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The p75 Neurotrophin Receptor Promotes Amyloid-β(1-42)-Induced Neuritic Dystrophy In Vitro and In Vivo
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Oligomeric forms of amyloid-beta (Abeta) are thought to play a causal role in Alzheimer's disease (AD), and the p75 neurotrophin receptor (p75(NTR)) has been implicated in Abeta-induced neurodegeneration. To further define the functions of p75(NTR) in AD, we examined the interaction of oligomeric Abeta(1-42) with p75(NTR), and the effects of that interaction on neurite integrity in neuron cultures and in a chronic AD mouse model. Atomic force microscopy was used to ascertain the aggregated state of Abeta, and fluorescence resonance energy transfer analysis revealed that Abeta oligomers interact with the extracellular domain of p75(NTR). In vitro studies of Abeta-induced death in neuron cultures isolated from wild-type and p75(NTR-/-) mice, in which the p75(NTR) extracellular domain is deleted, showed reduced sensitivity of mutant cells to Abeta-induced cell death. Interestingly, Abeta-induced neuritic dystrophy and activation of c-Jun, a known mediator of Abeta-induced deleterious signaling, were completely prevented in p75(NTR-/-) neuron cultures. Thy1-hAPP(Lond/Swe) x p75(NTR-/-) mice exhibited significantly diminished hippocampal neuritic dystrophy and complete reversal of basal forebrain cholinergic neurite degeneration relative to those expressing wild-type p75(NTR). Abeta levels were not affected, suggesting that removal of p75(NTR) extracellular domain reduced the ability of excess Abeta to promote neuritic degeneration. These findings indicate that although p75(NTR) likely does not mediate all Abeta effects, it does play a significant role in enabling Abeta-induced neurodegeneration in vitro and in vivo, establishing p75(NTR) as an important therapeutic target for AD.
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“Other putative receptors/co-receptors involved in neuronal binding of Aβ oligomers include the p75 neurotrophin receptor (p75NTR) (Knowles et al., 2009), the receptor for advanced glycation end products (RAGE) (Sturchler et al., 2008), nicotinic acetylcholine receptors (Magdesian et al., 2005) and Frizzled (Magdesian et al., 2008).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Knowles et al., 2009
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Metadata
- Authors
- Knowles, J. K., Rajadas, J., Nguyen, T.-V. V., Yang, T., LeMieux, M. C., Vander Griend, L., Ishikawa, C., Massa, S. M., Wyss-Coray, T., & Longo, F. M.
- Affiliations
- Stanford University (US)
- University of North Carolina at Chapel Hill (US)
- VA Palo Alto Health Care System (US)
- San Francisco VA Medical Center (US)
- Corresponding author
- Longo, Frank M.
- ORCID
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2009-08-26
- Volume
- 29
- Issue
- 34
- Pages
- 10627-10637
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC2771439
- OpenAlex
- W2090434536
- Cited by
- 184
- References
- 70
- Citations by year
- 2026: 10 · 2025: 6 · 2024: 6 · 2023: 4 · 2022: 9 · 2021: 14 · 2020: 11 · 2019: 11 · 2018: 4 · 2017: 10 · 2016: 17 · 2015: 14 · 2014: 17 · 2013: 15 · 2012: 12
- FWCI
- 7.73
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Alzheimer's Association
- U.S. Public Health Service (F30 NA051971)
- National Institute of Neurological Disorders and Stroke (F30NS051971)
- 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
- p75 neurotrophin receptor, amyloid-beta 42, Alzheimer's disease, neuritic dystrophy, amyloid-beta oligomers, c-Jun activation, cholinergic neurons, hippocampus, APP transgenic mice, therapeutic target
- MeSH terms
- Acetylcholinesterase, Alzheimer Disease, Analysis of Variance, Animals, Cell Survival, Cells, Cultured, Disease Models, Animal, Embryo, Mammalian, Enzyme-Linked Immunosorbent Assay, Exons, Hippocampus, Humans, Mice, Inbred C57BL, Mice, Transgenic, Mutation, Nerve Degeneration, Neurons, Peptide Fragments, Spectrophotometry, Atomic, Amyloid beta-Peptides, Neurites, Prosencephalon, Amyloid beta-Protein Precursor, Receptor, Nerve Growth Factor, Fluorescence Resonance Energy Transfer, Mice
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