336102 – volume: 28 start-page: 4231 year: 2008 ident: 2024110407435006800_awt062-B56 article-title: Amyloid β protein dimer-containing human CSF disrupts plasticity: prevention by systemic passive immunization publication-title: Journal of Neuroscience doi: 10.1523/JNEUROSCI.5161-07.2008 – volume: 66 start-page: 631 year: 2010 ident: 2024110407435006800_awt062-B2 article-title: Probing the biology of Alzheimer's disease in mice publication-title: Neuron doi: 10.1016/j.neuron.2010.04.031 – volume: 68 start-page: 1067 year: 2010 ident: 2024110407435006800_awt062-B25 article-title: Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration publication-title: Neuron doi: 10.1016/j.neuron.2010.11.030 – volume: 133 start-page: 1328 year: 2010 ident: 2024110407435006800_awt062-B36 article-title: The presence of sodium dodecyl sulphate-stable Abeta dimers is strongly associated with Alzheimer-type dementia publication-title: Brain doi: 10.1093/brain/awq065 – volume: 64 start-page: 492 year: 2008 ident: 2024110407435006800_awt062-B1 article-title: Prodromal Alzheimer's disease: successive emergence of the clinical symptoms publication-title: Ann Neurol doi: 10.1002/ana.21509 – volume: 24 start-page: 10191 year: 2004 ident: 2024110407435006800_awt062-B32 article-title: Synaptic targeting by Alzheimer's-related amyloid beta oligomers publication-title: J Neurosci doi: 10.1523/JNEUROSCI.3432-04.2004 – volume: 60 start-page: 246 year: 2003 ident: 2024110407435006800_awt062-B10 article-title: Apolipoprotein E epsilon4 allele, AD pathology, and the clinical expression of Alzheimer's disease publication-title: Neurology doi: 10.1212/01.WNL.0000042478.08543.F7 – volume: 61 start-page: 378 year: 2004 ident: 2024110407435006800_awt062-B9 article-title: Neurofibrillary tangles mediate the association of amyloid load with clinical Alzheimer disease and level of cognitive function publication-title: Arch Neurol doi: 10.1001/archneur.61.3.378 – volume: 33 start-page: 381 year: 2010 ident: 2024110407435006800_awt062-B55 article-title: ‘Too much good news'—are Alzheimer mouse models trying to tell us how to prevent, not cure, Alzheimer's disease? publication-title: Trends Neurosci doi: 10.1016/j.tins.2010.05.004 – volume: 15 start-page: 349 year: 2012 ident: 2024110407435006800_awt062-B5 article-title: The toxic Abeta oligomer and Alzheimer's disease: an emperor in need of clothes publication-title: Nat Neurosci doi: 10.1038/nn.3028 – volume: 284 start-page: 4230 year: 2009 ident: 2024110407435006800_awt062-B31 article-title: Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer publication-title: J Biol Chem doi: 10.1074/jbc.M808591200 – volume: 41 start-page: 17 year: 1997 ident: 2024110407435006800_awt062-B21 article-title: Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease publication-title: Ann Neurol doi: 10.1002/ana.410410106 – volume: 151 start-page: 745 year: 2008 ident: 2024110407435006800_awt062-B35 article-title: Plaque-bearing mice with reduced levels of oligomeric amyloid-beta assemblies have intact memory function publication-title: Neuroscience doi: 10.1016/j.neuroscience.2007.10.054 – volume: 277 start-page: 3051 year: 2010 ident: 2024110407435006800_awt062-B41 article-title: Progressive accumulation of amyloid-beta oligomers in Alzheimer's disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins publication-title: FEBS J doi: 10.1111/j.1742-4658.2010.07719.x – volume: 101 start-page: 284 year: 2004 ident: 2024110407435006800_awt062-B44 article-title: Functional brain abnormalities in young adults at genetic risk for late-onset Alzheimer's dementia publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.2635903100 – volume: 14 start-page: 837 year: 2008 ident: 2024110407435006800_awt062-B48 article-title: Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory publication-title: Nat Med doi: 10.1038/nm1782 – volume: 7 start-page: 280 year: 2011 ident: 2024110407435006800_awt062-B51 article-title: Toward defining the preclinical stages of Alzheimer's disease: recommendations from the National Institute on Aging-Alzheimer's Association workgroups on diagnostic guidelines for Alzheimer's disease publication-title: Alzheimers Dement doi: 10.1016/j.jalz.2011.03.003 – volume: 15 start-page: 447 year: 1993 ident: 2024110407435006800_awt062-B54 article-title: Learning, forgetting, and retrieval of everyday material across the adult life span publication-title: J Clin Exp Neuropsychol doi: 10.1080/01688639308402570 – volume: 67 start-page: 441 year: 2006 ident: 2024110407435006800_awt062-B11 article-title: Mild cognitive impairment: risk of Alzheimer disease and rate of cognitive decline publication-title: Neurology doi: 10.1212/01.wnl.0000228244.10416.20 – volume: 282 start-page: 23818 year: 2007 ident: 2024110407435006800_awt062-B15 article-title: Accelerating amyloid-beta fibrillization reduces oligomer levels and functional deficits in Alzheimer disease mouse models publication-title: J Biol Chem doi: 10.1074/jbc.M701078200 – volume: 1097 start-page: 114 year: 2007 ident: 2024110407435006800_awt062-B16 article-title: Imaging and CSF studies in the preclinical