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Amyloid-Beta Protein Clearance and Degradation (ABCD) Pathways and their Role in Alzheimer’s Disease
Open accessAbstract
Amyloid-β proteins (Aβ) of 42 (Aβ42) and 40 aa (Aβ40) accumulate as senile plaques (SP) and cerebrovascular amyloid protein deposits that are defining diagnostic features of Alzheimer's disease (AD). A number of rare mutations linked to familial AD (FAD) on the Aβ precursor protein (APP), Presenilin-1 (PS1), Presenilin- 2 (PS2), Adamalysin10, and other genetic risk factors for sporadic AD such as the ε4 allele of Apolipoprotein E (ApoE-ε4) foster the accumulation of Aβ and also induce the entire spectrum of pathology associated with the disease. Aβ accumulation is therefore a key pathological event and a prime target for the prevention and treatment of AD. APP is sequentially processed by β-site APP cleaving enzyme (BACE1) and γ-secretase, a multisubunit PS1/PS2-containing integral membrane protease, to generate Aβ. Although Aβ accumulates in all forms of AD, the only pathways known to be affected in FAD increase Aβ production by APP gene duplication or via base substitutions on APP and γ-secretase subunits PS1 and PS2 that either specifically increase the yield of the longer Aβ42 or both Aβ40 and Aβ42. However, the vast majority of AD patients accumulate Aβ without these known mutations. This led to proposals that impairment of Aβ degradation or clearance may play a key role in AD pathogenesis. Several candidate enzymes, including Insulin-degrading enzyme (IDE), Neprilysin (NEP), Endothelin-converting enzyme (ECE), Angiotensin converting enzyme (ACE), Plasmin, and Matrix metalloproteinases (MMPs) have been identified and some have even been successfully evaluated in animal models. Several studies also have demonstrated the capacity of γ-secretase inhibitors to paradoxically increase the yield of Aβ and we have recently established that the mechanism is by skirting Aβ degradation. This review outlines major cellular pathways of Aβ degradation to provide a basis for future efforts to fully characterize the panel of pathways responsible for Aβ turnover.
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“cerebrospinal fluid (CSF) levels of the angiotensin-converting enzyme (ACE) are associated with Aβ levels81 and LOAD risk82, and studies show ACE can inhibit Aβ toxicity and aggregation83.”
From Genetic meta-analysis of diagnosed Alzheimer’s disease identifies new risk loci and implicates Aβ, tau, immunity and lipid processing (2019) · cites this paper as [83]
In the citing paper
“In the hippocampus of AD patients, the enzymes IDE, ACE and NEP had decreased activity.30”
From Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future (2023) · cites this paper as [30]
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Metadata
- Authors
- Baranello, R., Bharani, K., Padmaraju, V., Chopra, N., Lahiri, D., Greig, N., Pappolla, M., & Sambamurti, K.
- Affiliations
- Medical University of South Carolina (US)
- Indiana University – Purdue University Indianapolis (US)
- Indiana University Bloomington (US)
- National Institutes of Health (US)
- The University of Texas Medical Branch at Galveston (US)
- ORCID
- Venue
- Current Alzheimer Research
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2015-01-03
- Volume
- 12
- Issue
- 1
- Pages
- 32-46
- ISSN
- 1567-2050 (ISSN-L)
- PMC
- PMC4820400
- OpenAlex
- W2136334732
- Cited by
- 331
- References
- 201
- Citations by year
- 2026: 9 · 2025: 26 · 2024: 14 · 2023: 30 · 2022: 34 · 2021: 44 · 2020: 45 · 2019: 45 · 2018: 31 · 2017: 22 · 2016: 20 · 2015: 10
- FWCI
- 20.39
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Current Alzheimer Research (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- IUScholarWorks (Indiana University) (submittedVersion)
- Purdue University Indianapolis (Indiana University) (submittedVersion)
- Funders
- National Institutes of Health (5r21ag042804-02)
- National Institute on Aging (R21-AG042804, AG046200, R01AG022103, R21AG046200, AG042804)
- National Institute of General Medical Sciences (T32 GM08716-13, T32GM008716)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta, Alzheimer's disease, amyloid-beta clearance, amyloid beta degradation, amyloid plaques, familial Alzheimer's disease, APP mutations, presenilin, gamma-secretase, BACE1, insulin-degrading enzyme, neprilysin, matrix metalloproteinases, APOE ε4, gamma-secretase inhibitors
- MeSH terms
- Alzheimer Disease, Animals, Apolipoproteins E, Humans, Models, Biological, Mutation, Signal Transduction, Amyloid beta-Peptides, Presenilin-1, Presenilin-2, Amyloid Precursor Protein Secretases, Plaque, Amyloid
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