Phospholipids influence the aggregation of recombinant ovine prions. From rapid extensive aggregation to amyloidogenic conversion.
Identifieur interne : 002776 ( Main/Exploration ); précédent : 002775; suivant : 002777Phospholipids 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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From rapid extensive aggregation to amyloidogenic conversion.</title><author><name sortKey="Tsiroulnikov, Kirill" sort="Tsiroulnikov, Kirill" uniqKey="Tsiroulnikov K" first="Kirill" last="Tsiroulnikov">Kirill Tsiroulnikov</name><affiliation wicri:level="3"><nlm:affiliation>Institut National de la Recherche Agronomique, BIA-FIPL, BP 71627, F-44316 Nantes Cedex 3, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut National de la Recherche Agronomique, BIA-FIPL, BP 71627, F-44316 Nantes Cedex 3</wicri:regionArea><placeName><region type="region" nuts="2">Pays de la Loire</region><settlement type="city">Nantes</settlement></placeName></affiliation></author><author><name sortKey="Shchutskaya, Yuliya" sort="Shchutskaya, Yuliya" uniqKey="Shchutskaya Y" first="Yuliya" last="Shchutskaya">Yuliya Shchutskaya</name></author><author><name sortKey="Muronetz, Vladimir" sort="Muronetz, Vladimir" uniqKey="Muronetz V" first="Vladimir" last="Muronetz">Vladimir Muronetz</name></author><author><name sortKey="Chobert, Jean Marc" sort="Chobert, Jean Marc" uniqKey="Chobert J" first="Jean-Marc" last="Chobert">Jean-Marc Chobert</name></author><author><name sortKey="Haertle, Thomas" sort="Haertle, Thomas" uniqKey="Haertle T" first="Thomas" last="Haertlé">Thomas Haertlé</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19124088</idno><idno type="pmid">19124088</idno><idno type="doi">10.1016/j.bbapap.2008.12.002</idno><idno type="wicri:Area/PubMed/Corpus">002041</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002041</idno><idno type="wicri:Area/PubMed/Curation">002041</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002041</idno><idno type="wicri:Area/PubMed/Checkpoint">001E91</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001E91</idno><idno type="wicri:Area/Ncbi/Merge">000660</idno><idno type="wicri:Area/Ncbi/Curation">000660</idno><idno type="wicri:Area/Ncbi/Checkpoint">000660</idno><idno type="wicri:doubleKey">0006-3002:2009:Tsiroulnikov K:phospholipids:influence:the</idno><idno type="wicri:Area/Main/Merge">002801</idno><idno type="wicri:Area/Main/Curation">002776</idno><idno type="wicri:Area/Main/Exploration">002776</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Phospholipids influence the aggregation of recombinant ovine prions. From rapid extensive aggregation to amyloidogenic conversion.</title><author><name sortKey="Tsiroulnikov, Kirill" sort="Tsiroulnikov, Kirill" uniqKey="Tsiroulnikov K" first="Kirill" last="Tsiroulnikov">Kirill Tsiroulnikov</name><affiliation wicri:level="3"><nlm:affiliation>Institut National de la Recherche Agronomique, BIA-FIPL, BP 71627, F-44316 Nantes Cedex 3, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut National de la Recherche Agronomique, BIA-FIPL, BP 71627, F-44316 Nantes Cedex 3</wicri:regionArea><placeName><region type="region" nuts="2">Pays de la Loire</region><settlement type="city">Nantes</settlement></placeName></affiliation></author><author><name sortKey="Shchutskaya, Yuliya" sort="Shchutskaya, Yuliya" uniqKey="Shchutskaya Y" first="Yuliya" last="Shchutskaya">Yuliya Shchutskaya</name></author><author><name sortKey="Muronetz, Vladimir" sort="Muronetz, Vladimir" uniqKey="Muronetz V" first="Vladimir" last="Muronetz">Vladimir Muronetz</name></author><author><name sortKey="Chobert, Jean Marc" sort="Chobert, Jean Marc" uniqKey="Chobert J" first="Jean-Marc" last="Chobert">Jean-Marc Chobert</name></author><author><name sortKey="Haertle, Thomas" sort="Haertle, Thomas" uniqKey="Haertle T" first="Thomas" last="Haertlé">Thomas Haertlé</name></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Endopeptidase K (metabolism)</term><term>Phospholipids (pharmacology)</term><term>PrPC Proteins (metabolism)</term><term>Prion Diseases (metabolism)</term><term>Prions (chemistry)</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Secondary</term><term>Sheep</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Endopeptidase K (métabolisme)</term><term>Maladies à prions (métabolisme)</term><term>Ovis</term><term>Phospholipides (pharmacologie)</term><term>Prions ()</term><term>Protéines PrPC (métabolisme)</term><term>Structure quaternaire des protéines</term><term>Structure secondaire des protéines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Prions</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Endopeptidase K</term><term>PrPC Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Phospholipids</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Prion Diseases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Endopeptidase K</term><term>Maladies à prions</term><term>Protéines PrPC</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Phospholipides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Secondary</term><term>Sheep</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Ovis</term><term>Prions</term><term>Structure quaternaire des protéines</term><term>Structure secondaire des protéines</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><affiliations><list><country><li>France</li></country><region><li>Pays de la Loire</li></region><settlement><li>Nantes</li></settlement></list><tree><noCountry><name sortKey="Chobert, Jean Marc" sort="Chobert, Jean Marc" uniqKey="Chobert J" first="Jean-Marc" last="Chobert">Jean-Marc Chobert</name><name sortKey="Haertle, Thomas" sort="Haertle, Thomas" uniqKey="Haertle T" first="Thomas" last="Haertlé">Thomas Haertlé</name><name sortKey="Muronetz, Vladimir" sort="Muronetz, Vladimir" uniqKey="Muronetz V" first="Vladimir" last="Muronetz">Vladimir Muronetz</name><name sortKey="Shchutskaya, Yuliya" sort="Shchutskaya, Yuliya" uniqKey="Shchutskaya Y" first="Yuliya" last="Shchutskaya">Yuliya Shchutskaya</name></noCountry><country name="France"><region name="Pays de la Loire"><name sortKey="Tsiroulnikov, Kirill" sort="Tsiroulnikov, Kirill" uniqKey="Tsiroulnikov K" first="Kirill" last="Tsiroulnikov">Kirill Tsiroulnikov</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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