diagnosis of Alzheimer's disease publication-title: Ann N Y Acad Sci doi: 10.1196/annals.1379.012 – volume: 281 start-page: 39413 year: 2006 ident: 2024110407435006800_awt062-B39 article-title: Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles publication-title: J Biol Chem doi: 10.1074/jbc.M608485200 – volume: 316 start-page: 750 year: 2007 ident: 2024110407435006800_awt062-B45 article-title: Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model publication-title: Science doi: 10.1126/science.1141736 – volume: 9 start-page: 628 year: 2012 ident: 2024110407435006800_awt062-B7 article-title: Overview and findings from the religious orders study publication-title: Curr Alzheimer Res doi: 10.2174/156720512801322573 – volume: 309 start-page: 476 year: 2005 ident: 2024110407435006800_awt062-B47 article-title: Tau suppression in a neurodegenerative mouse model improves memory function publication-title: Science doi: 10.1126/science.1113694 – volume: 440 start-page: 352 year: 2006 ident: 2024110407435006800_awt062-B34 article-title: A specific amyloid-beta protein assembly in the brain impairs memory publication-title: Nature doi: 10.1038/nature04533 – volume: 20 start-page: 4050 year: 2000 ident: 2024110407435006800_awt062-B37 article-title: High-level neuronal expression of abeta 1-42 in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation publication-title: J Neurosci doi: 10.1523/JNEUROSCI.20-11-04050.2000 – volume: 284 start-page: 32895 year: 2009 ident: 2024110407435006800_awt062-B38 article-title: Isolation and characterization of patient-derived, toxic, high mass amyloid beta-protein (Abeta) assembly from Alzheimer disease brains publication-title: J Biol Chem doi: 10.1074/jbc.M109.000208 – volume: 99 start-page: 6364 year: 2002 ident: 2024110407435006800_awt062-B42 article-title: Tau is essential to beta-amyloid-induced neurotoxicity publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.092136199 – volume: 670 start-page: 45 year: 2011 ident: 2024110407435006800_awt062-B49 article-title: Detecting abeta*56 oligomers in brain tissues publication-title: Methods Mol Biol doi: 10.1007/978-1-60761-744-0_4 – volume: 33 start-page: 825 e1 year: 2012 ident: 2024110407435006800_awt062-B3 article-title: Different beta-amyloid oligomer assemblies in Alzheimer brains correlate with age of disease onset and impaired cholinergic activity publication-title: Neurobiol Aging doi: 10.1016/j.neurobiolaging.2011.05.003 – volume: 256 start-page: 184 year: 1992 ident: 2024110407435006800_awt062-B23 article-title: Alzheimer's disease: the amyloid cascade hypothesis publication-title: Science doi: 10.1126/science.1566067 – volume: 30 start-page: 6315 year: 2010 ident: 2024110407435006800_awt062-B52 article-title: Blood-borne amyloid-beta dimer correlates with clinical markers of Alzheimer's disease publication-title: J Neurosci doi: 10.1523/JNEUROSCI.5180-09.2010 – volume: 66 start-page: 632 year: 2009 ident: 2024110407435006800_awt062-B40 article-title: Preclinical evidence of Alzheimer changes: convergent cerebrospinal fluid biomarker and fluorodeoxyglucose positron emission tomography findings publication-title: Arch Neurol doi: 10.1001/archneurol.2009.59 – volume: 27 start-page: 169 year: 2006 ident: 2024110407435006800_awt062-B6 article-title: Decision rules guiding the clinical diagnosis of Alzheimer's disease in two community-based cohort studies compared to standard practice in a clinic-based cohort study publication-title: Neuroepidemiology doi: 10.1159/000096129 – volume: 69 start-page: 203 year: 2011 ident: 2024110407435006800_awt062-B20 article-title: Anti-abeta therapeutics in Alzheimer's disease: the need for a paradigm shift publication-title: Neuron doi: 10.1016/j.neuron.2011.01.002 – volume: 68 start-page: 220 year: 2010 ident: 2024110407435006800_awt062-B17 article-title: Days to criterion as an indicator of toxicity associated with human Alzheimer amyloid-beta oligomers publication-title: Ann Neurol doi: 10.1002/ana.22052 – volume: 367 start-page: 795 year: 2012 ident: 2024110407435006800_awt062-B4 article-title: Clinical and biomarker changes in dominantly inherited Alzheimer's disease publication-title: N Engl J Med doi: 10.1056/NEJMoa1202753 – reference: 35552385 - Brain. 2022 May 13;: |
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| SubjectTerms | Adolescence Adolescent Adult Aged Aged, 80 and over Aging - metabolism Aging - pathology Aging - physiology Alzheimer Disease - etiology Alzheimer Disease - metabolism Alzheimer Disease - pathology Amyloid beta-Peptides - chemistry Amyloid beta-Peptides - metabolism Biological and medical sciences Brain Chemistry - physiology Child Child, Preschool Cognition - physiology Cohort Studies Cross-Sectional Studies Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Female Follow-Up Studies Humans Infant Male Medical sciences Middle Aged Neurology Original Plaque, Amyloid - etiology Plaque, Amyloid - metabolism Plaque, Amyloid - pathology Protein Multimerization Young Adult |
| Title | Brain amyloid-β oligomers in ageing and Alzheimer’s disease |
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