ArticleThe Journal of biological chemistry2011
Amyloid-β-induced synapse damage is mediated via cross-linkage of cellular prion proteins.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 85 citations in OpenAlex.
- Unveiling the Interplay: Neurovascular Coupling, Astrocytes and G Protein-Coupled Receptors in Alzheimer's Disease.ACS pharmacology & translational science · 2025Review
- Molecular Factors Mediating Neural Cell Plasticity Changes in Dementia Brain Diseases.Neural plasticity · 2021Review
- Review
- Binding between Prion Protein and Aβ Oligomers Contributes to the Pathogenesis of Alzheimer's Disease.Virologica Sinica · 2019Review
- In vivo induction of membrane damage by β-amyloid peptide oligomers.Acta neuropathologica communications · 2018Article
- Prion protein stabilizes amyloid-β (Aβ) oligomers and enhances Aβ neurotoxicity in aThe Journal of biological chemistry · 2018Article
- Synaptotoxic Signaling by Amyloid Beta Oligomers in Alzheimer's Disease Through Prion Protein and mGluR5.Advances in pharmacology (San Diego, Calif.) · 2018Review
- Soluble Aβ aggregates can inhibit prion propagation.Open biology · 2017Article
- Mediation of insulin growth factor-1 in Alzheimer's disease and the mechanism of PRNP genetic expression and the PI3K/Akt signaling pathway.Experimental and therapeutic medicine · 2017Article
- Binding Sites for Amyloid-β Oligomers and Synaptic Toxicity.Cold Spring Harbor perspectives in medicine · 2017Review
- The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules.Frontiers in molecular neuroscience · 2017Article
- Breaking the Cycle, Cholesterol Cycling, and Synapse Damage in Response to Amyloid-β.Journal of experimental neuroscience · 2017Article
- The expression of insulin-like growth factor-1 in senior patients with diabetes and dementia.Experimental and therapeutic medicine · 2017Article
- Regulation of Amyloid β Oligomer Binding to Neurons and Neurotoxicity by the Prion Protein-mGluR5 Complex.The Journal of biological chemistry · 2016Article
- Actin dynamics and cofilin-actin rods in alzheimer disease.Cytoskeleton (Hoboken, N.J.) · 2016Review
- The Essential Role of Soluble Aβ Oligomers in Alzheimer's Disease.Molecular neurobiology · 2016Review
- Metabotropic glutamate receptor 5 couples cellular prion protein to intracellular signalling in Alzheimer's disease.Brain : a journal of neurology · 2016Article
- Sialic Acid on the Glycosylphosphatidylinositol Anchor Regulates PrP-mediated Cell Signaling and Prion Formation.The Journal of biological chemistry · 2016Article
- Prion-Protein-interacting Amyloid-β Oligomers of High Molecular Weight Are Tightly Correlated with Memory Impairment in Multiple Alzheimer Mouse Models.The Journal of biological chemistry · 2015Article
- Monoacylated Cellular Prion Proteins Reduce Amyloid-β-Induced Activation of Cytoplasmic Phospholipase A2 and Synapse Damage.Biology · 2015Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cellular prion protein (PrP(C)), which is highly expressed at synapses, was identified as a receptor for the amyloid-β (Aβ) oligomers that are associated with dementia in Alzheimer disease. Here, we report that Aβ oligomers secreted by 7PA2 cells caused synapse damage in cultured neurons via a PrP(C)-dependent process. Exogenous PrP(C) added to Prnp knock-out((0/0)) neurons was targeted to synapses and significantly increased Aβ-induced synapse damage. In contrast, the synapse damage induced by a phospholipase A(2)-activating peptide was independent of PrP(C). In Prnp wild-type((+/+)) neurons Aβ oligomers activated synaptic cytoplasmic phospholipase A(2) (cPLA(2)). In these cells, the addition of Aβ oligomers triggered the translocation of cPLA(2) in synapses to cholesterol dense membranes (lipid rafts) where it formed a complex also containing Aβ and PrP(C). In contrast, the addition of Aβ to Prnp((0/0)) neurons did not activate synaptic cPLA(2), which remained in the cytoplasm and was not associated with Aβ. Filtration assays and non-denaturing gels demonstrated that Aβ oligomers cross-link PrP(C). We propose that it is the cross-linkage of PrP(C) by Aβ oligomers that triggers abnormal activation of cPLA(2) and synapse damage. This hypothesis was supported by our observation that monoclonal antibody mediated cross-linkage of PrP(C) also activated synaptic cPLA(2) and caused synapse damage.
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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.