ArticleThe American journal of pathology2014
Uptake and degradation of protease-sensitive and -resistant forms of abnormal human prion protein aggregates by human astrocytes.
Article in The American journal of pathology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 34 citations in OpenAlex.
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- Neurons and astrocytes have distinct organelle signatures and responses to stress.Cell reports · 2025Article
- Glial phagocytosis for synapse and toxic proteins in neurodegenerative diseases.Molecular neurodegeneration · 2025Review
- Strain-Dependent Morphology of Reactive Astrocytes in Human- and Animal-Vole-Adapted Prions.Biomolecules · 2023Article
- Article
- Astrocyte in prion disease: a double-edged sword.Neural regeneration research · 2022Review
- The role of astrocytes in prion-like mechanisms of neurodegeneration.Brain : a journal of neurology · 2022Review
- Review
- Article
- Lysosomal Functions in Glia Associated with Neurodegeneration.Biomolecules · 2021Review
- Non-cell autonomous astrocyte-mediated neuronal toxicity in prion diseases.Acta neuropathologica communications · 2021Article
- Region-specific glial homeostatic signature in prion diseases is replaced by a uniform neuroinflammation signature, common for brain regions and prion strains with different cell tropism.Neurobiology of disease · 2020Article
- Distinct responses of neurons and astrocytes to TDP-43 proteinopathy in amyotrophic lateral sclerosis.Brain : a journal of neurology · 2020Article
- Complement 3Acta neuropathologica communications · 2019Article
- Full restoration of specific infectivity and strain properties from pure mammalian prion protein.PLoS pathogens · 2019Article
- Region-Specific Response of Astrocytes to Prion Infection.Frontiers in neuroscience · 2019Article
- Article
- Diversity of astroglial responses across human neurodegenerative disorders and brain aging.Brain pathology (Zurich, Switzerland) · 2017Article
- PrPSc formation and clearance as determinants of prion tropism.PLoS pathogens · 2017Article
- Prion Strain Diversity.Cold Spring Harbor perspectives in medicine · 2016Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Sporadic Creutzfeldt-Jakob disease is the most common of the human prion diseases, a group of rare, transmissible, and fatal neurologic diseases associated with the accumulation of an abnormal form (PrP(Sc)) of the host prion protein. In sporadic Creutzfeldt-Jakob disease, disease-associated PrP(Sc) is present not only as an aggregated, protease-resistant form but also as an aggregated protease-sensitive form (sPrP(Sc)). Although evidence suggests that sPrP(Sc) may play a role in prion pathogenesis, little is known about how it interacts with cells during prion infection. Here, we show that protease-sensitive abnormal PrP aggregates derived from patients with sporadic Creutzfeldt-Jakob disease are taken up and degraded by immortalized human astrocytes similarly to abnormal PrP aggregates that are resistant to proteases. Our data suggest that relative proteinase K resistance does not significantly influence the astrocyte's ability to degrade PrP(Sc). Furthermore, the cell does not appear to distinguish between sPrP(Sc) and protease-resistant PrP(Sc), suggesting that sPrP(Sc) could contribute to prion infection.
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