ArticlePloS one2014
Role of lipid rafts and GM1 in the segregation and processing of prion protein.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 41 citations in OpenAlex.
- The Human Ganglioside Interactome in Live Cells Revealed Using Clickable Photoaffinity Ganglioside Probes.Journal of the American Chemical Society · 2024Article
- What is the role of lipids in prion conversion and disease?Frontiers in molecular neuroscience · 2022Review
- A Comprehensive Review: Sphingolipid Metabolism and Implications of Disruption in Sphingolipid Homeostasis.International journal of molecular sciences · 2021Review
- Article
- PrPFrontiers in molecular neuroscience · 2021Review
- Mutant prion proteins increase calcium permeability of AMPA receptors, exacerbating excitotoxicity.PLoS pathogens · 2020Article
- Prion Protein in Stem Cells: A Lipid Raft Component Involved in the Cellular Differentiation Process.International journal of molecular sciences · 2020Review
- Neurotrophic effects of GScientific reports · 2020Article
- Differential Aggregation and Phosphorylation of Alpha Synuclein in Membrane Compartments Associated With Parkinson Disease.Frontiers in neuroscience · 2019Article
- Inflammatory mediators reduce surface PrPLaboratory investigation; a journal of technical methods and pathology · 2018Article
- Article
- Changes in Membrane Protein Clustering in Peripheral Lymphocytes in an Animal Model of Depression Parallel Those Observed in Naïve Depression Patients: Implications for the Development of Novel Biomarkers of Depression.Frontiers in pharmacology · 2018Article
- Membrane Disruption Mechanism of a Prion Peptide (106-126) Investigated by Atomic Force Microscopy, Raman and Electron Paramagnetic Resonance Spectroscopy.The journal of physical chemistry. B · 2017Article
- Monosialoganglioside-GM1 triggers binding of the amyloid-protein salmon calcitonin to a Langmuir membrane model mimicking the occurrence of lipid-rafts.Biochemistry and biophysics reports · 2016Article
- The Anti-Prion Antibody 15B3 Detects Toxic Amyloid-β Oligomers.Journal of Alzheimer's disease : JAD · 2016Article
- Impact of cholesterol on disease progression.BioMedicine · 2015Article
- Mechanism of scrapie prion precipitation with phosphotungstate anions.ACS chemical biology · 2015Article
- Structural and dynamic views of GM1 ganglioside.Glycoconjugate journal · 2015Review
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The prion protein (PrPC) is highly expressed within the nervous system. Similar to other GPI-anchored proteins, PrPC is found in lipid rafts, membrane domains enriched in cholesterol and sphingolipids. PrPC raft association, together with raft lipid composition, appears essential for the conversion of PrPC into the scrapie isoform PrPSc, and the development of prion disease. Controversial findings were reported on the nature of PrPC-containing rafts, as well as on the distribution of PrPC between rafts and non-raft membranes. We investigated PrPC/ganglioside relationships and their influence on PrPC localization in a neuronal cellular model, cerebellar granule cells. Our findings argue that in these cells at least two PrPC conformations coexist: in lipid rafts PrPC is present in the native folding (α-helical), stabilized by chemico-physical condition, while it is mainly present in other membrane compartments in a PrPSc-like conformation. We verified, by means of antibody reactivity and circular dichroism spectroscopy, that changes in lipid raft-ganglioside content alters PrPC conformation and interaction with lipid bilayers, without modifying PrPC distribution or cleavage. Our data provide new insights into the cellular mechanism of prion conversion and suggest that GM1-prion protein interaction at the cell surface could play a significant role in the mechanism predisposing to pathology.
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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.