The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Angiotensin-Converting Enzyme Converts Amyloid β-Protein 1–42 (Aβ1–42) to Aβ1–40, and Its Inhibition Enhances Brain Aβ Deposition
Open accessAbstract
The abnormal deposition of the amyloid β-protein (Aβ) in the brain appears crucial to the pathogenesis of Alzheimer's disease (AD). Recent studies have suggested that highly amyloidogenic Aβ 1–42 is a cause of neuronal damage leading to AD pathogenesis and that monomeric Aβ 1–40 has less neurotoxicity than Aβ 1–42. We found that mouse and human brain homogenates exhibit an enzyme activity converting Aβ 1–42 to Aβ 1–40 and that the major part of this converting activity is mediated by the angiotensin-converting enzyme (ACE). Purified human ACE converts Aβ 1–42 to Aβ 1–40 as well as decreases Aβ 1–42/Aβ 1–40 ratio and degrades Aβ 1–42 and Aβ 1–40. Importantly, the treatment of Tg2576 mice with an ACE inhibitor, captopril, promotes predominant Aβ 1–42 deposition in the brain, suggesting that ACE regulates Aβ 1–42/Aβ 1–40 ratio in vivo by converting secreted Aβ 1–42 to Aβ 1–40 and degrading Aβs. The upregulation of ACE activity can be a novel therapeutic strategy for AD.
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Cites
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A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity
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“Thioflavin-S staining was performed as described previously (Wyss-Coray et al., 2001).”
Method[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
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Nonsteroidal Antiinflammatory Drugs and the Risk of Alzheimer's Disease
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“Consistent with a previous study (Kawarabayashi et al., 2001), the present study also showed that small “diffuse plaques” appear to be labeled preferentially by the anti-A 1– 42 antibody, whereas big “cored plaques” are labeled by the anti-A 1– 40 antibody (Fig.”
MethodResultAph-1, Pen-2, and Nicastrin with Presenilin Generate an Active γ-Secretase Complex
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Cited by
Amyloid cascade hypothesis: Pathogenesis and therapeutic strategies in Alzheimer's disease
Barage, S. H., & Sonawane, K. D. (2015) · Neuropeptides · doi:10.1016/j.npep.2015.06.008 · Cited by 579
Proteases and Proteolysis in Alzheimer Disease: A Multifactorial View on the Disease Process
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The Rebirth of Matrix Metalloproteinase Inhibitors: Moving Beyond the Dogma
Fields, G. B. (2019) · Cells · doi:10.3390/cells8090984 · Cited by 299
Sun, B., Zhou, Y., Halabisky, B., Lo, I., Cho, S.-H., Mueller-Steiner, S., Devidze, N., Wang, X., Grubb, A., & Gan, L. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.001 · Cited by 231
Metadata
- Authors
- Zou, K., Yamaguchi, H., Akatsu, H., Sakamoto, T., Ko, M., Mizoguchi, K., Gong, J.-S., Yu, W., Yamamoto, T., Kosaka, K., Yanagisawa, K., & Michikawa, M.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2007-08-08
- Volume
- 27
- Issue
- 32
- Pages
- 8628-8635
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- OpenAlex
- W2077595053
- Cited by
- 187
- References
- 20
- FWCI
- 5.54
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Angiotensin-Converting Enzyme Converts Amyloid β-Protein 1–42 (Aβ1–42) to Aβ1–40, and Its Inhibition Enhances Brain Aβ Deposition. https://app.cochat.ai/papers/10.1523/jneurosci.1549-07.2007
- The paper
- Zou, K., Yamaguchi, H., Akatsu, H., Sakamoto, T., Ko, M., Mizoguchi, K., Gong, J.-S., Yu, W., Yamamoto, T., Kosaka, K., Yanagisawa, K., & Michikawa, M. (2007). Angiotensin-Converting Enzyme Converts Amyloid β-Protein 1–42 (Aβ1–42) to Aβ1–40, and Its Inhibition Enhances Brain Aβ Deposition. The Journal of Neuroscience. https://doi.org/10.1523/jneurosci.1549-07.2007
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
