The low-density lipoprotein receptor-related protein 1 and amyloid-β clearance in Alzheimer’s disease
Open accessAbstract
Accumulation and aggregation of amyloid-β (Aβ) peptides in the brain trigger the development of progressive neurodegeneration and dementia associated with Alzheimer's disease (AD). Perturbation in Aβ clearance, rather than Aβ production, is likely the cause of sporadic, late-onset AD, which accounts for the majority of AD cases. Since cellular uptake and subsequent degradation constitute a major Aβ clearance pathway, the receptor-mediated endocytosis of Aβ has been intensely investigated. Among Aβ receptors, the low-density lipoprotein receptor-related protein 1 (LRP1) is one of the most studied receptors. LRP1 is a large endocytic receptor for more than 40 ligands, including apolipoprotein E, α2-macroglobulin and Aβ. Emerging in vitro and in vivo evidence demonstrates that LRP1 is critically involved in brain Aβ clearance. LRP1 is highly expressed in a variety of cell types in the brain including neurons, vascular cells and glial cells, where LRP1 functions to maintain brain homeostasis and control Aβ metabolism. LRP1-mediated endocytosis regulates cellular Aβ uptake by binding to Aβ either directly or indirectly through its co-receptors or ligands. Furthermore, LRP1 regulates several signaling pathways, which also likely influences Aβ endocytic pathways. In this review, we discuss how LRP1 regulates the brain Aβ clearance and how this unique endocytic receptor participates in AD pathogenesis. Understanding of the mechanisms underlying LRP1-mediated Aβ clearance should enable the rational design of novel diagnostic and therapeutic strategies for AD.
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APOE 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 [18]
The Summary and Perspective (page not provided) identifies apoE as an LRP1 ligand that affects Aβ aggregation and cellular uptake. The section on the relationship among LRP1, apoE, and Aβ also discusses apoE binding and receptor-dependent Aβ uptake. The passages found do not address neuronal uptake of extracellular tau. (LLM, conf=0.87)
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 [18]
The section “Relationship among LRP1, apoE, and Aβ in AD” links apoE isoforms to Aβ aggregation and uptake, supporting that part of the claim. Our copy does not address APOE3Ch or an effect of APOE on tau pathology; its discussion of inflammation concerns LRP1, not an APOE-to-tau pathway. Page numbers are unavailable in our copy. (LLM, conf=0.89)
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 and Bu, 2014
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“While decreased apoE levels reduce Aβ deposition (Kim et al., 2011; Bien-Ly et al., 2012), the pharmacological approaches to increase lipidated apoE by liver X receptor (LXR) and retinoid X receptor (RXR) agonists facilitate Aβ clearance and restore cognitive function in amyloid model mice (Riddell…”
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The low density lipoprotein receptor
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Liver X receptor activation restores memory in aged AD mice without reducing amyloid
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Sorting nexin 17 facilitates LRP recycling in the early endosome
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Self-citationNeurovascular Defects and Faulty Amyloid-β Vascular Clearance in Alzheimer's Disease
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γ-Secretase Limits the Inflammatory Response Through the Processing of LRP1
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LRP1 mediates bidirectional transcytosis of amyloid-β across the blood-brain barrier
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Ligand binding to LRP1 transactivates Trk receptors by a Src family kinase-dependent pathway.
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Self-citationSoluble Low Density Lipoprotein Receptor-related Protein (LRP) Circulates in Human Plasma
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“Since the APOE 4 allele increases the risk for late-onset Alzheimer’s disease (AD) compared with the APOE 2 and 3 alleles (Corder et al., 1993; Farrer et al., 1997), LDLR family has been vigorously studied as a target to explore the complex pathogenesis of AD.”
BackgroundLRP1 shedding in human brain: roles of ADAM10 and ADAM17
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Self-citationβ‐Amyloid is transmitted via neuronal connections along axonal membranes
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LRP1 is critical for the surface distribution and internalization of the NR2B NMDA receptor subtype
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Uptake of Aβ 1–40‐ and Aβ 1–42‐coated yeast by microglial cells: a role for LRP
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A systemic view of Alzheimer disease — insights from amyloid-β metabolism beyond the brain
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Self-citationRole of Blood-Brain Barrier in Alzheimer’s Disease
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A Consensus Definitive Classification of Scavenger Receptors and Their Roles in Health and Disease
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β-Amyloid: the key peptide in the pathogenesis of Alzheimer’s disease
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ApoE Cascade Hypothesis in the pathogenesis of Alzheimer’s disease and related dementias
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Self-citationMicroglia in Alzheimer’s disease: pathogenesis, mechanisms, and therapeutic potentials
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Astrocytic LRP1 Mediates Brain Aβ Clearance and Impacts Amyloid Deposition
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The role of ABCA7 in Alzheimer’s disease: evidence from genomics, transcriptomics and methylomics
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- Authors
- Kanekiyo, T., & Bu, G.
- Affiliations
- Mayo Clinic (US)
- Corresponding author
- Kanekiyo, Takahisa
- Venue
- Frontiers in Aging Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2014-05-20
- Volume
- 6
- Pages
- 93-93
- ISSN
- 1663-4365 (ISSN-L)
- PMC
- PMC4033011
- OpenAlex
- W2003708432
- Cited by
- 281
- References
- 156
- Citations by year
- 2026: 23 · 2025: 28 · 2024: 25 · 2023: 34 · 2022: 25 · 2021: 27 · 2020: 18 · 2019: 20 · 2018: 17 · 2017: 23 · 2016: 20 · 2015: 17 · 2014: 3
- FWCI
- 2.46
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Frontiers in Aging Neuroscience (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- 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
- National Institutes of Health
- National Institute on Aging (P01AG030128, R01AG027924, RF1AG046205, R01AG046205, R01AG035355)
- National Institute of Neurological Disorders and Stroke (P01NS074969)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- LRP1, amyloid-beta clearance, Alzheimer's disease, receptor-mediated endocytosis, co-receptors, apolipoprotein E, alpha2-macroglobulin, amyloid-beta aggregation, neurodegeneration, glial cells, vascular cells, signaling pathways
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