Alzheimer's disease-type neuronal tau hyperphosphorylation induced by Aβ oligomers

De Felice, Fernanda G.; Wu, Diana; Lambert, Mary P.; Fernandez, Sara J.; Velasco, Pauline T.; Lacor, Pascale N.; Bigio, Eileen H.; Jerecic, Jasna; Acton, Paul J.; Shughrue, Paul J.; Chen-Dodson, Elizabeth; Kinney, Gene G.; Klein, William L.

doi:10.1016/j.neurobiolaging.2007.02.029

Cited by 432Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Alzheimer's disease-type neuronal tau hyperphosphorylation induced by Aβ oligomers

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De Felice, Fernanda G., Wu, Diana, Lambert, Mary P., Fernandez, Sara J., Velasco, Pauline T., Lacor, Pascale N., Bigio, Eileen H., Jerecic, Jasna +5 more·2008·Neurobiology of Aging

DOI 10.1016/j.neurobiolaging.2007.02.029PMC PMC3142933

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Abstract

Alzheimer's disease (AD) is characterized by presence of extracellular fibrillar A beta in amyloid plaques, intraneuronal neurofibrillary tangles consisting of aggregated hyperphosphorylated tau and elevated brain levels of soluble A beta oligomers (ADDLs). A major question is how these disparate facets of AD pathology are mechanistically related. Here we show that, independent of the presence of fibrils, ADDLs stimulate tau phosphorylation in mature cultures of hippocampal neurons and in neuroblastoma cells at epitopes characteristically hyperphosphorylated in AD. A monoclonal antibody that targets ADDLs blocked their attachment to synaptic binding sites and prevented tau hyperphosphorylation. Tau phosphorylation was blocked by the Src family tyrosine kinase inhibitor, 4-amino-5-(4-chlorophenyl)-7(t-butyl)pyrazol(3,4-D)pyramide (PP1), and by the phosphatidylinositol-3-kinase inhibitor LY294002. Significantly, tau hyperphosphorylation was also induced by a soluble aqueous extract containing A beta oligomers from AD brains, but not by an extract from non-AD brains. A beta oligomers have been increasingly implicated as the main neurotoxins in AD, and the current results provide a unifying mechanism in which oligomer activity is directly linked to tau hyperphosphorylation in AD pathology.

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Crossref · 10.1016/j.neurobiolaging.2007.02.029

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Soluble AβOs enhance kinase activity triggering tau hyperphosphorylation at threonine 231 in primary neuronal cultures.
“Interestingly, soluble AβOs are known to enhance kinase activity triggering tau hyperphosphorylation at threonine 231 in primary neuronal cultures.16”
From Cerebrospinal fluid p-tau231 as an early indicator of emerging pathology in Alzheimer's disease (2022) · cites this paper as [16]
Results §§3.3 and 3.5 show that Aβ oligomers induced tau phosphorylation at Thr231 in primary hippocampal neuronal cultures and that Src-family kinase and PI3K inhibitors blocked it. The inhibitor results implicate kinase signaling, but the paper does not establish that the oligomers enhanced kinase activity; the Discussion presents pathway activation as a possibility. (LLM, conf=0.85)
Experimental — accuracy not yet measured
Aβ promotes tau phosphorylation at disease-associated sites in in vitro and in vivo models of AD.
“Aβ promotes tau phosphorylation at disease-associated sites in in vitro and in vivo models of AD [2, 35–41].”
From Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity (2016) · cites this paper as [40]
The Results (§3.3; page unavailable) show that Aβ oligomers increased phosphorylation at the AD-associated Thr231 and Ser404 sites in cultured neurons. The Introduction (§1; page unavailable) reports tau hyperphosphorylation after Aβ injection in animals, but does not establish phosphorylation at those specific sites in vivo; this paper's own experiments were in vitro. (LLM, conf=0.82)
Experimental — accuracy not yet measured
In cellular and animal models, co-expression of Aβ augments tau phosphorylation at these sites and increases the levels of active GSK3 and PAR-1/MARK.
“In cellular and animal models, co-expression of Aβ augments tau phosphorylation at these sites and increases the levels of active GSK3 and PAR-1/MARK [2, 35–41, 43, 44].”
From Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity (2016) · cites this paper as [40]
Results §3.3 reports increased tau phosphorylation at Thr231 and Ser404 after Aβ-oligomer exposure in cultured rat hippocampal neurons. The Introduction also reports prior findings of GSK-3β activation and describes transgenic mice expressing APP and tau. However, this paper does not show that Aβ co-expression increases active GSK3 in its models, and the cited passages do not establish an increase in active PAR-1/MARK. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Evidence from AD neuronal culture models indicates that soluble Aβ oligomers induce tau hyperphosphorylation in multiple sites.
“Interestingly, evidence from AD neuronal culture models indicate that soluble Aβ oligomers (AβOs) induce tau hyperphosphorylation in multiple sites.16,17”
From Cerebrospinal fluid p-tau231 as an early indicator of emerging pathology in Alzheimer's disease (2022) · cites this paper as [16]
Aβ oligomers can induce tau hyperphosphorylation.
“several studies reporting that Aβ oligomers can induce tau hyperphosphorylation [51]”
From Astrocytic APOE3-Christchurch expression ameliorates brain amyloid-β pathology in 5xFAD mice (2026) · cites this paper as [51]

