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Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease
Cataldo AM, Paskevich PA, Kominami E, Nixon RA.. Proceedings of the National Academy of Sciences of the United States of America, 1991-12-01
Topic: Amyloid, tau and blood-test diagnosis
beta-Amyloid formation requires multiple abnormal proteolytic cleavages of amyloid precursor protein (APP), including one within its intramembrane domain. Lysosomes, which contain a wide variety of proteases (cathepsins) and other acid hydrolases, are major sites for the turnover of membrane proteins and other cell constituents. Using immunocytochemistry, immunoelectron microscopy, and enzyme histochemistry, we studied the expression and cellular distributions of 10 lysosomal hydrolases, including 4 cathepsins, in neocortex from patients with Alzheimer disease and control (non-Alzheimer-disease) individuals.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Cataldo, A. M., Paskevich, P. A., Kominami, E., & Nixon, R. A. (1991). Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease. Proceedings of the National Academy of Sciences of the United States of America. https://doi.org/10.1073/pnas.88.24.10998
Vancouver
Cataldo AM, Paskevich PA, Kominami E, Nixon RA. Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease. Proceedings of the National Academy of Sciences of the United States of America. 1991. doi:10.1073/pnas.88.24.10998. PMID: 1837142.
BibTeX
@article{cataldo1991-1837142,
author = {Cataldo, A. M. and Paskevich, P. A. and Kominami, E. and Nixon, R. A.},
title = {{Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease}},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
year = {1991},
doi = {10.1073/pnas.88.24.10998},
pmid = {1837142},
url = {https://doi.org/10.1073/pnas.88.24.10998}
}
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Key findings
- Lysosomes, which contain a wide variety of proteases (cathepsins) and other acid hydrolases, are major sites for the turnover of membrane proteins and other cell constituents.
- Using immunocytochemistry, immunoelectron microscopy, and enzyme histochemistry, we studied the expression and cellular distributions of 10 lysosomal hydrolases, including 4 cathepsins, in neocortex from patients with Alzheimer disease and control (non-Alzheimer-disease) individuals.
- In control brains, acid hydrolases were localized exclusively to intracellular lysosome-related compartments, and 8 of the 10 enzymes predominated in neurons.
- In Alzheimer disease brains, strongly immunoreactive lysosomes and lipofuscin granules accumulated markedly in the perikarya and proximal dendrites of many cortical neurons, some of which were undergoing degeneration.
Why it matters
In brain tissue from people with Alzheimer's disease, lysosomal hydrolases were abnormally distributed compared with controls. This describes a difference in tissue and does not show that changing lysosomal function treats or prevents the disease.
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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 (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 | 1991 — 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 | 5 / 7 | Cited 267 times (OpenAlex, 2026-10-10) |
| Citations per year | 2 / 5 | 7.2 citations a year over 37 year(s) since 1991 |
| Impact for its field and year | 3 / 6 | Cited 6.6× 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 | 1 / 4 | Cited 14 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 | Juntendo University: institution h-index 530 (OpenAlex) |
| Multi-centre collaboration | 1 / 3 | OpenAlex lists 2 institution(s) in 2 countries |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 1837142) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 43 / 100 | — |
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