β-Amyloid Monomers Are Neuroprotective
Open accessAbstract
The 42-aa-long beta-amyloid protein--Abeta(1-42)--is thought to play a central role in the pathogenesis of Alzheimer's disease (AD) (Walsh and Selkoe, 2007). Data from AD brain (Shankar et al., 2008), transgenic APP (amyloid precursor protein)-overexpressing mice (Lesné et al., 2006), and neuronal cultures treated with synthetic Abeta peptides (Lambert et al., 1998) indicate that self-association of Abeta(1-42) monomers into soluble oligomers is required for neurotoxicity. The function of monomeric Abeta(1-42) is unknown. The evidence that Abeta(1-42) is present in the brain and CSF of normal individuals suggests that the peptide is physiologically active (Shoji, 2002). Here we show that synthetic Abeta(1-42) monomers support the survival of developing neurons under conditions of trophic deprivation and protect mature neurons against excitotoxic death, a process that contributes to the overall neurodegeneration associated with AD. The neuroprotective action of Abeta(1-42) monomers was mediated by the activation of the PI-3-K (phosphatidylinositol-3-kinase) pathway, and involved the stimulation of IGF-1 (insulin-like growth factor-1) receptors and/or other receptors of the insulin superfamily. Interestingly, monomers of Abeta(1-42) carrying the Arctic mutation (E22G) associated with familiar AD (Nilsberth et al., 2001) were not neuroprotective. We suggest that pathological aggregation of Abeta(1-42) may also cause neurodegeneration by depriving neurons of the protective activity of Abeta(1-42) monomers. This "loss-of-function" hypothesis of neuronal death should be taken into consideration when designing therapies aimed at reducing Abeta burden.
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Relative levels of Aβ42 to Aβ40 appear to influence the mechanism of oligomerization, with higher levels of Aβ40 in normal individuals likely impeding formation of stable toxic oligomers.
“Relative levels of Aβ42 to Aβ40 appear to influence the mechanism of oligomerization, with higher levels of Aβ40 in normal individuals likely impeding formation of stable toxic oligomers (Giuffrida et al., 2009).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Giuffrida et al., 2009
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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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- Authors
- Giuffrida, M. L., Caraci, F., Pignataro, B., Cataldo, S., De Bona, P., Bruno, V., Molinaro, G., Pappalardo, G., Messina, A., Palmigiano, A., Garozzo, D., Nicoletti, F., Rizzarelli, E., & Copani, A.
- Affiliations
- University of Catania (IT)
- University of Palermo (IT)
- Istituto Neurologico Mediterraneo (IT)
- Institute of Biostructure and Bioimaging (IT)
- National Research Council (IT)
- ORCID
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2009-08-26
- Volume
- 29
- Issue
- 34
- Pages
- 10582-10587
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6665714
- OpenAlex
- W1991988242
- Cited by
- 421
- References
- 33
- Citations by year
- 2026: 10 · 2025: 19 · 2024: 30 · 2023: 27 · 2022: 21 · 2021: 34 · 2020: 23 · 2019: 21 · 2018: 27 · 2017: 30 · 2016: 22 · 2015: 23 · 2014: 31 · 2013: 23 · 2012: 18
- FWCI
- 17.73
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Nova Science Publishers (Nova Science Publishers, Inc.) (submittedVersion, other-oa)
- IRIS Research product catalog (Sapienza University of Rome) (submittedVersion)
- Funders
- Università di Catania
- Topics
- Health Sciences › Medicine › Physiology › 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
- amyloid-beta 42, neuroprotection, Alzheimer's disease, excitotoxicity, IGF-1 receptor, Arctic mutation, amyloid fibril formation, neurodegeneration
- MeSH terms
- Analysis of Variance, Animals, Butadienes, Cells, Cultured, Cerebral Cortex, Dose-Response Relationship, Drug, Embryo, Mammalian, Enzyme Inhibitors, Neurons, Nitriles, Peptide Fragments, Podophyllotoxin, N-Methylaspartate, Amyloid beta-Peptides, Cell Death, Excitatory Amino Acid Agonists, Neuroprotective Agents, Tyrphostins, Rats
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