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Interaction of human and mouse Aβ peptides

Fung, Justin, Frost, David, Chakrabartty, Avijit, McLaurin, JoAnne·2004·Journal of Neurochemistry

Abstract

Transgenic mice over‐expressing mutant human amyloid precursor protein have become an important tool for research on Alzheimer's disease (AD) and, in particular, for therapeutic screening. Many models have reported formation of amyloid plaques with age as is detected in AD. However, the plaques generated in transgenic mice are more soluble than human plaques. Differences in solubility may occur for a number of reasons; one proposal is the presence of murine Aβ peptides within the CNS milieu. Here, we report the interaction of human and murine Aβ peptides, Aβ40 and Aβ42, utilizing a fluorescence assay to monitor formation of mixed pre‐fibrillar aggregates, electron microscopy to examine morphological characteristics and detergent solubility to monitor stability. Our results demonstrate that interspecies Aβ aggregates and fibres are readily formed and are more stable than homogenous human fibres. Furthermore, these results suggest that the presence of endogenous murine Aβ in human APP transgenic mice does not account for the increased solubility of plaques.

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Crossref · 10.1111/j.1471-4159.2004.02828.x

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Research works printed but not linked: 24

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Metadata

Authors
Fung, J., Frost, D., Chakrabartty, A., & McLaurin, J.
Venue
Journal of Neurochemistry
Publisher
Wiley
Published
2004-12
Volume
91
Issue
6
Pages
1398-1403
ISSN
  • 0022-3042
  • 1471-4159
Cited by
46
References
3
Language
en

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CoChat. (2026). Citation check: Interaction of human and mouse Aβ peptides. https://app.cochat.ai/papers/10.1111/j.1471-4159.2004.02828.x
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Fung, J., Frost, D., Chakrabartty, A., & McLaurin, J. (2004). Interaction of human and mouse Aβ peptides. Journal of Neurochemistry. https://doi.org/10.1111/j.1471-4159.2004.02828.x