Aβ oligomers induce a striking redistribution of insulin receptors, causing their internalization from dendritic membranes and accumulation in the cell body, which renders neurons insulin resistant.
“Aβ oligomers induce a striking redistribution of IRs, causing their internalization from dendritic membranes and accumulation in the cell body. This renders neurons insulin resistant (De Felice et al., 2009; De Felice et al., 2008; Zhao et al., 2008).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as De Felice et al., 2008
Stimulation of insulin signaling protects against accumulation of hyperphosphorylated tau, a pathological hallmark of Alzheimer's disease that is induced by Aβ oligomers.
“stimulation of insulin signaling also protects against accumulation of hyperphosphorylated tau (Escribano et al., 2010), a pathological hallmark of AD that is induced by Aβ oligomers (De Felice et al., 2008).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as De Felice et al., 2008
Clustering of oligomers at synapses shows a cause-and-effect relationship with characteristic Alzheimer neuropathologies: AD-type tau hyperphosphorylation, redistribution of insulin receptors, spine loss and oxidative stress are manifest exclusively in neurons showing synapses targeted by oligomers.
“Clustering of oligomers at synapses, moreover, shows a cause-and-effect relationship with characteristic Alzheimer neuropathologies. AD type tau hyperphosphorylation (De Felice et al., 2008), redistribution of insulin receptors (De Felice et al., 2009; Zhao et al., 2008), spine loss (Lacor et al., 2007) and oxidative stress (De Felice et al., 2007; Decker et al., 2010a) are manifest exclusively in”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as De Felice et al., 2008
Both gain-of-toxic-function and loss-of-normal-function deleterious effects have been described for phospho-tau.
“Both gain-of-toxic-function and loss-of-normal-function deleterious effects also have been described for phospho-tau (84-89).”
From Correlation of Alzheimer Disease Neuropathologic Changes With Cognitive Status: A Review of the Literature (2012) · cites this paper as [88]
It has been suggested that the pathogenetic effect of AβP-related substances may be mediated by 'seeding' neurofibrillary pathology.
“Owing in part to the scarcity of neocortical NFTs in the absence of AβPs, and the relatively modest apparent direct impact of AβPs on cognition, it has been suggested that the pathogenetic effect of AβP-related substances may be mediated by “seeding” neurofibrillary pathology (46, 88, 189, 264, 265).”
From Correlation of Alzheimer Disease Neuropathologic Changes With Cognitive Status: A Review of the Literature (2012) · cites this paper as [88]
Several neuronal receptors have been proposed as mediating the effect of Aβ on synaptic plasticity and memory, including α-7-nicotinic, glutamatergic, and insulin receptors.
“Several neuronal receptors have been proposed as mediating the effect of Aβ on synaptic plasticity and memory, including the α-7-nicotinic (16), glutamatergic (39–40), and insulin (14) receptors.”
From Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein (2010) · cites this paper as [39]

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[1]Abramoff MD, Magelhaes PJ, Ram SJ. Image Processing with Image J Biophotonics International. 2004;11:36–42. [[Google Scholar](https://scholar.google.com/scholar_lookup?journal=Image%20Processing%20with%20Image%20J%20Biophotonics%20International&author=MD%20Abramoff&author=PJ%20Magelhaes&author=SJ%20Ram&volume=11&publication_year=2004&pages=36-42&)]

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“In the current study, we also showed Ab oligomers in plaques, which are considered the most toxic Ab forms affecting synapses and inducing tau phosphorylation (Lacor et al., 2007; Lambert et al., 2007; De Felice et al., 2008).”
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Authors: De Felice, F. G., Wu, D., Lambert, M. P., Fernandez, S. J., Velasco, P. T., Lacor, P. N., Bigio, E. H., Jerecic, J., Acton, P. J., Shughrue, P. J., Chen-Dodson, E., Kinney, G. G., & Klein, W. L.
Affiliations: Northwestern University (US)
Merck & Co., Inc., Rahway, NJ, USA (United States) (US)
Corresponding author: Klein, William L.
ORCID: Wu, Diana
Bigio, Eileen H.
Kinney, Gene G.
Klein, William L.
Venue: Neurobiology of Aging
Publisher: Elsevier BV
Published: 2008-09
Volume: 29
Issue: 9
Pages: 1334-1347
ISSN: 0197-4580 (ISSN-L)
DOI: 10.1016/j.neurobiolaging.2007.02.029
PMC: PMC3142933
OpenAlex: W1976602187
Cited by: 432
References: 57
Citations by year: 2026: 8 · 2025: 9 · 2024: 17 · 2023: 16 · 2022: 16 · 2021: 30 · 2020: 27 · 2019: 24 · 2018: 30 · 2017: 27 · 2016: 18 · 2015: 23 · 2014: 31 · 2013: 36 · 2012: 32
FWCI: 14.25
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Neurobiology of Aging (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Institute on Aging (R01 AG11385, R01AG022547, R01-AG22547, R01AG011385, R01-AG18877, R01AG029460, P30AG013854, R01AG018877)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: Alzheimer's disease, tau hyperphosphorylation, amyloid-beta oligomers, soluble amyloid-beta, neurofibrillary tangles, amyloid plaques, hippocampal neurons, neuroblastoma cells, Src family kinases, protein phosphatase 1, phosphatidylinositol 3-kinase, LY294002, neurotoxicity
MeSH terms: Alzheimer Disease, Cells, Cultured, Hippocampus, Humans, Neurons, Peptide Fragments, Phosphorylation, Amyloid beta-Peptides, tau Proteins

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Alzheimer's disease-type neuronal tau hyperphosphorylation induced by Aβ oligomers

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