Home › Research › Risk genes beyond APOE
Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain
Cataldo AM, Nixon RA.. Proceedings of the National Academy of Sciences of the United States of America, 1990-05-01
Topic: Amyloid, tau and blood-test diagnosis
The formation of beta-amyloid in the brains of individuals with Alzheimer disease requires the proteolytic cleavage of a membrane-associated precursor protein. The proteases that may be involved in this process have not yet been identified. Cathepsins are normally intracellular proteolytic enzymes associated with lysosomes; however, when sections from Alzheimer brains were stained by antisera to cathepsin D and cathepsin B, high levels of immunoreactivity were also detected in senile plaques.
Key findings
- The proteases that may be involved in this process have not yet been identified.
- Cathepsins are normally intracellular proteolytic enzymes associated with lysosomes; however, when sections from Alzheimer brains were stained by antisera to cathepsin D and cathepsin B, high levels of immunoreactivity were also detected in senile plaques.
- Extracellular sites of cathepsin immunoreactivity were not seen in control brains from age-matched individuals without neurologic disease or from patients with Huntington disease or Parkinson disease.
- In situ enzyme histochemistry of cathepsin D and cathepsin B on sections of neocortex using synthetic peptides and protein substrates showed that senile plaques contained the highest levels of enzymatically active cathepsin.
Why it matters
This study found that cathepsins D and B, normally lysosomal proteases, were highly immunoreactive in senile plaques in Alzheimer brains but not in control brains. It suggests a possible role for these proteases in beta-amyloid formation but does not provide a treatment, cure, or prevention.
New to this subject? Start with our plain-English guide: Genetics →
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 (Proceedings of the National Academy of Sciences of the United States of America) |
| Journal's citation record | 4 / 4 | Proceedings of the National Academy of Sciences: journal h-index 1,167 (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 | 1990 — 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 440 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 11.6 citations a year over 38 year(s) since 1990 |
| Impact for its field and year | 4 / 6 | Cited 15.1× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 3 / 6 | Cited by 12 other studies in this library |
| Still being cited | 2 / 4 | Cited 27 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 4 / 4 | Last-listed author Ralph A. Nixon: h-index 115 (OpenAlex, whole career) |
| Institution's track record | 0 / 3 | McLean Hospital: institution h-index 470 (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 1692625) |
| 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
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. Check the citation against the original before you use it.
APA 7th
Cataldo, A. M., & Nixon, R. A. (1990). Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain. Proceedings of the National Academy of Sciences of the United States of America. https://doi.org/10.1073/pnas.87.10.3861
Vancouver
Cataldo AM, Nixon RA. Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain. Proceedings of the National Academy of Sciences of the United States of America. 1990. doi:10.1073/pnas.87.10.3861. PMID: 1692625.
BibTeX
@article{cataldo1990-1692625,
author = {Cataldo, A. M. and Nixon, R. A.},
title = {{Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain}},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
year = {1990},
doi = {10.1073/pnas.87.10.3861},
pmid = {1692625},
url = {https://doi.org/10.1073/pnas.87.10.3861}
}
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
12 studies in the alzhub library list this one in their references. Showing the 8 highest-scoring.