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Amyloid-beta protein oligomer at low nanomolar concentrations activates microglia and induces microglial neurotoxicity
Maezawa I, Zimin PI, Wulff H, Jin LW.. The Journal of biological chemistry, 2010-10-22
Topic: Brain proteins, microglia and lab models
Neuroinflammation and associated neuronal dysfunction mediated by activated microglia play an important role in the pathogenesis of Alzheimer disease (AD). Microglia are activated by aggregated forms of amyloid-β protein (Aβ), usually demonstrated in vitro by stimulating microglia with micromolar concentrations of fibrillar Aβ, a major component of amyloid plaques in AD brains. Here we report that amyloid-β oligomer (AβO), at 5-50 nm, induces a unique pattern of microglia activation that requires the activity of the scavenger receptor A and the Ca(2+)-activated potassium channel KCa3.1.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Maezawa, I., Zimin, P. I., Wulff, H., & Jin, L. W. (2011). Amyloid-beta protein oligomer at low nanomolar concentrations activates microglia and induces microglial neurotoxicity. The Journal of biological chemistry. https://doi.org/10.1074/jbc.m110.135244
Vancouver
Maezawa I, Zimin PI, Wulff H, Jin LW. Amyloid-beta protein oligomer at low nanomolar concentrations activates microglia and induces microglial neurotoxicity. The Journal of biological chemistry. 2011. doi:10.1074/jbc.m110.135244. PMID: 20971854.
BibTeX
@article{maezawa2011-20971854,
author = {Maezawa, I. and Zimin, P. I. and Wulff, H. and Jin, L. W.},
title = {{Amyloid-beta protein oligomer at low nanomolar concentrations activates microglia and induces microglial neurotoxicity}},
journal = {The Journal of biological chemistry},
year = {2011},
doi = {10.1074/jbc.m110.135244},
pmid = {20971854},
url = {https://doi.org/10.1074/jbc.m110.135244}
}
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Key findings
- Microglia are activated by aggregated forms of amyloid-β protein (Aβ), usually demonstrated in vitro by stimulating microglia with micromolar concentrations of fibrillar Aβ, a major component of amyloid plaques in AD brains.
- Here we report that amyloid-β oligomer (AβO), at 5-50 nm, induces a unique pattern of microglia activation that requires the activity of the scavenger receptor A and the Ca(2+)-activated potassium channel KCa3.1.
- AβO treatment induced an activated morphological and biochemical profile of microglia, including activation of p38 MAPK and nuclear factor κB.
- Interestingly, although increasing nitric oxide (NO) production, AβO did not increase several proinflammatory mediators commonly induced by lipopolyliposaccharides or fibrillar Aβ, suggesting that AβO stimulates both common and divergent pathways of microglia activation.
Why it matters
In laboratory microglia, amyloid-beta oligomer at 5-50 nM activated microglia and induced neurotoxicity through the scavenger receptor A and the KCa3.1 channel. This is cell research on a mechanism, not a treatment or cure for Alzheimer's disease.
Study details
- Evidence strengthLow
How this study scored 43/100
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.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (The Journal of biological chemistry) |
| Journal's citation record | 4 / 4 | Journal of Biological Chemistry: journal h-index 780 (OpenAlex, 2026-10-29) |
| 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 | 2011 — 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 | 5 / 7 | Cited 279 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 16.4 citations a year over 17 year(s) since 2011 |
| Impact for its field and year | 3 / 6 | Cited 7.8× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 2 / 6 | Cited by 5 other studies in this library |
| Still being cited | 2 / 4 | Cited 34 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 2 / 4 | Last-listed author Lee‐Way Jin: h-index 32 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | University of California, Davis: institution h-index 1,257 (OpenAlex) |
| Multi-centre collaboration | 0 / 3 | OpenAlex lists 1 institution(s) in 1 country — scores zero (affiliation lists can be incomplete) |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 20971854) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 43 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1074/jbc.m110.135244
- PubMed: 20971854
- Original source →
- Free full text: Journal of Biological Chemistry →
Full text: free to read — OpenAlex lists this copy as free to read: the link above (checked 6 Feb 1020).
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