Phospholipids influence the aggregation of recombinant ovine prions. From rapid extensive aggregation to amyloidogenic conversion.
Identifieur interne : 001E91 ( PubMed/Checkpoint ); précédent : 001E90; suivant : 001E92Phospholipids influence the aggregation of recombinant ovine prions. From rapid extensive aggregation to amyloidogenic conversion.
Auteurs : Kirill Tsiroulnikov [France] ; Yuliya Shchutskaya ; Vladimir Muronetz ; Jean-Marc Chobert ; Thomas HaertléSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2009.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Endopeptidase K, Maladies à prions, Protéines PrPC.
- pharmacologie : Phospholipides.
- Animaux, Ovis, Prions, Structure quaternaire des protéines, Structure secondaire des protéines.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Prions.
- chemical , metabolism : Endopeptidase K, PrPC Proteins.
- chemical , pharmacology : Phospholipids.
- metabolism : Prion Diseases.
- Animals, Protein Structure, Quaternary, Protein Structure, Secondary, Sheep.
Abstract
The transformation of prion protein (PrP) into its insoluble amyloid form correlates with neurodegeneration in transmissible spongiform encephalopathies. PrP is connected to the neuronal membrane by a covalently-linked glycosylphosphatidylinositol (GPI) anchor. The current study demonstrates that phosphatidylinositol and phosphatidylethanolamine in low concentrations (0.5-50 muM) stimulate rapid unlimited aggregation of PrP. At a higher concentration (500 muM), lipid particles prevent the formation of large PrP aggregates and induce an increase in the beta-sheet structure content of PrP protein. Thus, the liberation of PrP from the membrane and its direct interaction with its own GPI moiety, as well as with membrane lipids, can promote the formation of aggregated structures of PrP. The phospholipids studied are also able to upregulate the aggregation of oligomeric PrP forms (12-mers and 36-mers), the neurotoxicity of which has been reported recently. Low phosphatidylinositol concentrations induce these oligomers to form aggregates of smaller size when compared with aggregates formed directly from monomers. The inhibition of extensive aggregation observed at a high concentration of phosphatidylinositol (500 muM) results in both the formation of amyloids from PrP monomers and the interaction of protein molecules with lipid micelles. Thus, phospholipids are not only involved in the aggregation of prion monomers and their amyloidogenic conversion, but also regulate the aggregative status of prion oligomers already formed. Consequently, depending on their micellar status, phospholipids can either promote amyloidogenic conversion and conserve neurotoxic oligomeric forms (lipid micelles) or mediate the formation of large-size amorphous aggregates (non-micellar phospholipids).
DOI: 10.1016/j.bbapap.2008.12.002
PubMed: 19124088
Affiliations:
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pubmed:19124088Le document en format XML
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<front><div type="abstract" xml:lang="en">The transformation of prion protein (PrP) into its insoluble amyloid form correlates with neurodegeneration in transmissible spongiform encephalopathies. PrP is connected to the neuronal membrane by a covalently-linked glycosylphosphatidylinositol (GPI) anchor. The current study demonstrates that phosphatidylinositol and phosphatidylethanolamine in low concentrations (0.5-50 muM) stimulate rapid unlimited aggregation of PrP. At a higher concentration (500 muM), lipid particles prevent the formation of large PrP aggregates and induce an increase in the beta-sheet structure content of PrP protein. Thus, the liberation of PrP from the membrane and its direct interaction with its own GPI moiety, as well as with membrane lipids, can promote the formation of aggregated structures of PrP. The phospholipids studied are also able to upregulate the aggregation of oligomeric PrP forms (12-mers and 36-mers), the neurotoxicity of which has been reported recently. Low phosphatidylinositol concentrations induce these oligomers to form aggregates of smaller size when compared with aggregates formed directly from monomers. The inhibition of extensive aggregation observed at a high concentration of phosphatidylinositol (500 muM) results in both the formation of amyloids from PrP monomers and the interaction of protein molecules with lipid micelles. Thus, phospholipids are not only involved in the aggregation of prion monomers and their amyloidogenic conversion, but also regulate the aggregative status of prion oligomers already formed. Consequently, depending on their micellar status, phospholipids can either promote amyloidogenic conversion and conserve neurotoxic oligomeric forms (lipid micelles) or mediate the formation of large-size amorphous aggregates (non-micellar phospholipids).</div>
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