ArticleThe Journal of biological chemistry2009
Receptor-associated protein interacts with amyloid-beta peptide and promotes its cellular uptake.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
30 citing papers in PubMed, 52 citations in OpenAlex.
- Deciphering the role of APOE in cerebral amyloid angiopathy: from genetic insights to therapeutic horizons.Annals of medicine · 2025Review
- Secreted LRPAP1 binds and triggers IFNAR1 degradation to facilitate virus evasion from cellular innate immunity.Signal transduction and targeted therapy · 2023Article
- Brain Hydrophobic Peptides Antagonists of Neurotoxic Amyloid β Peptide Monomers/Oligomers-Protein Interactions.International journal of molecular sciences · 2023Review
- LRPAP1 is released from activated microglia and inhibits microglial phagocytosis and amyloid beta aggregation.Frontiers in immunology · 2023Article
- Amentoflavone Promotes Cellular Uptake and Degradation of Amyloid-Beta in Neuronal Cells.International journal of molecular sciences · 2022Article
- Role of the Extracellular Matrix in Alzheimer's Disease.Frontiers in aging neuroscience · 2021Review
- The Impact of Apolipoprotein E Genetic Variability in Health and Life Span.The journals of gerontology. Series A, Biological sciences and medical sciences · 2020Article
- Alzheimer's amyloid-β and tau protein accumulation is associated with decreased expression of the LDL receptor-associated protein in human brain tissue.Brain and behavior · 2020Article
- Circadian rhythm and sleep-wake systems share the dynamic extracellular synaptic milieu.Neurobiology of sleep and circadian rhythms · 2018Review
- Apolipoprotein E and Alzheimer's disease: the influence of apolipoprotein E on amyloid-β and other amyloidogenic proteins.Journal of lipid research · 2017Review
- Increased amyloid β-peptide uptake in skeletal muscle is induced by hyposialylation and may account for apoptosis in GNE myopathy.Oncotarget · 2016Article
- Signaling pathways regulating neuron-glia interaction and their implications in Alzheimer's disease.Journal of neurochemistry · 2016Review
- Primate-specific miR-603 is implicated in the risk and pathogenesis of Alzheimer's disease.Aging · 2016Article
- Heparan sulfate proteoglycans mediate Aβ-induced oxidative stress and hypercontractility in cultured vascular smooth muscle cells.Molecular neurodegeneration · 2016Article
- More than cholesterol transporters: lipoprotein receptors in CNS function and neurodegeneration.Neuron · 2014Review
- The role of choroid plexus in IVIG-induced beta-amyloid clearance.Neuroscience · 2014Article
- New therapeutic approaches for Alzheimer's disease and cerebral amyloid angiopathy.Frontiers in aging neuroscience · 2014Review
- Mechanisms of U87 astrocytoma cell uptake and trafficking of monomeric versus protofibril Alzheimer's disease amyloid-β proteins.PloS one · 2014Article
- The low-density lipoprotein receptor-related protein 1 and amyloid-β clearance in Alzheimer's disease.Frontiers in aging neuroscience · 2014Review
- Prion protein-mediated toxicity of amyloid-β oligomers requires lipid rafts and the transmembrane LRP1.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Brain amyloid-beta (Abeta) peptide accumulation and aggregation are critical events in the pathogenesis of Alzheimer disease. Increasing evidence has demonstrated that LRP1 is involved in Alzheimer disease pathogenesis. The physiological ligands of LRP1, including apoE, play significant roles in the cellular clearance of Abeta. The receptor-associated protein (RAP) is a specialized chaperone for members of the low density lipoprotein receptor family. RAP shares structural and receptor-binding properties with apoE. Here, we show that RAP binds to both Abeta40 and Abeta42 in a concentration-dependent manner and forms complexes with them. Fluorescence-activated cell sorter analysis showed that RAP significantly enhances the cellular internalization of Abeta in different cell types, including brain vascular smooth muscle, neuroblastoma, glioblastoma, and Chinese hamster ovary cells. This effect of RAP was confirmed by fluorescence microscopy and enzyme-linked immunosorbent assay. RAP binds to both LRP1 and heparin; however, the ability of RAP to enhance Abeta cellular uptake was blocked by heparin and heparinase treatment but not by LRP1 deficiency. Furthermore, the effects of RAP were significantly decreased in heparan sulfate proteoglycan-deficient Chinese hamster ovary cells. Our findings reveal that RAP is a novel Abeta-binding protein that promotes cellular internalization of Abeta.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.