Ford_et_al-2017-FEBS_Letters (1).pdf (653.65 kB)
Structure dependent effects of Amyloid-ß on long-term memory in Lymnaea stagnalis
Version 2 2023-06-12, 08:40
Version 1 2023-06-09, 05:37
journal contribution
posted on 2023-06-12, 08:40 authored by Lenzie Ford, Michael CrossleyMichael Crossley, Devkee M Vadukul, György Kemenes, Louise SerpellLouise SerpellAmyloid-ß (Aß) peptides are implicated in the causation of memory loss, neuronal impairment, and neurodegeneration in Alzheimer's disease. Our recent work revealed that Aß 1–42 and Aß 25–35 inhibit long-term memory (LTM) recall in Lymnaea stagnalis (pond snail) in the absence of cell death. Here, we report the characterization of the active species prepared under different conditions, describe which Aß species is present in brain tissue during the behavioral recall time point and relate the sequence and structure of the oligomeric species to the resulting neuronal properties and effect on LTM. Our results suggest that oligomers are the key toxic Aß1–42 structures, which likely affect LTM through synaptic plasticity pathways, and that Aß 1–42 and Aß 25–35 cannot be used as interchangeable peptides.
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Publication status
- Published
File Version
- Published version
Journal
FEBS LettersISSN
0014-5793Publisher
ElsevierExternal DOI
Issue
9Volume
591Page range
1236-1246Department affiliated with
- Biochemistry Publications
Research groups affiliated with
- Dementia Research Group Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2017-04-04First Open Access (FOA) Date
2017-04-04First Compliant Deposit (FCD) Date
2017-04-04Usage metrics
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