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Alzheimer's Disease β-Amyloid Peptide Is Increased in Mice Deficient in Endothelin-converting Enzyme
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“A is cleared from the brain via several clearance mechanisms, such as uptake and degradation by astro- cytes and microglia, 7,8 via A-degrading enzymes, such as neprilysin, endothelin-converting enzyme, and insulindegrading enzyme, 40 -42 and via transport by cerebral cells across the blood-brain barrier into the blood.”
From Lipoprotein Receptor-Related Protein-1 Mediates Amyloid-β-Mediated Cell Death of Cerebrovascular Cells (2007) · cites this paper as [40]
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REVIEWThe Gene Defects Responsible for Familial Alzheimer's Disease
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Turnover of Amyloid β-Protein in Mouse Brain and Acute Reduction of Its Level by Phorbol Ester
Savage, M. J., Trusko, S. P., Howland, D. S., Pinsker, L. R., Mistretta, S., Reaume, A. G., Greenberg, B. D., Siman, R., & Scott, R. W. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-05-01743.1998 · Cited by 213
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Cited by
Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development
Chen, G.-F., Xu, T.-H., Yan, Y., Zhou, Y.-R., Jiang, Y., Melcher, K., & Xu, H. E. (2017) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.28 · Cited by 1,965
Autophagy, amyloidogenesis and Alzheimer disease
Nixon, R. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.019265 · Cited by 749
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
Mechanisms of Aβ Clearance and Degradation by Glial Cells
Ries, M., & Sastre, M. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00160 · Cited by 527
“Neprilysin (NEP), the insulin degrading enzyme (IDE) and endothelin-converting enzymes-1 and -2 (ECE1 and ECE2) (Eckman et al., 2001, 2003) are metalloendopeptidases particularly involved in the degradation of monomeric Aβ species (although neprilysin can also hydrolyse oligomeric forms).”
BackgroundProteases and Proteolysis in Alzheimer Disease: A Multifactorial View on the Disease Process
De Strooper, B. (2010) · Physiological Reviews · doi:10.1152/physrev.00023.2009 · Cited by 455
Metadata
- Authors
- Eckman, E. A., Watson, M., Marlow, L., Sambamurti, K., & Eckman, C. B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-01
- Volume
- 278
- Issue
- 4
- Pages
- 2081-2084
- ISSN
- 0021-9258
- Cited by
- 218
- References
- 6
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- creativecommons.org/licenses/by/4.0/ (vor, 6497 d)
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- CoChat. (2026). Citation check: Alzheimer's Disease β-Amyloid Peptide Is Increased in Mice Deficient in Endothelin-converting Enzyme. https://app.cochat.ai/papers/10.1074/jbc.c200642200
- The paper
- Eckman, E. A., Watson, M., Marlow, L., Sambamurti, K., & Eckman, C. B. (2003). Alzheimer's Disease β-Amyloid Peptide Is Increased in Mice Deficient in Endothelin-converting Enzyme. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.c200642200
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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.
