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Sphingolipid-modulated exosome secretion promotes clearance of amyloid-β by microglia
Yuyama K, Sun H, Mitsutake S, Igarashi Y.. The Journal of biological chemistry, 2012-02-02
Topic: Brain proteins, microglia and lab models
Amyloid β-peptide (Aβ), the pathogenic agent of Alzheimer disease, is a physiological metabolite whose levels are constantly controlled in normal brain. Recent studies have demonstrated that a fraction of extracellular Aβ is associated with exosomes, small membrane vesicles of endosomal origin, although the fate of Aβ in association with exosome is largely unknown. In this study, we identified novel roles for neuron-derived exosomes acting on extracellular Aβ, i.e. exosomes drive conformational changes in Aβ to form nontoxic amyloid fibrils and promote uptake of Aβ by microglia.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Yuyama, K., Sun, H., Mitsutake, S., & Igarashi, Y. (2012). Sphingolipid-modulated exosome secretion promotes clearance of amyloid-β by microglia. The Journal of biological chemistry. https://doi.org/10.1074/jbc.m111.324616
Vancouver
Yuyama K, Sun H, Mitsutake S, Igarashi Y. Sphingolipid-modulated exosome secretion promotes clearance of amyloid-β by microglia. The Journal of biological chemistry. 2012. doi:10.1074/jbc.m111.324616. PMID: 22303002.
BibTeX
@article{yuyama2012-22303002,
author = {Yuyama, K. and Sun, H. and Mitsutake, S. and Igarashi, Y.},
title = {{Sphingolipid-modulated exosome secretion promotes clearance of amyloid-β by microglia}},
journal = {The Journal of biological chemistry},
year = {2012},
doi = {10.1074/jbc.m111.324616},
pmid = {22303002},
url = {https://doi.org/10.1074/jbc.m111.324616}
}
Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. Check the citation against the original before you use it.
Key findings
- Recent studies have demonstrated that a fraction of extracellular Aβ is associated with exosomes, small membrane vesicles of endosomal origin, although the fate of Aβ in association with exosome is largely unknown.
- In this study, we identified novel roles for neuron-derived exosomes acting on extracellular Aβ, i.e. exosomes drive conformational changes in Aβ to form nontoxic amyloid fibrils and promote uptake of Aβ by microglia.
- The Aβ internalized together with exosomes was further transported to lysosomes and degraded.
- We also found that blockade of phosphatidylserine on the surface of exosomes by annexin V not only prevented exosome uptake but also suppressed Aβ incorporation into microglia.
Why it matters
This laboratory study reports that neuron-derived exosomes drive amyloid-beta into nontoxic fibrils and promote its uptake by microglia. It is a cell-level mechanism study and reports no treatment, cure or prevention for Alzheimer's disease.
Study details
- Evidence strengthLow
How this study scored 47/100
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 | 2012 — 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 | 6 / 7 | Cited 596 times (OpenAlex, 2026-10-10) |
| Citations per year | 4 / 5 | 37.2 citations a year over 16 year(s) since 2012 |
| Impact for its field and year | 4 / 6 | Cited 13.8× 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 | 3 / 4 | Cited 112 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 3 / 4 | Last-listed author Yasuyuki Igarashi: h-index 68 (OpenAlex, whole career) |
| Institution's track record | 0 / 3 | Hokkaido University: institution h-index 656 (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 22303002) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 47 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1074/jbc.m111.324616
- PubMed: 22303002
- 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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