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The role of microglia in amyloid clearance from the AD brain
Open accessAbstract
Alzheimer's disease (AD), the most prominent cause of senile dementia, is clinically characterized by the extracellular deposition of beta-amyloid (Abeta) and the intracellular neurofibrillary tangles. It has been well accepted that AD pathogenesis arises from perturbation in the homeostasis of Abeta in the brain. Abeta is normally produced at high levels in the brain and cleared in an equivalent rate. Thus, even a moderate decrease in the clearance leads to the accumulation of Abeta and subsequent amyloid deposition. Microglia are the tissue macrophages in the central nervous system (CNS) and have been shown to play major roles in internalization and degradation of Abeta. Abeta exists in the brain both in soluble and in fibrillar forms. Microglia interact with these two forms of Abeta in different ways. They take up soluble forms of Abeta through macropinocytosis and LDL receptor-related proteins (LRPs) mediated pathway. Fibrillar forms of Abeta interact with the cell surface innate immune receptor complex, initiating intracellular signaling cascades that stimulate phagocytosis. Inflammatory responses influence the activation status of microglia and subsequently regulate their ability to take up and degrade Abeta. ApoE and its receptors have been shown to play critical roles in these processes. In this review, we will explore the mechanisms that microglia utilize to clear Abeta and the effectors that modulate the processes.
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“Evidence for a important role of microglial phagocytosis comes from studies that show that restricting microglial A uptake leads to increased cerebral A levels (El Khoury et al., 2007;Lee and Landreth, 2010).”
From PPARγ/RXRα-Induced and CD36-Mediated Microglial Amyloid-β Phagocytosis Results in Cognitive Improvement in Amyloid Precursor Protein/Presenilin 1 Mice (2012) · cites this paper as Lee and Landreth, 2010
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“Microglial expression of receptors that promote the clearance and phagocytosis of A, such as CD36, TLR4, and TLR6 (Lee and Landreth, 2010), are mandatory for restricting amyloid plaque formation.”
From PPARγ/RXRα-Induced and CD36-Mediated Microglial Amyloid-β Phagocytosis Results in Cognitive Improvement in Amyloid Precursor Protein/Presenilin 1 Mice (2012) · cites this paper as Lee and Landreth, 2010
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“Thus, microglia interacts with A through a recently characterized cell-surface receptor complex comprising CD36, ␣61 integrin, and CD47 (Lee and Landreth, 2010).”
From PPARγ/RXRα-Induced and CD36-Mediated Microglial Amyloid-β Phagocytosis Results in Cognitive Improvement in Amyloid Precursor Protein/Presenilin 1 Mice (2012) · cites this paper as Lee and Landreth, 2010
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“For example, they facilitate the clearance of Aβ through phagocytosis42, yet they can also exacerbate neurodegeneration by driving persistent neuroinflammation43.”
From Deletion of SPI1 in microglia exacerbates amyloid pathology by impairing microglial response in Alzheimer’s disease models (2026) · cites this paper as [42]
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“Microglia, the innate immune cells of the brain, dynamically interact with these disease processes to influence AD progression.”
From PLCG2 modulates TREM2 expression and signaling in response to Alzheimer's disease pathology (2025) · cites this paper as [5]
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“Because microglia are critical for A phagocytosis, the microglial presence at the A plaque can be interpreted as an attempt to clear this pathological deposit.”
From PPARγ/RXRα-Induced and CD36-Mediated Microglial Amyloid-β Phagocytosis Results in Cognitive Improvement in Amyloid Precursor Protein/Presenilin 1 Mice (2012) · cites this paper as Lee and Landreth, 2010
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“However, persisting neuroinflammation and sustained exposure to proinflammatory stimuli compromises microglial clearance functions as AD progresses (Lee and Landreth, 2010).”
From PPARγ/RXRα-Induced and CD36-Mediated Microglial Amyloid-β Phagocytosis Results in Cognitive Improvement in Amyloid Precursor Protein/Presenilin 1 Mice (2012) · cites this paper as Lee and Landreth, 2010
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Metadata
- Authors
- Lee, C. Y. D., & Landreth, G. E.
- Affiliations
- Case Western Reserve University (US)
- Corresponding author
- Landreth, Gary E.
- ORCID
- Landreth, Gary E.
- Venue
- Journal of Neural Transmission
- Published
- 2010-06-15
- Volume
- 117
- Issue
- 8
- Pages
- 949-960
- ISSN
- 0300-9564 (ISSN-L)
- 1435-1463
- PMC
- PMC3653296
- OpenAlex
- W2038594716
- Cited by
- 701
- References
- 161
- Citations by year
- 2026: 26 · 2025: 49 · 2024: 74 · 2023: 54 · 2022: 66 · 2021: 50 · 2020: 51 · 2019: 43 · 2018: 56 · 2017: 31 · 2016: 29 · 2015: 43 · 2014: 35 · 2013: 36 · 2012: 31
- FWCI
- 3.02
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Journal of Neural Transmission (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (R01AG020202, R01AG030482, R01AG016740)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- microglia, amyloid-beta clearance, Alzheimer's disease, amyloid deposition, macropinocytosis, LDL receptor-related protein, phagocytosis, innate immune receptors, inflammation, microglial activation, apolipoprotein E, amyloid clearance
- MeSH terms
- Alzheimer Disease, Amyloid, Apolipoproteins E, Brain, Humans, Inflammation, Microglia
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