Home › Research › Brain tissue and pathology
Somatostatin regulates brain amyloid beta peptide Abeta42 through modulation of proteolytic degradation
Saito T, Iwata N, Tsubuki S, Takaki Y, Takano J, Huang SM, Suemoto T, Higuchi M et al.. Nature medicine, 2005-03-20
Topic: Brain proteins, microglia and lab models
Expression of somatostatin in the brain declines during aging in various mammals including apes and humans. A prominent decrease in this neuropeptide also represents a pathological characteristic of Alzheimer disease. Using in vitro and in vivo paradigms, we show that somatostatin regulates the metabolism of amyloid beta peptide (Abeta), the primary pathogenic agent of Alzheimer disease, in the brain through modulating proteolytic degradation catalyzed by neprilysin.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Saito, T., Iwata, N., Tsubuki, S., Takaki, Y., Takano, J., Huang, S. M., et al. (2005). Somatostatin regulates brain amyloid beta peptide Abeta42 through modulation of proteolytic degradation. Nature medicine. https://doi.org/10.1038/nm1206
Vancouver
Saito T, Iwata N, Tsubuki S, Takaki Y, Takano J, Huang SM, et al. Somatostatin regulates brain amyloid beta peptide Abeta42 through modulation of proteolytic degradation. Nature medicine. 2005. doi:10.1038/nm1206. PMID: 15778722.
BibTeX
@article{saito2005-15778722,
author = {Saito, T. and Iwata, N. and Tsubuki, S. and Takaki, Y. and Takano, J. and Huang, S. M. and Suemoto, T. and Higuchi, M. and others},
title = {{Somatostatin regulates brain amyloid beta peptide Abeta42 through modulation of proteolytic degradation}},
journal = {Nature medicine},
year = {2005},
doi = {10.1038/nm1206},
pmid = {15778722},
url = {https://doi.org/10.1038/nm1206}
}
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.
Key findings
- A prominent decrease in this neuropeptide also represents a pathological characteristic of Alzheimer disease.
- Using in vitro and in vivo paradigms, we show that somatostatin regulates the metabolism of amyloid beta peptide (Abeta), the primary pathogenic agent of Alzheimer disease, in the brain through modulating proteolytic degradation catalyzed by neprilysin.
- Among various effector candidates, only somatostatin upregulated neprilysin activity in primary cortical neurons.
- A genetic deficiency of somatostatin altered hippocampal neprilysin activity and localization, and increased the quantity of a hydrophobic 42-mer form of Abeta, Abeta(42), in a manner similar to presenilin gene mutations that cause familial Alzheimer disease.
Why it matters
Using in vitro and in vivo methods, this study found that somatostatin regulates the metabolism of amyloid beta peptide by modulating its degradation by neprilysin. It describes a possible mechanism and does not report any treatment, cure, or prevention for Alzheimer's disease in people.
Study details
- Evidence strengthLow
How this study scored 52/100
Published in a top-tier 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 | 10 / 10 | Tier 1 — top-tier general journal (Nature medicine) |
| Journal's citation record | 4 / 4 | Nature Medicine: journal h-index 763 (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 | 2005 — older than 20 years, still counted |
| 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 361 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 15.7 citations a year over 23 year(s) since 2005 |
| Impact for its field and year | 4 / 6 | Cited 16.8× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 3 / 6 | Cited by 13 other studies in this library |
| Still being cited | 2 / 4 | Cited 30 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 4 / 4 | Last-listed author Takaomi C. Saido: h-index 114 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | RIKEN: institution h-index 1,012 (OpenAlex) |
| Multi-centre collaboration | 1 / 3 | OpenAlex lists 2 institution(s) in 1 country |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 15778722) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 52 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
May need a subscription OpenAlex found no free copy of the full text (checked 6 Feb 1020), so the publisher may charge for it. The PubMed abstract is free.
Studies this one cites
Referenced by this study and also in the alzhub library, so you can read them here.
Later studies that cite this one
13 studies in the alzhub library list this one in their references. Showing the 8 highest-scoring.
Related studies in Brain tissue and pathology
Also tagged “tdp-43”
1,150 studies in the library carry the topic tag “tdp-43”; these are this study's neighbours in a fixed, alphabetical-by-hash tour of them, not the closest in content. All 1,150 tagged studies.