Cathepsin D is involved in the clearance of Alzheimer's β‐amyloid protein
Open accessAbstract
The cerebral deposition of 39–42 residue amyloid β‐protein (Aβ) is a histopathological characteristic of Alzheimer's disease. The present study is aimed at finding proteinases responsible for the intracellular clearance of Aβ. The Aβ‐degrading proteinase was purified from rat brain. Amino‐terminal sequence analysis indicated the Aβ‐degrading proteinase was cathepsin D. Purified cathepsin D hydrolyzed Aβ between Phe 19 and Phe 20. Cathepsin D is likely to be involved in the intracellular clearance of aggregatable Aβ, since Aβ fragments with Phe 20 at the amino‐terminus have been reported to be secreted from several lines of cultured cells.
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Other plaque-induced genes were upregulated later in CPS in donors with higher levels of pathology, including more cathepsins, LYZ, and APOE.
“Other plaque-induced genes were upregulated later in CPS in donors with higher levels of pathology (Fig. 6d, bottom, blue), including more cathepsins (CTSD and CTSS) that may facilitate Aβ clearance67, the gene encoding lysozyme (LYZ) and APOE, which is by far the most strongly associated genetic risk factor for AD68.”
From Integrated multimodal cell atlas of Alzheimer’s disease (2024) · cites this paper as [67]
The Abstract and Introduction report that cathepsin D degrades Aβ and may contribute to its clearance, supporting the CTSD part of the cited clause. The paper does not establish that CTSS facilitates Aβ clearance. The sentence's observations about gene upregulation and donor pathology are presented as the citing study's own findings, not as findings attributed to this source. (LLM, conf=0.87)
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References 15 · Cited by 92
Research works printed but not linked: 3
- Sisodia, S.S. (1992) Proc. Natl. Acad. Sci. USA 89, 6075-6079.
- Nordstedt, C., Caporaso, G.L., Thyberg, J., Gandy, S.E. and Greengard, P. (1993) J. Biol. Chem. 268, 608-612. 18733468, 1996, 2-3, Downloaded from https://febs.onlinelibrary.wiley.com/doi/10.1016/0014-5793(96)01087-3, Wiley Online Library on [06/01/2024]. See the Terms and Conditions (https://onlinelibrary.wiley.com/terms-and-conditions) on Wiley Online Library for rules of use; OA articles are governed by the applicable Creative Commons License
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- Authors
- Hamazaki, H.
- Affiliations
- Kitasato University (JP)
- Corresponding author
- Hamazaki, Hideaki
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1996-11-04
- Volume
- 396
- Issue
- 2-3
- Pages
- 139-142
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1989756817
- Cited by
- 92
- References
- 15
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 6 · 2023: 1 · 2022: 5 · 2021: 3 · 2020: 4 · 2019: 3 · 2018: 4 · 2017: 4 · 2016: 5 · 2015: 4 · 2014: 3 · 2013: 1 · 2012: 2
- FWCI
- 1.83
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- cathepsin D, amyloid-beta, Alzheimer's disease, proteolytic enzymes, proteolytic cleavage, amyloid fibril formation
- MeSH terms
- Amino Acid Sequence, Animals, Brain, Cathepsin D, Hydrogen-Ion Concentration, Molecular Sequence Data, Amyloid beta-Peptides, Rats
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