Heparan Sulphate Proteoglycan and the Low-Density Lipoprotein Receptor-Related Protein 1 Constitute Major Pathways for Neuronal Amyloid-β Uptake
Open accessAbstract
Alzheimer's disease (AD) is a progressive and irreversible neurodegenerative disorder in which the aggregation and deposition of amyloid-β (Aβ) peptides in the brain are central to its pathogenesis. In healthy brains, Aβ is effectively metabolized with little accumulation. Cellular uptake and subsequent degradation of Aβ is one of the major pathways for its clearance in the brain. Increasing evidence has demonstrated significant roles for the low-density lipoprotein receptor-related protein 1 (LRP1) in the metabolism of Aβ in neurons, glia cells, and along the brain vasculatures. Heparan sulfate proteoglycan (HSPG) has also been implicated in several pathogenic features of AD, including its colocalization with amyloid plaques. Here, we demonstrate that HSPG and LRP1 cooperatively mediate cellular Aβ uptake. Fluorescence-activated cell sorter and confocal microscopy revealed that knockdown of LRP1 suppresses Aβ uptake, whereas overexpression of LRP1 enhances this process in neuronal cells. Heparin, which antagonizes HSPG, significantly inhibited cellular Aβ uptake. Importantly, treatment with heparin or heparinase blocked LRP1-mediated cellular uptake of Aβ. We further showed that HSPG is more important for the binding of Aβ to the cell surface than LRP1. The critical roles of HSPG in cellular Aβ binding and uptake were confirmed in Chinese hamster ovary cells genetically deficient in HSPG. We also showed that heparin and a neutralizing antibody to LRP1 suppressed Aβ uptake in primary neurons. Our findings demonstrate that LRP1 and HSPG function in a cooperative manner to mediate cellular Aβ uptake and define a major pathway through which Aβ gains entry to neuronal cells.
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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 [17]
The Introduction identifies APOE as an LRP1 ligand, and the Discussion describes LRP1 and HSPG roles in neuronal Aβ uptake. But the paper does not establish that APOE binding is integral to Aβ aggregation, and it does not address neuronal uptake of extracellular tau. Page numbers are unavailable in our copy. (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 [17]
The Introduction (page unavailable) identifies apoE as an LRP1 ligand involved in Aβ production and clearance, providing limited support for the APOE–Aβ part of the claim. The paper does not address APOE3Ch or show that APOE affects tau pathology or acts through neuroinflammation; its findings concern HSPG- and LRP1-mediated neuronal Aβ uptake. (LLM, conf=0.84)
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 Kanekiyo et al., 2011
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“Furthermore, the remnants of these aggregates after cell death may induce extracellular amyloid plaque formation through its seeding effect (Hu et al., 2009).”
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- Authors
- Kanekiyo, T., Zhang, J., Liu, Q., Liu, C.-C., Zhang, L., & Bu, G.
- Affiliations
- Washington University in St. Louis (US)
- Mayo Clinic (US)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2011-02-02
- Volume
- 31
- Issue
- 5
- Pages
- 1644-1651
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC3272839
- OpenAlex
- W2009401461
- Cited by
- 212
- References
- 3
- Citations by year
- 2026: 3 · 2025: 10 · 2024: 19 · 2023: 12 · 2022: 19 · 2021: 21 · 2020: 26 · 2019: 6 · 2018: 10 · 2017: 16 · 2016: 12 · 2015: 8 · 2014: 21 · 2013: 12 · 2012: 15
- FWCI
- 10.91
- 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
- Alzheimer's Association
- American Health Assistance Foundation
- American Heart Association
- Hope Center for Neurological Disorders
- National Institutes of Health
- National Institute on Aging (P01AG030128, R01AG027924, R01AG031784)
- 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 › Proteoglycans and glycosaminoglycans research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta uptake, heparan sulfate proteoglycans, LRP1, Alzheimer's disease, amyloid-beta clearance, heparin, heparinase, neurons, amyloid-beta binding
- MeSH terms
- Animals, Biological Transport, Cell Line, Cells, Cultured, Cricetulus, Embryo, Mammalian, Endocytosis, Enzyme-Linked Immunosorbent Assay, Female, Fibroblasts, Flow Cytometry, Cricetinae, Heparin, Hypothalamus, Neurons, Peptide Fragments, Pregnancy, Receptors, LDL, Transfection, Blotting, Western, Up-Regulation, Amyloid beta-Peptides, CHO Cells, Microscopy, Confocal, Heparan Sulfate Proteoglycans, Tumor Suppressor Proteins, Low Density Lipoprotein Receptor-Related Protein-1, RNA, Small Interfering, Mice, Gene Knockdown Techniques
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