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Cited by 213Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsDementia and Cognitive Impairment Research

The DOI matches its Crossref record; 128 of the 128 references it cites were found in a registry or an index.

Mouse Models of Alzheimer’s Disease

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Yokoyama, Miyabishara, Kobayashi, Honoka, Tatsumi, Lisa, Tomita, Taisuke·2022·Frontiers in Molecular Neuroscience
DOI 10.3389/fnmol.2022.912995PMC PMC9254908
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Abstract

Alzheimer’s disease (AD) is a neurodegenerative disorder characterized by memory loss and personality changes, eventually leading to dementia. The pathological hallmarks of AD are senile plaques and neurofibrillary tangles, which comprise abnormally aggregated β-amyloid peptide (Aβ) and hyperphosphorylated tau protein. To develop preventive, diagnostic, and therapeutic strategies for AD, it is essential to establish animal models that recapitulate the pathophysiological process of AD. In this review, we will summarize the advantages and limitations of various mouse models of AD, including transgenic, knock-in, and injection models based on Aβ and tau. We will also discuss other mouse models based on neuroinflammation because recent genetic studies have suggested that microglia are crucial in the pathogenesis of AD. Although each mouse model has its advantages and disadvantages, further research on AD pathobiology will lead to the establishment of more accurate mouse models, and accelerate the development of innovative therapeutics.

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Figure 1 Aβ production from APP. (A) Schematic depiction of the Aβ production pathway. APP is sequentially cleaved by β- and γ-secretases to release Aβ into the extracellular space. Aβ monomer is prone to aggregate, forming oligomers, protofibrils, and fibrils. (B) Diagram of the APP (above) and sequence of Aβ (below). The transmembrane segment (TM) is highlighted in yellow. The bold letters below the Aβ sequence indicate the missense FAD mutations within the Aβ sequence. The above and below the number of the Aβ sequence follow the numbering of the longest isoform of APP and Aβ amino acid sequence, respectively.
Figure 1 Aβ production from APP. (A) Schematic depiction of the Aβ production pathway. APP is sequentially cleaved by β- and γ-secretases to release Aβ into the extracellular space. Aβ monomer is prone to aggregate, forming oligomers, protofibrils, and fibrils. (B) Diagram of the APP (above) and sequence of Aβ (below). The transmembrane segment (TM) is highlighted in yellow. The bold letters below the Aβ sequence indicate the missense FAD mutations within the Aβ sequence. The above and below the number of the Aβ sequence follow the numbering of the longest isoform of APP and Aβ amino acid sequence, respectively.CC BY · PubMed Central
Figure 2 Tau isoforms in the human brain. (A) Schematic depiction of the formation of neurofibrillary tangles. Tau protein control stabilization of microtubules by kinases. Phosphorylated tau leads to microtubule disassembly. Irregular hyperphosphorylation of tau proteins results in the generation of insoluble tau oligomers, which then accumulate to form PHF, then NFT. (B) Schematic diagram of tau isoforms that are expressed in the adult human brain. MAPT gene encodes tau protein. The six tau isoforms are generated by splicing of exons 2, 3, and/or 10 that encode for N1 (blue), N2 (yellow), and R2 (red), respectively. The inclusion of exon 10 results in the generation of mRNA encoding 4R tau. The location of missense MAPT mutations utilized in the transgenic mice is shown.
Figure 2 Tau isoforms in the human brain. (A) Schematic depiction of the formation of neurofibrillary tangles. Tau protein control stabilization of microtubules by kinases. Phosphorylated tau leads to microtubule disassembly. Irregular hyperphosphorylation of tau proteins results in the generation of insoluble tau oligomers, which then accumulate to form PHF, then NFT. (B) Schematic diagram of tau isoforms that are expressed in the adult human brain. MAPT gene encodes tau protein. The six tau isoforms are generated by splicing of exons 2, 3, and/or 10 that encode for N1 (blue), N2 (yellow), and R2 (red), respectively. The inclusion of exon 10 results in the generation of mRNA encoding 4R tau. The location of missense MAPT mutations utilized in the transgenic mice is shown.CC BY · PubMed Central

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Metadata

Authors
Yokoyama, M., Kobayashi, H., Tatsumi, L., & Tomita, T.
Affiliations
The University of Tokyo (JP)
Corresponding author
Tomita, Taisuke
ORCID
Venue
Frontiers in Molecular Neuroscience
Publisher
Frontiers Media SA
Published
2022-06-21
Volume
15
Pages
912995-912995
ISSN
1662-5099 (ISSN-L)
DOI
10.3389/fnmol.2022.912995
PMC
PMC9254908
OpenAlex
W4283267746
Cited by
213
References
128
Citations by year
2026: 40 · 2025: 63 · 2024: 77 · 2023: 31 · 2022: 1
FWCI
5.91
Type
journal article
Language
en
Open access
Licence
Locations
  • Frontiers in Molecular Neuroscience (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Japan Society for the Promotion of Science
  • Japan Agency for Medical Research and Development
  • Moonshot Research and Development Program
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
  • Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords
Alzheimer's disease, mouse model, transgenic mice, knock-in mice, amyloid-beta, tau protein, neurofibrillary tangles, amyloid plaques, neuroinflammation, microglia

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