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Cited by 67Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Novel rat Alzheimer's disease models based on AAV-mediated gene transfer to selectively increase hippocampal Aβ levels

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Lawlor, Patricia A, Bland, Ross J, Das, Pritam, Price, Robert W, Holloway, Vallie, Smithson, Lisa, Dicker, Bridget L, During, Matthew J +2 more·2007·Molecular Neurodegeneration
DOI 10.1186/1750-1326-2-11PMC PMC1906777
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Abstract

BACKGROUND: Alzheimer's disease (AD) is characterized by a decline in cognitive function and accumulation of amyloid-beta peptide (Abeta) in extracellular plaques. Mutations in amyloid precursor protein (APP) and presenilins alter APP metabolism resulting in accumulation of Abeta42, a peptide essential for the formation of amyloid deposits and proposed to initiate the cascade leading to AD. However, the role of Abeta40, the more prevalent Abeta peptide secreted by cells and a major component of cerebral Abeta deposits, is less clear. In this study, virally-mediated gene transfer was used to selectively increase hippocampal levels of human Abeta42 and Abeta40 in adult Wistar rats, allowing examination of the contribution of each to the cognitive deficits and pathology seen in AD. RESULTS: Adeno-associated viral (AAV) vectors encoding BRI-Abeta cDNAs were generated resulting in high-level hippocampal expression and secretion of the specific encoded Abeta peptide. As a comparison the effect of AAV-mediated overexpression of APPsw was also examined. Animals were tested for development of learning and memory deficits (open field, Morris water maze, passive avoidance, novel object recognition) three months after infusion of AAV. A range of impairments was found, with the most pronounced deficits observed in animals co-injected with both AAV-BRI-Abeta40 and AAV-BRI-Abeta42. Brain tissue was analyzed by ELISA and immunohistochemistry to quantify levels of detergent soluble and insoluble Abeta peptides. BRI-Abeta42 and the combination of BRI-Abeta40+42 overexpression resulted in elevated levels of detergent-insoluble Abeta. No significant increase in detergent-insoluble Abeta was seen in the rats expressing APPsw or BRI-Abeta40. No pathological features were noted in any rats, except the AAV-BRI-Abeta42 rats which showed focal, amorphous, Thioflavin-negative Abeta42 deposits. CONCLUSION: The results show that AAV-mediated gene transfer is a valuable tool to model aspects of AD pathology in vivo, and demonstrate that whilst expression of Abeta42 alone is sufficient to initiate Abeta deposition, both Abeta40 and Abeta42 may contribute to cognitive deficits.

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  • The apparent lack of a consistent trend in behavioral changes across behavioral tests in AAV-BRI2-Aβ1-42 rats and their apparently unimpaired spatial and short-term object recognition memories are consistent with the lack of cognitive impairment in BRI2-Aβ1-42 mice observed in the present study.

    “The apparent lack of a consistent trend in behavioral changes across behavioral tests in AAV-BRI2-Aβ1-42 rats and apparently their unimpaired spatial and short-term object recognition memories [58] are consistent with the lack of cognitive impairment in BRI2-Aβ1-42 mice observed in the present study.”

    From Normal cognition in transgenic BRI2-Aβ mice (2013) · cites this paper as [58]

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  • Selective expression of Aβ1-42 and Aβ1-40 in the brain using virally-mediated gene transfer of BRI2-Aβ fusion proteins modified behavior in a rat model.

    “Interestingly, it has been reported that selective expression of Aβ1-42 and Aβ1-40 in the brain using virally-mediated gene transfer of BRI2-Aβ fusion proteins modified behavior in a rat model [58].”

    From Normal cognition in transgenic BRI2-Aβ mice (2013) · cites this paper as [58]

  • The reported behavioral outcomes in the rat model of virally-mediated BRI2-Aβ expression were not fully consistent with memory impairment.

    “However, the reported behavioral outcomes were not fully consistent with memory impairment.”

    From Normal cognition in transgenic BRI2-Aβ mice (2013) · cites this paper as [58]

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Cited by

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Authors
Lawlor, P. A., Bland, R. J., Das, P., Price, R. W., Holloway, V., Smithson, L., Dicker, B. L., During, M. J., Young, D., & Golde, T. E.
Affiliations
  • University of Auckland (NZ)
  • Mayo Clinic (US)
Corresponding author
Lawlor, Patricia A
ORCID
Venue
Molecular Neurodegeneration
Publisher
Springer Science and Business Media LLC
Published
2007
Volume
2
Issue
1
Pages
11
ISSN
1750-1326 (ISSN-L)
DOI
10.1186/1750-1326-2-11
PMC
PMC1906777
OpenAlex
W2167064901
Cited by
67
References
10
Citations by year
2025: 3 · 2024: 1 · 2023: 1 · 2022: 4 · 2021: 4 · 2020: 4 · 2019: 3 · 2018: 4 · 2017: 5 · 2016: 3 · 2015: 1 · 2014: 4 · 2013: 7 · 2012: 3
FWCI
2.91
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Molecular Neurodegeneration (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • The Knowledge Bank (The Ohio State University) (submittedVersion, cc-by)
  • ResearchSpace (University of Auckland) (submittedVersion, cc-by)
Funders
National Institute on Aging
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, amyloid-beta, amyloid-beta 42, Aβ40, AAV gene delivery, hippocampus, transgenic rats, cognitive impairment, learning and memory, amyloid plaques

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