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Cathepsin B degrades amyloid-β in mice expressing wild-type human amyloid precursor protein
Wang C, Sun B, Zhou Y, Grubb A, Gan L.. The Journal of biological chemistry, 2012-09-28
Topic: Brain proteins, microglia and lab models
Accumulation of amyloid-β (Aβ), believed to be a key trigger of Alzheimer disease (AD), could result from impaired clearance mechanisms. Previously, we showed that the cysteine protease cathepsin B (CatB) degrades Aβ, most likely by C-terminal truncation, in mice expressing human amyloid precursor protein with familial AD-linked mutations (hAPP(FAD)). In addition, the Aβ-degrading activity of CatB is inhibited by its endogenous inhibitor, cystatin C (CysC).
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Wang, C., Sun, B., Zhou, Y., Grubb, A., & Gan, L. (2012). Cathepsin B degrades amyloid-β in mice expressing wild-type human amyloid precursor protein. The Journal of biological chemistry. https://doi.org/10.1074/jbc.m112.371641
Vancouver
Wang C, Sun B, Zhou Y, Grubb A, Gan L. Cathepsin B degrades amyloid-β in mice expressing wild-type human amyloid precursor protein. The Journal of biological chemistry. 2012. doi:10.1074/jbc.m112.371641. PMID: 23024364.
BibTeX
@article{wang2012-23024364,
author = {Wang, C. and Sun, B. and Zhou, Y. and Grubb, A. and Gan, L.},
title = {{Cathepsin B degrades amyloid-β in mice expressing wild-type human amyloid precursor protein}},
journal = {The Journal of biological chemistry},
year = {2012},
doi = {10.1074/jbc.m112.371641},
pmid = {23024364},
url = {https://doi.org/10.1074/jbc.m112.371641}
}
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.
Key findings
- Previously, we showed that the cysteine protease cathepsin B (CatB) degrades Aβ, most likely by C-terminal truncation, in mice expressing human amyloid precursor protein with familial AD-linked mutations (hAPP(FAD)).
- In addition, the Aβ-degrading activity of CatB is inhibited by its endogenous inhibitor, cystatin C (CysC).
- Reducing CysC expression markedly lowers Aβ levels by enhancing CatB-mediated Aβ degradation in hAPP(FAD) mice.
- However, because a vast majority of AD patients do not carry familial mutations, we investigated how the CysC-CatB axis affects Aβ levels in mice expressing wild-type hAPP (hAPP(WT)).
Why it matters
The cysteine protease cathepsin B was shown to degrade amyloid-beta in mice expressing human amyloid precursor protein, and reducing cystatin C expression lowered amyloid-beta levels by enhancing this degradation. This is mouse research, and the authors note that most Alzheimer patients do not carry the mutations studied, so it does not establish a treatment for people.
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Study details
- Evidence strengthLow
How this study scored 45/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported 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 | 2012 — 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 | Laboratory or animal study (title names “mice”) — scores zero |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 5 / 7 | Cited 107 times (OpenAlex, 2026-10-10) |
| Citations per year | 2 / 5 | 6.7 citations a year over 16 year(s) since 2012 |
| Impact for its field and year | 3 / 6 | Cited 4.5× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 1 / 6 | Cited by 2 other studies in this library |
| Still being cited | 2 / 4 | Cited 17 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 3 / 4 | Last-listed author Li Gan: h-index 71 (OpenAlex, whole career) |
| Institution's track record | 2 / 3 | University of California, San Francisco: institution h-index 1,915 (OpenAlex) |
| Multi-centre collaboration | 2 / 3 | OpenAlex lists 4 institution(s) in 2 countries |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 23024364) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 45 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1074/jbc.m112.371641
- PubMed: 23024364
- 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).
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