Aβ Immunotherapy Leads to Clearance of Early, but Not Late, Hyperphosphorylated Tau Aggregates via the Proteasome

Oddo, Salvatore; Billings, Lauren; Kesslak, J.Patrick; Cribbs, David H.; LaFerla, Frank M.

doi:10.1016/j.neuron.2004.07.003

Cited by 780Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Aβ Immunotherapy Leads to Clearance of Early, but Not Late, Hyperphosphorylated Tau Aggregates via the Proteasome

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Oddo, Salvatore, Billings, Lauren, Kesslak, J.Patrick, Cribbs, David H., LaFerla, Frank M.·2004·Neuron

DOI 10.1016/j.neuron.2004.07.003

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Abstract

Amyloid-beta (Abeta) plaques and neurofibrillary tangles are the hallmark neuropathological lesions of Alzheimer's disease (AD). Using a triple transgenic model (3xTg-AD) that develops both lesions in AD-relevant brain regions, we determined the consequence of Abeta clearance on the development of tau pathology. Here we show that Abeta immunotherapy reduces not only extracellular Abeta plaques but also intracellular Abeta accumulation and most notably leads to the clearance of early tau pathology. We find that Abeta deposits are cleared first and subsequently reemerge prior to the tau pathology, indicative of a hierarchical and direct relationship between Abeta and tau. The clearance of the tau pathology is mediated by the proteasome and is dependent on the phosphorylation state of tau, as hyperphosphorylated tau aggregates are unaffected by the Abeta antibody treatment. These findings indicate that Abeta immunization may be useful for clearing both hallmark lesions of AD, provided that intervention occurs early in the disease course.

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Passive immunization against Aβ in the 3xTg mouse model reduced extracellular amyloid plaques and resulted in decreased tau pathology.
“Related findings were reported by Vasconselos and colleagues, showing that pre-aggregated Aβ is able to induce fibrillization of tau both in vitro and in vivo [32], and interestingly, passive immunization against Aβ in the 3xTg mouse model not only reduced extracellular amyloid plaques but also resulted in decreased tau pathology [33].”
From Characterization of a Mouse Model of Alzheimer’s Disease Expressing Aβ4-42 and Human Mutant Tau (2021) · cites this paper as [33]
Reducing Aβ was sufficient to clear early stage tauopathy in a combinatorial transgenic model.
“In one of these combinatorial transgenic models, reducing Aβ was sufficient to clear early stage tauopathy (5).”
From Combinatorial model of amyloid β and tau reveals synergy between amyloid deposits and tangle formation (2022) · cites this paper as [5]
Genetic, pathological, and biochemical evidence suggests that elevation of Aβ levels is a causal event in AD pathogenesis that lies upstream of tau-induced neurodegeneration.
“Genetic, pathological, and biochemical evidence suggests that elevation of Aβ levels is a causal event in AD pathogenesis [2–8] that lies upstream of tau-induced neurodegeneration [3, 5, 9, 10].”
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 [5]
Combined reduction of both Aβ and tau, but not Aβ alone, improves cognition in a mouse model with both plaques and tangles.
“A combined reduction of both Aβ and tau, but not Aβ alone, was found to improve cognition in a mouse model with both plaques and tangles (Oddo et al., 2004).”
From CIP2A Causes Tau/APP Phosphorylation, Synaptopathy, and Memory Deficits in Alzheimer’s Disease (2018) · cites this paper as Oddo et al., 2004
Experimental therapies such as Aβ immunotherapy reduce cerebral Aβ and improve behavior in transgenic mouse models of AD-like cerebral β-amyloidosis.
“Experimental therapies, such as Aβ immunotherapy [8, 53, 138, 164, 178], were not only shown to reduce cerebral Aβ, but even more importantly, to improve behavior in transgenic mouse models of AD-like cerebral β-amyloidosis.”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [138]

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Authors: Oddo, S., Billings, L., Kesslak, J. P., Cribbs, D. H., & LaFerla, F. M.
Affiliations: University of California, Irvine (US)
Corresponding author: LaFerla, Frank M.
ORCID: Oddo, Salvatore
Billings, Lauren
Cribbs, David H.
LaFerla, Frank M.
Venue: Neuron
Publisher: Elsevier BV
Published: 2004-08
Volume: 43
Issue: 3
Pages: 321-332
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/j.neuron.2004.07.003
OpenAlex: W2121448546
Cited by: 780
References: 34
Citations by year: 2026: 5 · 2025: 5 · 2024: 13 · 2023: 13 · 2022: 12 · 2021: 21 · 2020: 27 · 2019: 24 · 2018: 27 · 2017: 25 · 2016: 24 · 2015: 20 · 2014: 44 · 2013: 38 · 2012: 57
FWCI: 39.05
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3272 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (AG0212982)
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: amyloid-beta immunotherapy, Alzheimer's disease, tau hyperphosphorylation, tau aggregates, proteasome, amyloid plaques, neurofibrillary tangles, 3xTg-AD mice, antibody treatment
MeSH terms: Alzheimer Disease, Animals, Antibodies, Cysteine Endopeptidases, Female, Hippocampus, Injections, Intraventricular, Intracellular Fluid, Male, Mice, Transgenic, Multienzyme Complexes, Phosphorylation, Amyloid beta-Peptides, tau Proteins, Alzheimer Vaccines, Extracellular Fluid, Proteasome Endopeptidase Complex, Mice

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Aβ Immunotherapy Leads to Clearance of Early, but Not Late, Hyperphosphorylated Tau Aggregates via the Proteasome

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