Astrocytic LRP1 Mediates Brain Aβ Clearance and Impacts Amyloid Deposition
Open accessAbstract
Accumulation and deposition of amyloid-β (Aβ) in the brain represent an early and perhaps necessary step in the pathogenesis of Alzheimer's disease (AD). Aβ accumulation leads to the formation of Aβ aggregates, which may directly and indirectly lead to eventual neurodegeneration. While Aβ production is accelerated in many familial forms of early-onset AD, increasing evidence indicates that impaired clearance of Aβ is more evident in late-onset AD. To uncover the mechanisms underlying impaired Aβ clearance in AD, we examined the role of low-density lipoprotein receptor-related protein 1 (LRP1) in astrocytes. Although LRP1 has been shown to play critical roles in brain Aβ metabolism in neurons and vascular mural cells, its role in astrocytes, the most abundant cell type in the brain responsible for maintaining neuronal homeostasis, remains unclear. Here, we show that astrocytic LRP1 plays a critical role in brain Aβ clearance. LRP1 knockdown in primary astrocytes resulted in decreased cellular Aβ uptake and degradation. In addition, silencing of LRP1 in astrocytes led to downregulation of several major Aβ-degrading enzymes, including matrix metalloproteases MMP2, MMP9, and insulin-degrading enzyme. More important, conditional knock-out of the Lrp1 gene in astrocytes in the background of APP/PS1 mice impaired brain Aβ clearance, exacerbated Aβ accumulation, and accelerated amyloid plaque deposition without affecting its production. Together, our results demonstrate that astrocytic LRP1 plays an important role in Aβ metabolism and that restoring LRP1 expression and function in the brain could be an effective strategy to facilitate Aβ clearance and counter amyloid pathology in AD. SIGNIFICANCE STATEMENT Astrocytes represent a major cell type regulating brain homeostasis; however, their roles in brain clearance of amyloid-β (Aβ) and underlying mechanism are not clear. In this study, we used both cellular models and conditional knock-out mouse models to address the role of a critical Aβ receptor, the low-density lipoprotein receptor-related protein 1 (LRP1) in astrocytes. We found that LRP1 in astrocytes plays a critical role in brain Aβ clearance by modulating several Aβ-degrading enzymes and cellular degradation pathways. Our results establish a critical role of astrocytic LRP1 in brain Aβ clearance and shed light on specific Aβ clearance pathways that may help to establish new targets for AD prevention and therapy.
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Receptors that bind to apoE influence amyloid pathology.
“Furthermore, receptors that bind to apoE have been shown to influence amyloid pathology. 21 , 41”
From Deletion of miR-33, a regulator of the ABCA1–APOE pathway, ameliorates neuropathological phenotypes in APP/PS1 mice (2024) · cites this paper as [41]
Apoe-deficient astrocytes upregulate genes associated with inhibition of Aβ fibrillization (Ptgds and Cst3) and regulation of protein degradation (Ubb, Ubc and Ctsl).
“Interestingly, Apoe-deficient astrocytes upregulate genes associated with inhibition of Aβ fibrillization (Ptgds and Cst3) and regulation of protein degradation (Ubb, Ubc and Ctsl) (Apelt et al, 2003; Davis et al, 2021; Liu et al, 2017a; Wegiel et al, 2000).”
From APOE from astrocytes restores Alzheimer’s Aβ-pathology and DAM-like responses in APOE deficient microglia (2024) · cites this paper as Liu et al, 2017a
The Discussion (page unavailable) mentions improved Aβ clearance with apoE deficiency, but does not report gene expression in Apoe-deficient astrocytes. Searches for Ptgds, Cst3, Ubb, Ubc and Ctsl, and for astrocyte gene-expression changes, found no passage supporting the claimed upregulation. (LLM, conf=0.75)
Experimental — accuracy not yet measuredAD is accompanied by activation of microglia and astrocytes that affects clearance and production of Aβ, development and propagation of tau pathology, exacerbates neurodegeneration, and influences disease progression and severity.
“AD is accompanied by activation of microglia and astrocytes1,2 that affects the clearance and production of Aβ42,3,4 development and propagation of tau pathology,5 exacerbates neurodegeneration, and influences disease progression and severity.6,7”
From CSF biomarkers of neuroinflammation and cerebrovascular dysfunction in early Alzheimer disease (2018) · cites this paper as [4]
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- Authors
- Liu, C.-C., Hu, J., Zhao, N., Wang, J., Wang, N., Cirrito, J. R., Kanekiyo, T., Holtzman, D. M., & Bu, G.
- Affiliations
- Mayo Clinic (US)
- Washington University in St. Louis (US)
- ORCID
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2017-03-08
- Volume
- 37
- Issue
- 15
- Pages
- 4023-4031
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC5391682
- OpenAlex
- W2593036876
- Cited by
- 267
- References
- 75
- Citations by year
- 2026: 23 · 2025: 39 · 2024: 27 · 2023: 32 · 2022: 29 · 2021: 32 · 2020: 36 · 2019: 26 · 2018: 13 · 2017: 10
- FWCI
- 17.39
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Digital Commons@Becker (Washington University School of Medicine) (submittedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- Funders
- American Heart Association (15SDG22460003)
- National Institutes of Health
- National Institute on Aging (RF1AG051504, R01AG027924, RF1AG046205, R01AG046205, R01AG035355, P50AG016574)
- National Institute of Neurological Disorders and Stroke (P01NS074969)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Cerebrospinal fluid and hydrocephalus
- Keywords
- LRP1, astrocytes, amyloid-beta clearance, Alzheimer's disease, amyloid deposition, amyloid plaques, matrix metalloproteinases, insulin-degrading enzyme, APP/PS1 mice, conditional knockout
- MeSH terms
- Animals, Astrocytes, Brain, Cells, Cultured, Female, Humans, Male, Peptide Fragments, Receptors, LDL, Amyloid beta-Peptides, Mice, Knockout, Tumor Suppressor Proteins, Low Density Lipoprotein Receptor-Related Protein-1, Mice, Plaque, Amyloid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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