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Rodent Aβ Modulates the Solubility and Distribution of Amyloid Deposits in Transgenic Mice
Open accessAbstract
The amino acid sequence of amyloid precursor protein (APP) is highly conserved, and age-related A beta aggregates have been described in a variety of vertebrate animals, with the notable exception of mice and rats. Three amino acid substitutions distinguish mouse and human A beta that might contribute to their differing properties in vivo. To examine the amyloidogenic potential of mouse A beta, we studied several lines of transgenic mice overexpressing wild-type mouse amyloid precursor protein (moAPP) either alone or in conjunction with mutant PS1 (PS1dE9). Neither overexpression of moAPP alone nor co-expression with PS1dE9 caused mice to develop Alzheimer-type amyloid pathology by 24 months of age. We further tested whether mouse A beta could accelerate the deposition of human A beta by crossing the moAPP transgenic mice to a bigenic line expressing human APPswe with PS1dE9. The triple transgenic animals (moAPP x APPswe/PS1dE9) produced 20% more A beta but formed amyloid deposits no faster and to no greater extent than APPswe/PS1dE9 siblings. Instead, the additional mouse A beta increased the detergent solubility of accumulated amyloid and exacerbated amyloid deposition in the vasculature. These findings suggest that, although mouse A beta does not influence the rate of amyloid formation, the incorporation of A beta peptides with differing sequences alters the solubility and localization of the resulting aggregates.
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“For example, multiple reports indicate that there are endogenous differences in rodent and human APP (136), which could significantly alter the production on Aβ after TBI.”
From The Inflammatory Continuum of Traumatic Brain Injury and Alzheimer’s Disease (2018) · cites this paper as [136]
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Sorted by citations
Alzheimer's Disease and the Amyloid-β Peptide
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“An additional concern is that in the majority of these models the rodent Aβ is present which can affect the assembly of the human sequence peptide in vitro and in vivo [120-122].”
Myelin dysfunction drives amyloid-β deposition in models of Alzheimer’s disease
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“Transfection of human APP is necessary [153], and the trisomy16 murine model (where no A deposition is found) suggests that hAPP has to be mutated to obtain a reliable and abundant deposition.”
BackgroundMainardi, M., Garbo, A. D., Caleo, M., Berardi, N., Sale, A., & Maffei, L. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00001 · Cited by 550
“It is also worth noting that, due to three mutations in the aminoacilyc sequence, murine Aβ does not aggregate to form amyloid plaques (Jankowsky et al., 2007).”
BackgroundSystemic immune challenges trigger and drive Alzheimer-like neuropathology in mice
Krstic, D., Madhusudan, A., Doehner, J., Vogel, P., Notter, T., Imhof, C., Manalastas, A., Hilfiker, M., Pfister, S., Schwerdel, C., et al. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-151 · Cited by 400
“The absence of significant accumulations of mouse Aβ peptides in these APP deposits might be due to the different aggregation properties of the rodent compared with the human form [55], or might be linked to the premature age and disease stage in these animals (15 months).”
Background
Metadata
- Authors
- Jankowsky, J. L., Younkin, L. H., Gonzales, V., Fadale, D. J., Slunt, H. H., Lester, H. A., Younkin, S. G., & Borchelt, D. R.
- Affiliations
- California Institute of Technology (US)
- Mayo Clinic (US)
- Johns Hopkins University (US)
- University of Florida (US)
- Corresponding author
- Jankowsky, Joanna L.
- Borchelt, David R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-08
- Volume
- 282
- Issue
- 31
- Pages
- 22707-22720
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC4435736
- OpenAlex
- W2156398762
- Cited by
- 122
- References
- 56
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 5 · 2023: 8 · 2022: 4 · 2021: 13 · 2020: 9 · 2019: 3 · 2018: 7 · 2017: 4 · 2016: 3 · 2015: 7 · 2014: 4 · 2013: 6 · 2012: 10
- FWCI
- 3.80
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- John Douglas French Alzheimer's Foundation
- National Institutes of Health
- National Institute on Aging (K01 AG26144-01, AG06656, 1 P01 AG-98-003, K01AG026144, 1 P50 AG-14-248)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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, amyloid precursor protein, APPswe, transgenic mice, Alzheimer's disease, amyloid deposition, detergent solubility, vascular amyloid, triple transgenic mice
- MeSH terms
- Amino Acid Sequence, Amyloid, Animals, Humans, Mice, Inbred C57BL, Mice, Transgenic, Molecular Sequence Data, Peptides, Solubility, Amyloid beta-Peptides, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Transgenes, Mice, Presenilin-1
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