ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2013
A mutant prion protein sensitizes neurons to glutamate-induced excitotoxicity.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 47 citations in OpenAlex.
- Mutant prion protein enhances NMDA receptor activity, activates PKC, and triggers rapid excitotoxicity in mice.The Journal of clinical investigation · 2025Article
- Abnormal synaptic architecture in iPSC-derived neurons from a multi-generational family with genetic Creutzfeldt-Jakob disease.Stem cell reports · 2024Article
- Mechanisms of prion-induced toxicity.Cell and tissue research · 2023Review
- Review
- Cellular Prion Protein (PrPc): Putative Interacting Partners and Consequences of the Interaction.International journal of molecular sciences · 2020Review
- Intrinsic toxicity of the cellular prion protein is regulated by its conserved central region.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Transgenic Overexpression of the Disordered Prion Protein N1 Fragment in Mice Does Not Protect Against Neurodegenerative Diseases Due to Impaired ER Translocation.Molecular neurobiology · 2020Article
- The Interplay between CaInternational journal of molecular sciences · 2019Review
- Altered Domain Structure of the Prion Protein Caused by CuStructure (London, England : 1993) · 2019Article
- Prion neurotoxicity.Brain pathology (Zurich, Switzerland) · 2019Review
- Cellular and Molecular Mechanisms of Prion Disease.Annual review of pathology · 2019Review
- Article
- An antipsychotic drug exerts anti-prion effects by altering the localization of the cellular prion protein.PloS one · 2017Article
- Identification of Anti-prion Compounds using a Novel Cellular Assay.The Journal of biological chemistry · 2016Article
- The prion protein family member Shadoo induces spontaneous ionic currents in cultured cells.Scientific reports · 2016Article
- Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice.Scientific reports · 2016Article
- The Essential Role of Soluble Aβ Oligomers in Alzheimer's Disease.Molecular neurobiology · 2016Review
- A cationic tetrapyrrole inhibits toxic activities of the cellular prion protein.Scientific reports · 2016Article
- Expression of the Prion Protein Family Member Shadoo Causes Drug Hypersensitivity That Is Diminished by the Coexpression of the Wild Type Prion Protein.The Journal of biological chemistry · 2016Article
- Activation of zebrafish Src family kinases by the prion protein is an amyloid-β-sensitive signal that prevents the endocytosis and degradation of E-cadherin/β-catenin complexes in vivo.Molecular neurodegeneration · 2016Article
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 4 countries.
Funding
Abstract
Growing evidence suggests that a physiological activity of the cellular prion protein (PrP(C)) plays a crucial role in several neurodegenerative disorders, including prion and Alzheimer's diseases. However, how the functional activity of PrP(C) is subverted to deliver neurotoxic signals remains uncertain. Transgenic (Tg) mice expressing PrP with a deletion of residues 105-125 in the central region (referred to as ΔCR PrP) provide important insights into this problem. Tg(ΔCR) mice exhibit neonatal lethality and massive degeneration of cerebellar granule neurons, a phenotype that is dose dependently suppressed by the presence of wild-type PrP. When expressed in cultured cells, ΔCR PrP induces large, ionic currents that can be detected by patch-clamping techniques. Here, we tested the hypothesis that abnormal ion channel activity underlies the neuronal death seen in Tg(ΔCR) mice. We find that ΔCR PrP induces abnormal ionic currents in neurons in culture and in cerebellar slices and that this activity sensitizes the neurons to glutamate-induced, calcium-mediated death. In combination with ultrastructural and biochemical analyses, these results demonstrate a role for glutamate-induced excitotoxicity in PrP-mediated neurodegeneration. A similar mechanism may operate in other neurodegenerative disorders attributable to toxic, β-rich oligomers that bind to PrP(C).
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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.