Autophagy in microglia degrades extracellular β-amyloid fibrils and regulates the NLRP3 inflammasome
Open accessAbstract
Accumulation of β-amyloid (Aβ) and resultant inflammation are critical pathological features of Alzheimer disease (AD). Microglia, a primary immune cell in brain, ingests and degrades extracellular Aβ fibrils via the lysosomal system. Autophagy is a catabolic process that degrades native cellular components, however, the role of autophagy in Aβ degradation by microglia and its effects on AD are unknown. Here we demonstrate a novel role for autophagy in the clearance of extracellular Aβ fibrils by microglia and in the regulation of the Aβ-induced NLRP3 (NLR family, pyrin domain containing 3) inflammasome using microglia specific atg7 knockout mice and cell cultures. We found in microglial cultures that Aβ interacts with MAP1LC3B-II via OPTN/optineurin and is degraded by an autophagic process mediated by the PRKAA1 pathway. We anticipate that enhancing microglial autophagy may be a promising new therapeutic strategy for AD.
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Enhancing Aβ uptake/efflux without simultaneously improving intracellular degradative capacity may impose an additional proteostatic burden on cells.
“However, enhancing A β uptake/efflux without simultaneously improving intracellular degradative capacity may impose an additional proteostatic burden on cells [ 28, 31 ].”
From Restores Aβ Clearance by Overcoming PCSK9–LRP1 Dysregulation and TRIB3‐Mediated Autophagy Blockade in Alzheimer's Disease (2026) · cites this paper as [28]
In “Aβ degradation in microglia by autophagic processes” (page unavailable), the paper reports that microglia with impaired autophagy retained more Aβ after exposure to fibrils. This supports the concern about intracellular accumulation when degradation is inadequate, but the paper does not test enhanced Aβ uptake or efflux without a matching increase in degradative capacity, or establish a broader proteostatic burden across cells. (LLM, conf=0.84)
Experimental — accuracy not yet measuredIn Alzheimer's disease, autophagic flux is impaired, exacerbating Aβ deposition.
“In AD, autophagic flux is impaired, exacerbating A β deposition [ 28, 29 ].”
From Restores Aβ Clearance by Overcoming PCSK9–LRP1 Dysregulation and TRIB3‐Mediated Autophagy Blockade in Alzheimer's Disease (2026) · cites this paper as [28]
In the section on disrupted microglial autophagy (page unavailable), increased SQSTM1 and OPTN in AD brain samples are said to suggest inhibited autophagic flow. The Aβ-degradation results show that disrupting autophagy leaves more Aβ inside experimental microglia, but the paper does not establish that impaired flux exacerbates Aβ deposition in people with AD. (LLM, conf=0.86)
Experimental — accuracy not yet measuredMicroglial autophagy facilitates clearance of extracellular amyloid-beta fibrils and reduces amyloid-beta-induced NLRP3 activation.
“one study showed that microglial autophagy facilitates clearance of extracellular Aβ fibrils and reduces Aβ-induced NLRP3 activation (200).”
From Microglia Function in the Central Nervous System During Health and Neurodegeneration (2017) · cites this paper as [200]
Microglial phagocytosis of Aβ deposits in Alzheimer disease models requires the autophagy-related factors BECN1, ATG7 and LC3.
“microglial phagocytosis of Aβ deposits in Alzheimer disease models [430,431] requires the autophagy-related factors BECN1, ATG7 and LC3 [432,433].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [432]
Autophagy may enhance microglial clearance of Aβ, as it does in neurons.
“autophagy may also enhance microglial clearance of Aβ”
From TREM2 Maintains Microglial Metabolic Fitness in Alzheimer’s Disease (2017) · cites this paper as Cho et al., 2014
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- Authors
- Cho, M.-H., Cho, K., Kang, H.-J., Jeon, E.-Y., Kim, H.-S., Kwon, H.-J., Kim, H.-M., Kim, D.-H., & Yoon, S.-Y.
- Affiliations
- Asan Medical Center (KR)
- University of Ulsan (KR)
- Corresponding author
- Yoon, Seung-Yong
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2014-07-22
- Volume
- 10
- Issue
- 10
- Pages
- 1761-1775
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- PMC
- PMC4198361
- OpenAlex
- W2099588975
- Cited by
- 395
- References
- 47
- Citations by year
- 2026: 26 · 2025: 28 · 2024: 38 · 2023: 45 · 2022: 51 · 2021: 41 · 2020: 49 · 2019: 34 · 2018: 19 · 2017: 30 · 2016: 20 · 2015: 13 · 2014: 1
- FWCI
- 16.12
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Autophagy (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Research Foundation
- National Research Foundation of Korea (2008-0062286)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- microglia, amyloid-beta, Alzheimer's disease, NLRP3 inflammasome, lysosomal degradation, LC3B, PRKAA1, neuroinflammation
- MeSH terms
- Autophagy-Related Protein 7, NLR Family, Pyrin Domain-Containing 3 Protein, Sequestosome-1 Protein, Aged, Aged, 80 and over, Alzheimer Disease, Animals, Autophagy, Carrier Proteins, Cell Line, Extracellular Space, Eye Proteins, Female, Heat-Shock Proteins, Humans, Inflammation, Male, Microtubule-Associated Proteins, Models, Biological, Neurons, Amyloid beta-Peptides, Microglia, Cell Cycle Proteins, Integrases, Membrane Transport Proteins, Transcription Factor TFIIIA, Adaptor Proteins, Signal Transducing, Mice, AMP-Activated Protein Kinases, Inflammasomes, Proteolysis
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