ArticleThe Journal of biological chemistry2016
Sialic Acid on the Glycosylphosphatidylinositol Anchor Regulates PrP-mediated Cell Signaling and Prion Formation.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 40 citations in OpenAlex.
- Phosphatidic Acid Vesicles Convert the Prion Protein into β-Sheet Fibrils with a Thermostable Structure but Temperature-Sensitive Packing.International journal of molecular sciences · 2026Article
- The GPI sidechain ofmBio · 2024Article
- Biological function of sialic acid and sialylation in human health and disease.Cell death discovery · 2024Review
- Structure and Function of the Glycosylphosphatidylinositol Transamidase, a Transmembrane Complex Catalyzing GPI Anchoring of Proteins.Sub-cellular biochemistry · 2024Review
- A point mutation in GPI-attachment signal peptide accelerates the development of prion disease.Acta neuropathologica · 2023Article
- What is the role of lipids in prion conversion and disease?Frontiers in molecular neuroscience · 2022Review
- A knockout cell library of GPI biosynthetic genes for functional studies of GPI-anchored proteins.Communications biology · 2021Article
- The remodel of the "central dogma": a metabolomics interaction perspective.Metabolomics : Official journal of the Metabolomic Society · 2021Review
- α2,3 linkage of sialic acid to a GPI anchor and an unpredicted GPI attachment site in human prion protein.The Journal of biological chemistry · 2020Article
- Prion protein glycans reduce intracerebral fibril formation and spongiosis in prion disease.The Journal of clinical investigation · 2020Article
- Biosynthesis and biology of mammalian GPI-anchored proteins.Open biology · 2020Review
- Cross-talks of glycosylphosphatidylinositol biosynthesis with glycosphingolipid biosynthesis and ER-associated degradation.Nature communications · 2020Article
- Glycosylphosphatidylinositol-Anchor Synthesis in Plants: A Glycobiology Perspective.Frontiers in plant science · 2020Article
- Full restoration of specific infectivity and strain properties from pure mammalian prion protein.PLoS pathogens · 2019Article
- GPI-anchor signal sequence influences PrPC sorting, shedding and signalling, and impacts on different pathomechanistic aspects of prion disease in mice.PLoS pathogens · 2019Article
- Glycosylation Significantly Inhibits the Aggregation of Human Prion Protein and Decreases Its Cytotoxicity.Scientific reports · 2018Article
- Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain.Nature communications · 2018Article
- Characterization of physiochemical properties of caveolin-1 from normal and prion-infected human brains.Oncotarget · 2017Article
- PrP Knockout Cells Expressing Transmembrane PrP Resist Prion Infection.Journal of virology · 2017Article
- The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules.Frontiers in molecular neuroscience · 2017Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The prion diseases occur following the conversion of the cellular prion protein (PrP(C)) into disease-related isoforms (PrP(Sc)). In this study, the role of the glycosylphosphatidylinositol (GPI) anchor attached to PrP(C) in prion formation was examined using a cell painting technique. PrP(Sc) formation in two prion-infected neuronal cell lines (ScGT1 and ScN2a cells) and in scrapie-infected primary cortical neurons was increased following the introduction of PrP(C). In contrast, PrP(C) containing a GPI anchor from which the sialic acid had been removed (desialylated PrP(C)) was not converted to PrP(Sc). Furthermore, the presence of desialylated PrP(C) inhibited the production of PrP(Sc) within prion-infected cortical neurons and ScGT1 and ScN2a cells. The membrane rafts surrounding desialylated PrP(C) contained greater amounts of sialylated gangliosides and cholesterol than membrane rafts surrounding PrP(C). Desialylated PrP(C) was less sensitive to cholesterol depletion than PrP(C) and was not released from cells by treatment with glimepiride. The presence of desialylated PrP(C) in neurons caused the dissociation of cytoplasmic phospholipase A2 from PrP-containing membrane rafts and reduced the activation of cytoplasmic phospholipase A2. These findings show that the sialic acid moiety of the GPI attached to PrP(C) modifies local membrane microenvironments that are important in PrP-mediated cell signaling and PrP(Sc) formation. These results suggest that pharmacological modification of GPI glycosylation might constitute a novel therapeutic approach to prion diseases.
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