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Single-molecule imaging reveals aβ42:aβ40 ratio-dependent oligomer growth on neuronal processes
Johnson RD, Schauerte JA, Chang CC, Wisser KC, Althaus JC, Carruthers CJ, Sutton MA, Steel DG et al.. Biophysical journal, 2013-02-01
Topic: Brain proteins, microglia and lab models
Soluble oligomers of the amyloid-β peptide have been implicated as proximal neurotoxins in Alzheimer's disease. However, the identity of the neurotoxic aggregate(s) and the mechanisms by which these species induce neuronal dysfunction remain uncertain. Physiologically relevant experimentation is hindered by the low endogenous concentrations of the peptide, the metastability of Aβ oligomers, and the wide range of observed interactions between Aβ and biological membranes. Single-molecule microscopy represents one avenue for overcoming these challenges. Using this technique, we find that Aβ binds to primary rat hippocampal neurons at physiological concentrations. Although amyloid-β(1-40) as well as amyloid-β(1-42) initially form larger oligomers on neurites than on glass slides, a 1:1 mix of the two peptides result in smaller neurite-bound oligomers than those detected on-slide or for either peptide alone. With 1 nM peptide in solution, Aβ40 oligomers do not grow over the course of 48 h, Aβ42 oligomers grow slightly, and oligomers of a 1:1 mix grow substantially. Evidently, small Aβ oligomers are capable of binding to neurons at physiological concentrations and grow at rates dependent on local Aβ42:Aβ40 ratios. These results are intriguing in light of the increased Aβ42:Aβ40 ratios shown to correlate with familial Alzheimer's disease mutations.
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APA 7th
Johnson, R. D., Schauerte, J. A., Chang, C. C., Wisser, K. C., Althaus, J. C., Carruthers, C. J., et al. (2013). Single-molecule imaging reveals aβ42:aβ40 ratio-dependent oligomer growth on neuronal processes. Biophysical journal. https://doi.org/10.1016/j.bpj.2012.12.051
Vancouver
Johnson RD, Schauerte JA, Chang CC, Wisser KC, Althaus JC, Carruthers CJ, et al. Single-molecule imaging reveals aβ42:aβ40 ratio-dependent oligomer growth on neuronal processes. Biophysical journal. 2013. doi:10.1016/j.bpj.2012.12.051. PMID: 23442968.
BibTeX
@article{johnson2013-23442968,
author = {Johnson, R. D. and Schauerte, J. A. and Chang, C. C. and Wisser, K. C. and Althaus, J. C. and Carruthers, C. J. and Sutton, M. A. and Steel, D. G. and others},
title = {{Single-molecule imaging reveals aβ42:aβ40 ratio-dependent oligomer growth on neuronal processes}},
journal = {Biophysical journal},
year = {2013},
doi = {10.1016/j.bpj.2012.12.051},
pmid = {23442968},
url = {https://doi.org/10.1016/j.bpj.2012.12.051}
}
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Key findings
- Although amyloid-β(1-40) as well as amyloid-β(1-42) initially form larger oligomers on neurites than on glass slides, a 1:1 mix of the two peptides result in smaller neurite-bound oligomers than those detected on-slide or for either peptide alone.
- These results are intriguing in light of the increased Aβ42:Aβ40 ratios shown to correlate with familial Alzheimer's disease mutations.
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Study details
- Evidence strengthLow
How this study scored 36/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomised / blinded because the record does not state it. We have no data on journal's citation record, times cited, citations per year, impact for its field and year, cited by studies here, still being cited, senior author's track record, institution's track record and multi-centre collaboration, so those were left out: it earned 21 of the 58 points we could judge it on, which is 36 out of 100.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Biophysical journal) |
| Journal's citation record | — / 4 | No journal record from OpenAlex — left out of this score |
| Study design | 0 / 12 | No study design recorded — scores zero, not guessed (not stated in the record — scored 0) |
| Strength of evidence | 1 / 5 | Rated “low” in our summary |
| Peer-review validation | 10 / 10 | Peer-reviewed. Published as an article in a named peer-reviewed journal. |
| How recent | 1 / 5 | 2013 — within 20 year(s) of the newest study here |
| Sample size | 0 / 4 | Participant count not stated — scores zero (not stated in the record — scored 0) |
| Effect reported | 0 / 3 | No effect size reported — scores zero (not stated in the record — scored 0) |
| Studied in people | 0 / 3 | Not stated whether this was studied in people — scores zero (not stated in the record — scored 0) |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | — / 7 | No citation count (not found in OpenAlex) — left out of this score |
| Citations per year | — / 5 | No citation count or no year — left out of this score |
| Impact for its field and year | — / 6 | No field-weighted citation impact (OpenAlex has none yet) — left out of this score |
| Cited by studies here | — / 6 | Not yet checked against this library's citation graph — left out of this score |
| Still being cited | — / 4 | No yearly citation counts — left out of this score |
| Senior author's track record | — / 4 | Senior author's record not available — left out of this score |
| Institution's track record | — / 3 | No institution listed in OpenAlex — left out of this score |
| Multi-centre collaboration | — / 3 | Institutions not listed — left out of this score |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 23442968) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Points | 21 / 58 | Scored on 11 of 20 parts. We have no data for the rest, so they are left out: 21 of the 58 points we could judge it on is 36 out of 100. |
| Total | 36 / 100 | — |
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2 studies in the library carry the topic tag “oligomers”; these are this study's neighbours in a fixed, alphabetical-by-hash tour of them, not the closest in content. All 2 tagged studies.