Neuronal Clearance of Amyloid-β by Endocytic Receptor LRP1
Open accessAbstract
Alzheimer's disease (AD) is the most prevalent form of dementia in the elderly population. Accumulation, aggregation, and deposition of amyloid-β (Aβ) peptides generated through proteolytic cleavage of amyloid precursor protein (APP) are likely initiating events in the pathogenesis of AD. While Aβ production is accelerated in familial AD, increasing evidence indicates that impaired clearance of Aβ is responsible for late-onset AD. Because Aβ is mainly generated in neurons, these cells are predicted to have the highest risk of encountering Aβ among all cell types in the brain. However, it is still unclear whether they are also involved in Aβ clearance. Here we show that receptor-mediated endocytosis in neurons by the low-density lipoprotein receptor-related protein 1 (LRP1) plays a critical role in brain Aβ clearance. LRP1 is known to be an endocytic receptor for multiple ligands including Aβ. Conditional knock-out of Lrp1 in mouse forebrain neurons leads to increased brain Aβ levels and exacerbated amyloid plaque deposition selectively in the cortex of amyloid model APP/PS1 mice without affecting Aβ production.In vivo microdialysis studies demonstrated that Aβ clearance in brain interstitial fluid is impaired in neuronal Lrp1 knock-out mice. Because the neuronal LRP1-deletion did not affect the mRNA levels of major Aβ degrading enzymes, neprilysin and insulin-degrading enzyme, the disturbed Aβ clearance is likely due to the suppression of LRP1-mediated neuronal Aβ uptake and degradation. Together, our results demonstrate that LRP1 plays an important role in receptor-mediated clearance of Aβ and indicate that neurons not only produce but also clear Aβ.
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The bulk of soluble Aβ is cleared through its direct interaction with the LDL receptor family expressed by brain capillary endothelium, neurons, and astrocytes.
“Several studies have shown that the bulk of soluble Aβ is cleared through its direct interaction with the LDL receptor family expressed by brain capillary endothelium [37], neurons [24,38], and astrocytes [39,40], therefore pharmacological disruption of the apoE/Aβ binding is unlikely to impair this process.”
From Blocking the apoE/Aβ interaction ameliorates Aβ-related pathology in APOE ε2 and ε4 targeted replacement Alzheimer model mice (2014) · cites this paper as [38]
The Discussion reports that neuronal LRP1 mediates local Aβ uptake and clearance in the cortex of APP/PS1 mice, supporting the neuron-specific part of the cited statement. It does not establish that the bulk of soluble Aβ is cleared by direct interaction with LDL-family receptors. The sentence assigns endothelial and astrocyte claims to other citations, so those are not judged here. (LLM, conf=0.84)
Experimental — accuracy not yet measuredAPOE and APOE3Ch influence both Aβ and tau pathology, either directly or through downstream effects such as neuroinflammation.
“Collectively, these recent findings underscore the influence of APOE and APOE3Ch on both Aβ and tau pathology, either directly or through downstream effects such as neuroinflammation.”
From APOE Christchurch enhances a disease-associated microglial response to plaque but suppresses response to tau pathology (2025) · cites this paper as [19]
The Introduction (page not provided) identifies apolipoprotein E as an LRP1 ligand involved in Aβ production or clearance, supporting a connection between APOE and Aβ pathology. The paper's findings concern neuronal LRP1-mediated Aβ clearance; the searched passages do not support the attributed claims about APOE3Ch, tau pathology, or neuroinflammation. (LLM, conf=0.83)
Experimental — accuracy not yet measuredAPOE binding is integral to some processes involving lipoprotein receptors, including Aβ aggregation and neuronal uptake of extracellular tau.
“Studies indicate that APOE binding is integral to some of these processes [16–20] with differences in APOE isoform-specific receptor binding affinity and lipid interactions affecting neuroinflammation, tau pathology, and amyloid plaque dynamics [21–24].”
From APOE Christchurch enhances a disease-associated microglial response to plaque but suppresses response to tau pathology (2025) · cites this paper as [19]
The Introduction (page unavailable in our copy) identifies APOE as an LRP1 ligand involved in Aβ production or clearance, and the Results report that neuronal LRP1 deletion increases cortical Aβ deposition in amyloid-model mice. These passages connect an APOE-binding receptor to amyloid processes, but do not establish that APOE binding is integral to Aβ aggregation or address neuronal uptake of extracellular tau. (LLM, conf=0.83)
Experimental — accuracy not yet measuredReceptors such as LRP1 can regulate APP endocytosis and amyloidogenic processing while also mediating cellular uptake and clearance of extracellular Aβ.
“Receptors such as LRP1 can regulate APP endocytosis and amyloidogenic processing while also mediating cellular uptake and clearance of extracellular Aβ (Kanekiyo and Bu, 2014; Kanekiyo et al., 2013; Van Gool et al., 2019).”
From Isogenic human stem cell models reveal mutation-dependent protective mechanisms of APOE3 Christchurch (2026) · cites this paper as Kanekiyo et al., 2013
The Introduction and Discussion support LRP1-mediated neuronal uptake and clearance of Aβ. The Results report that deleting neuronal LRP1 did not significantly affect APP processing in the aged APP/PS1 mice studied, and the paper does not establish that LRP1 regulates APP endocytosis. Page numbers were not available in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measured
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- Authors
- Kanekiyo, T., Cirrito, J. R., Liu, C.-C., Shinohara, M., Li, J., Schuler, D. R., Shinohara, M., 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
- 2013-12-04
- Volume
- 33
- Issue
- 49
- Pages
- 19276-19283
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC3850043
- OpenAlex
- W2084969119
- Cited by
- 280
- References
- 40
- Citations by year
- 2026: 16 · 2025: 28 · 2024: 25 · 2023: 20 · 2022: 14 · 2021: 24 · 2020: 29 · 2019: 24 · 2018: 19 · 2017: 20 · 2016: 21 · 2015: 23 · 2014: 17
- FWCI
- 14.16
- 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
- National Institutes of Health
- National Institute on Aging (P01AG030128, P50‐AG16574, R01AG027924, R37AG13956, R01AG042513, RF1AG046205, R01AG046205, R37AG013956, 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
- amyloid-beta clearance, LRP1, Alzheimer's disease, receptor-mediated endocytosis, neurons, amyloid plaques, APP/PS1 mice, brain interstitial fluid, neprilysin, insulin-degrading enzyme, amyloid precursor protein, conditional knockout mice
- MeSH terms
- Animals, Cerebral Cortex, Enzyme-Linked Immunosorbent Assay, Hippocampus, Humans, Image Processing, Computer-Assisted, Immunohistochemistry, Neurons, Receptors, LDL, RNA, Messenger, Blotting, Western, Polymerase Chain Reaction, Amyloid beta-Peptides, Mice, Knockout, Microscopy, Confocal, Transport Vesicles, Tumor Suppressor Proteins, Low Density Lipoprotein Receptor-Related Protein-1, RNA, Small Interfering, Mice
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