Low-Density Lipoprotein Receptor-Related Protein 1 (LRP1) Mediates Neuronal Aβ42 Uptake and Lysosomal Trafficking
Open accessAbstract
BACKGROUND: Alzheimer's disease (AD) is characterized by the presence of early intraneuronal deposits of amyloid-beta 42 (Abeta42) that precede extracellular amyloid deposition in vulnerable brain regions. It has been hypothesized that endosomal/lysosomal dysfunction might be associated with the pathological accumulation of intracellular Abeta42 in the brain. Our previous findings suggest that the LDL receptor-related protein 1 (LRP1), a major receptor for apolipoprotein E, facilitates intraneuronal Abeta42 accumulation in mouse brain. However, direct evidence of neuronal endocytosis of Abeta42 through LRP1 is lacking. METHODOLOGY/PRINCIPAL FINDINGS: Here we show that LRP1 endocytic function is required for neuronal Abeta42 uptake. Overexpression of a functional LRP1 minireceptor, mLRP4, increases Abeta42 uptake and accumulation in neuronal lysosomes. Conversely, knockdown of LRP1 expression significantly decreases neuronal Abeta42 uptake. Disruptions of LRP1 endocytic function by either clathrin knockdown or by removal of its cytoplasmic tail decreased both uptake and accumulation of Abeta42 in neurons. Finally, we show that LRP1-mediated neuronal accumulation of Abeta42 is associated with increased cellular toxicity. CONCLUSIONS/SIGNIFICANCE: These results demonstrate that LRP1 endocytic function plays an important role in the uptake and accumulation of Abeta42 in neuronal lysosomes. These findings emphasize the central function of LRP1 in neuronal Abeta metabolism.
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Overexpression of LRP in several neuronal cell lines resulted in increased intraneuronal Aβ accumulation.
“Overexpression of low-density lipoprotein receptor-related protein (LRP) in several neuronal cell lines resulted in increased intraneuronal Ab accumulation.15,40”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [40]
The Results section (Figure 2; page unavailable) reports increased intracellular Aβ42 accumulation when an LRP1 minireceptor was overexpressed in N2a neuronal cells. It does not show overexpression producing this result in several neuronal cell lines: the other neuronal line tested, GT1-7, underwent LRP1 knockdown instead. (LLM, conf=0.87)
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 [16]
The Introduction says apoE is required for lipoprotein internalization by neuronal apoE receptors, and the Discussion supports a role for apoE in Aβ uptake. The paper does not establish that APOE binding is integral to Aβ aggregation or neuronal uptake of extracellular tau, so it supports only part of the attributed claim. (LLM, conf=0.85)
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 [16]
The Introduction links apoE to neuronal Aβ42 accumulation, and the Discussion identifies tau hyperphosphorylation as a downstream effect of intracellular Aβ (page numbers unavailable). The paper does not address APOE3Ch or neuroinflammation, so it supports only part of the attributed claim. (LLM, conf=0.87)
Experimental — accuracy not yet measuredUptake of Aβ through apolipoprotein receptors may be another Aβ clearance pathway.
“In addition, uptake of Aβ through apolipoprotein receptors may be another Aβ clearance pathway (Bu, 2009; Fuentealba et al., 2010; Kanekiyo et al., 2011).”
From miR-106b impairs cholesterol efflux and increases Aβ levels by repressing ABCA1 expression (2012) · cites this paper as Fuentealba et al., 2010
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- Authors
- Fuentealba, R. A., Liu, Q., Zhang, J., Kanekiyo, T., Hu, X., Lee, J.-M., LaDu, M. J., & Bu, G.
- Affiliations
- Washington University in St. Louis (US)
- University of Illinois Chicago (US)
- Corresponding author
- Bu, Guojun
- ORCID
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2010-07-29
- Volume
- 5
- Issue
- 7
- Pages
- e11884
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC2912373
- OpenAlex
- W2158409776
- Cited by
- 116
- References
- 65
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 8 · 2023: 4 · 2022: 5 · 2021: 4 · 2020: 5 · 2019: 3 · 2018: 7 · 2017: 7 · 2016: 4 · 2015: 9 · 2014: 14 · 2013: 9 · 2012: 10
- FWCI
- 6.93
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Digital Commons@Becker (Washington University School of Medicine) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- Funders
- Alzheimer's Association
- Hope Center for Neurological Disorders
- National Institutes of Health
- National Institute on Aging (P01AG030128, R01AG027924, R01AG019121, R01 AG19121, P01AG021184, R01AG035355)
- National Institute of Neurological Disorders and Stroke (P30NS057105)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- LRP1, LDL receptor-related protein 1, amyloid-beta 42, lysosomal trafficking, Alzheimer's disease, clathrin, cytoplasmic tail, apolipoprotein E receptor, neurotoxicity, amyloid-beta metabolism
- MeSH terms
- Animals, Biological Transport, Cell Survival, Clathrin, Endocytosis, Flow Cytometry, Kinetics, Lysosomes, Neurons, Peptide Fragments, Receptors, LDL, Immunoblotting, Amyloid beta-Peptides, Microscopy, Confocal, Tumor Suppressor Proteins, Low Density Lipoprotein Receptor-Related Protein-1, Cell Line, Tumor, Mice
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