ArticleThe American journal of pathology2010
A highly toxic cellular prion protein induces a novel, nonapoptotic form of neuronal death.
Article in The American journal of pathology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Reflections on Cerebellar Neuropathology in Classical Scrapie.Biomolecules · 2021Review
- 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
- Prion neurotoxicity.Brain pathology (Zurich, Switzerland) · 2019Review
- Altered distribution, aggregation, and protease resistance of cellular prion protein following intracranial inoculation.PloS one · 2019Article
- Article
- An antipsychotic drug exerts anti-prion effects by altering the localization of the cellular prion protein.PloS one · 2017Article
- A mutant prion protein sensitizes neurons to glutamate-induced excitotoxicity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Prion protein at the crossroads of physiology and disease.Trends in neurosciences · 2012Review
- Neurotoxic mutants of the prion protein induce spontaneous ionic currents in cultured cells.The Journal of biological chemistry · 2010Article
- Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Several different deletions within the N-terminal tail of the prion protein (PrP) induce massive neuronal death when expressed in transgenic mice. This toxicity is dose-dependently suppressed by coexpression of full-length PrP, suggesting that it results from subversion of a normal physiological activity of cellular PrP. We performed a combined biochemical and morphological analysis of Tg(DeltaCR) mice, which express PrP carrying a 21-aa deletion (residues 105-125) within a highly conserved region of the protein. Death of cerebellar granule neurons in Tg(DeltaCR) mice is not accompanied by activation of either caspase-3 or caspase-8 or by increased levels of the autophagy marker, LC3-II. In electron micrographs, degenerating granule neurons displayed a unique morphology characterized by heterogeneous condensation of the nuclear matrix without formation of discrete chromatin masses typical of neuronal apoptosis. Our data demonstrate that perturbations in PrP functional activity induce a novel, nonapoptotic, nonautophagic form of neuronal death whose morphological features are reminiscent of those associated with excitotoxic stress.
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