ArticlePrion
β-amyloid oligomers and prion protein: Fatal attraction?
Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Cellular Prion Protein and Amyloid-β Oligomers in Alzheimer's Disease-Are There Connections?International journal of molecular sciences · 2025Review
- α-Synuclein strain propagation is independent of cellular prion protein expression in a transgenic synucleinopathy mouse model.PLoS pathogens · 2024Article
- Cellular prion protein offers neuroprotection in astrocytes submitted to amyloid β oligomer toxicity.Molecular and cellular biochemistry · 2023Article
- Review
- Doxycycline for Alzheimer's Disease: Fighting β-Amyloid Oligomers and Neuroinflammation.Frontiers in pharmacology · 2019Review
- The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules.Frontiers in molecular neuroscience · 2017Article
- Soluble amyloid-β oligomers as synaptotoxins leading to cognitive impairment in Alzheimer's disease.Frontiers in cellular neuroscience · 2015Review
- Targeted discovery and validation of plasma biomarkers of Parkinson's disease.Journal of proteome research · 2014Article
- Derailed intraneuronal signalling drives pathogenesis in sporadic and familial Alzheimer's disease.BioMed research international · 2014Review
- Article
- Interaction between pathogenic proteins in neurodegenerative disorders.Journal of cellular and molecular medicine · 2012Review
- Allosteric function and dysfunction of the prion protein.Cellular and molecular life sciences : CMLS · 2012Review
- Postsynaptic Receptors for Amyloid-β Oligomers as Mediators of Neuronal Damage in Alzheimer's Disease.Frontiers in physiology · 2012Article
- Review
- Review
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The relationship between Alzheimer disease (AD) and prion-related encephalopathies (TSE) has been proposed by different points of view. Recently, the scientific attention has been attracted by the results proposing the possibility that PrPc, the protein whose pathologic form is responsible of TSE, can mediated the toxic effect of β amyloid (Aβ) oligomers. The oligomers are considered the culprit of the neurodegenerative process associated to AD, although the pathogenic mechanism activated by these small aggregates remain to be elucidated. In the initial study based on the binding screening PrPc was identified as ligand /receptor of Aβ oligomers, while long term potentiation (LTP) analysis in vitro and behavioural studies in vivo, demonstrated that the absence of PrPc abolished the damage induced by Aβ oligomers. The high affinity binding Aβ oligomers-PrPc has been confirmed, whereas a functional role of this association has been excluded by three different studies. We approached this issue by the direct application of Aβ oligomers in the brain followed by the behavioural examination of memory deficits. Our data using PrP knock-out mice suggest that Aβ 1-42 oligomers are responsible for cognitive impairment in AD but PrPc is not required for their effect. Similarly, in two other studies the LTP alterations induced by Aβ 1-42 oligomers was not influenced by the absence of PrP. Possible explanations of these contradictory results are discussed.
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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.