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Docosahexaenoic acid reduces amyloid beta production via multiple pleiotropic mechanisms
Grimm MO, Kuchenbecker J, Grösgen S, Burg VK, Hundsdörfer B, Rothhaar TL, Friess P, de Wilde MC et al.. The Journal of biological chemistry, 2011-02-15
Topic: Brain proteins, microglia and lab models
Alzheimer disease is characterized by accumulation of the β-amyloid peptide (Aβ) generated by β- and γ-secretase processing of the amyloid precursor protein (APP). The intake of the polyunsaturated fatty acid docosahexaenoic acid (DHA) has been associated with decreased amyloid deposition and a reduced risk in Alzheimer disease in several epidemiological trials; however, the exact underlying molecular mechanism remains to be elucidated. Here, we systematically investigate the effect of DHA on amyloidogenic and nonamyloidogenic APP processing and the potential cross-links to cholesterol metabolism in vivo and in vitro.
Key findings
- The intake of the polyunsaturated fatty acid docosahexaenoic acid (DHA) has been associated with decreased amyloid deposition and a reduced risk in Alzheimer disease in several epidemiological trials; however, the exact underlying molecular mechanism remains to be elucidated.
- Here, we systematically investigate the effect of DHA on amyloidogenic and nonamyloidogenic APP processing and the potential cross-links to cholesterol metabolism in vivo and in vitro.
- DHA reduces amyloidogenic processing by decreasing β- and γ-secretase activity, whereas the expression and protein levels of BACE1 and presenilin1 remain unchanged.
- In addition, DHA increases protein stability of α-secretase resulting in increased nonamyloidogenic processing.
Why it matters
This study found that docosahexaenoic acid reduces amyloidogenic processing of APP through multiple mechanisms in vivo and in vitro. It is laboratory and animal research and does not establish that DHA treats, cures, or prevents Alzheimer's disease in people.
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Study details
- Evidence strengthLow
How this study scored 46/100
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 219 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 12.9 citations a year over 17 year(s) since 2011 |
| Impact for its field and year | 4 / 6 | Cited 10.6× 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 32 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 3 / 4 | Last-listed author Tobias Hartmann: h-index 69 (OpenAlex, whole career) |
| Institution's track record | 0 / 3 | Hungarian Academy of Sciences: institution h-index 608 (OpenAlex) |
| Multi-centre collaboration | 2 / 3 | OpenAlex lists 5 institution(s) in 2 countries |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 21324907) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 46 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1074/jbc.m110.182329
- PubMed: 21324907
- 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).
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. The record's author list ends in “et al.”, so not every author is named. Check the citation against the original before you use it.
APA 7th
Grimm, M. O., Kuchenbecker, J., Grösgen, S., Burg, V. K., Hundsdörfer, B., Rothhaar, T. L., et al. (2011). Docosahexaenoic acid reduces amyloid beta production via multiple pleiotropic mechanisms. The Journal of biological chemistry. https://doi.org/10.1074/jbc.m110.182329
Vancouver
Grimm MO, Kuchenbecker J, Grösgen S, Burg VK, Hundsdörfer B, Rothhaar TL, et al. Docosahexaenoic acid reduces amyloid beta production via multiple pleiotropic mechanisms. The Journal of biological chemistry. 2011. doi:10.1074/jbc.m110.182329. PMID: 21324907.
BibTeX
@article{grimm2011-21324907,
author = {Grimm, M. O. and Kuchenbecker, J. and Grösgen, S. and Burg, V. K. and Hundsdörfer, B. and Rothhaar, T. L. and Friess, P. and de Wilde, M. C. and others},
title = {{Docosahexaenoic acid reduces amyloid beta production via multiple pleiotropic mechanisms}},
journal = {The Journal of biological chemistry},
year = {2011},
doi = {10.1074/jbc.m110.182329},
pmid = {21324907},
url = {https://doi.org/10.1074/jbc.m110.182329}
}
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