Structure-dependent effects of amyloid-$\beta$ on long-term memory in Lymnaea stagnalis. Ford, L., Crossley, M., Vadukul, D. M., Kemenes, G., & Serpell, L. C. FEBS Letters, 591(9):1236–1246, may, 2017.
Structure-dependent effects of amyloid-$\beta$ on long-term memory in Lymnaea stagnalis [link]Paper  doi  abstract   bibtex   
Amyloid-$\beta$ (A$\beta$) peptides are implicated in the causation of memory loss, neuronal impairment, and neurodegeneration in Alzheimer's disease. Our recent work revealed that A$\beta$ 1–42 and A$\beta$ 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 A$\beta$ 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 A$\beta$1–42 structures, which likely affect LTM through synaptic plasticity pathways, and that A$\beta$ 1–42 and A$\beta$ 25–35 cannot be used as interchangeable peptides.
@article{Ford2017,
abstract = {Amyloid-$\beta$ (A$\beta$) peptides are implicated in the causation of memory loss, neuronal impairment, and neurodegeneration in Alzheimer's disease. Our recent work revealed that A$\beta$ 1–42 and A$\beta$ 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 A$\beta$ 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 A$\beta$1–42 structures, which likely affect LTM through synaptic plasticity pathways, and that A$\beta$ 1–42 and A$\beta$ 25–35 cannot be used as interchangeable peptides.},
author = {Ford, Lenzie and Crossley, Michael and Vadukul, Devkee M. and Kemenes, Gy{\"{o}}rgy and Serpell, Louise C.},
doi = {10.1002/1873-3468.12633},
file = {:C$\backslash$:/Users/julia/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Ford et al. - 2017 - Structure-dependent effects of amyloid-$\beta$ on long-term memory in Lymnaea stagnalis.pdf:pdf},
isbn = {4955139574},
issn = {00145793},
journal = {FEBS Letters},
keywords = {Lymnaea,amyloid beta,classical conditioning,long-term memory,oligomer},
month = {may},
number = {9},
pages = {1236--1246},
pmid = {28337747},
title = {{Structure-dependent effects of amyloid-$\beta$ on long-term memory in Lymnaea stagnalis}},
url = {http://doi.wiley.com/10.1002/1873-3468.12633},
volume = {591},
year = {2017}
}

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