High pressure, a tool to switch between soluble and fibrillar prion protein structures
Identifieur interne : 000E86 ( Ncbi/Merge ); précédent : 000E85; suivant : 000E87High pressure, a tool to switch between soluble and fibrillar prion protein structures
Auteurs : Joan Torrent ; Reinhard LangeSource :
- Communicative & Integrative Biology [ 1942-0889 ] ; 2012.
Abstract
The native soluble as well as different aggregated states of recombinant prion proteins are highly sensitive to high pressure. On the one hand, its application to the native α-helical protein induces reversibly a metastable structure that relaxes to amyloid fibrils after prolonged incubation. On the other hand, its application to synthetic prion amyloid fibrils leads to partial disaggregation into native monomers as well as to proto-filaments that have lost several amyloid features. In addition, heat-induced β-sheet prion protein aggregates are dissolved and revert into α-helical monomers by applying high pressure. This profound pressure sensitivity of prion protein structure is explained by large volume differences of the different structural states. Hence, pressure appears as a suitable thermodynamic parameter for exploring the highly complex conformational landscape of prion protein. Its further analysis should help identifying prion protein structural states that are on the pathogenic pathway.
Url:
PubMed: 22482006
PubMed Central: 3291310
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">High pressure, a tool to switch between soluble and fibrillar prion protein structures</title><author><name sortKey="Torrent, Joan" sort="Torrent, Joan" uniqKey="Torrent J" first="Joan" last="Torrent">Joan Torrent</name><affiliation><nlm:aff>NONE</nlm:aff></affiliation></author><author><name sortKey="Lange, Reinhard" sort="Lange, Reinhard" uniqKey="Lange R" first="Reinhard" last="Lange">Reinhard Lange</name><affiliation><nlm:aff>NONE</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">22482006</idno><idno type="pmc">3291310</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3291310</idno><idno type="RBID">PMC:3291310</idno><date when="2012">2012</date><idno type="wicri:Area/Pmc/Corpus">000903</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000903</idno><idno type="wicri:Area/Pmc/Curation">000899</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000899</idno><idno type="wicri:Area/Pmc/Checkpoint">000613</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000613</idno><idno type="wicri:Area/Ncbi/Merge">000E86</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">High pressure, a tool to switch between soluble and fibrillar prion protein structures</title><author><name sortKey="Torrent, Joan" sort="Torrent, Joan" uniqKey="Torrent J" first="Joan" last="Torrent">Joan Torrent</name><affiliation><nlm:aff>NONE</nlm:aff></affiliation></author><author><name sortKey="Lange, Reinhard" sort="Lange, Reinhard" uniqKey="Lange R" first="Reinhard" last="Lange">Reinhard Lange</name><affiliation><nlm:aff>NONE</nlm:aff></affiliation></author></analytic><series><title level="j">Communicative & Integrative Biology</title><idno type="eISSN">1942-0889</idno><imprint><date when="2012">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The native soluble as well as different aggregated states of recombinant prion proteins are highly sensitive to high pressure. On the one hand, its application to the native α-helical protein induces reversibly a metastable structure that relaxes to amyloid fibrils after prolonged incubation. On the other hand, its application to synthetic prion amyloid fibrils leads to partial disaggregation into native monomers as well as to proto-filaments that have lost several amyloid features. In addition, heat-induced β-sheet prion protein aggregates are dissolved and revert into α-helical monomers by applying high pressure. This profound pressure sensitivity of prion protein structure is explained by large volume differences of the different structural states. Hence, pressure appears as a suitable thermodynamic parameter for exploring the highly complex conformational landscape of prion protein. Its further analysis should help identifying prion protein structural states that are on the pathogenic pathway.</p></div></front></TEI><pmc article-type="review-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Commun Integr Biol</journal-id><journal-id journal-id-type="iso-abbrev">Commun Integr Biol</journal-id><journal-id journal-id-type="publisher-id">CIB</journal-id><journal-title-group><journal-title>Communicative & Integrative Biology</journal-title></journal-title-group><issn pub-type="epub">1942-0889</issn><publisher><publisher-name>Landes Bioscience</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">22482006</article-id><article-id pub-id-type="pmc">3291310</article-id><article-id pub-id-type="publisher-id">2011CIB0165</article-id><article-id pub-id-type="pii">17969</article-id><article-categories><subj-group subj-group-type="heading"><subject>Mini Review</subject></subj-group></article-categories><title-group><article-title>High pressure, a tool to switch between soluble and fibrillar prion protein structures</article-title></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name><surname>Torrent</surname><given-names>Joan</given-names></name><xref ref-type="aff" rid="A1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Lange</surname><given-names>Reinhard</given-names></name><xref ref-type="aff" rid="A2"><sup>2</sup></xref></contrib><aff id="A1"><label>(1)</label>INRA; Unité de Virologie & Immunologie Moléculaires; Jouy-en-Josas, France; Univ Montpellier ; Montpellier, France; Inserm; Montpellier, France; EPHE; Paris, France</aff><aff id="A2"><label>(2)</label>Univ Montpellier ; Montpellier, France; Inserm; Montpellier, France; EPHE; Paris, France</aff></contrib-group><author-notes><corresp>Correspondence to: Joan Torrent; Email: <email>joan.torrent@inserm.fr</email></corresp></author-notes><pub-date pub-type="ppub"><day>01</day><month>1</month><year>2012</year></pub-date><pub-date pub-type="pmc-release"><day>01</day><month>1</month><year>2012</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
<volume>5</volume><issue>1</issue><fpage>30</fpage><lpage>33</lpage><permissions><copyright-statement>Copyright © 2012 Landes Bioscience</copyright-statement><copyright-year>2012</copyright-year></permissions><abstract><p>The native soluble as well as different aggregated states of recombinant prion proteins are highly sensitive to high pressure. On the one hand, its application to the native α-helical protein induces reversibly a metastable structure that relaxes to amyloid fibrils after prolonged incubation. On the other hand, its application to synthetic prion amyloid fibrils leads to partial disaggregation into native monomers as well as to proto-filaments that have lost several amyloid features. In addition, heat-induced β-sheet prion protein aggregates are dissolved and revert into α-helical monomers by applying high pressure. This profound pressure sensitivity of prion protein structure is explained by large volume differences of the different structural states. Hence, pressure appears as a suitable thermodynamic parameter for exploring the highly complex conformational landscape of prion protein. Its further analysis should help identifying prion protein structural states that are on the pathogenic pathway.</p></abstract><kwd-group kwd-group-type="author"><title>Keywords: </title><kwd>amyloid</kwd><kwd>high pressure</kwd><kwd>prion</kwd><kwd>protein misfolding</kwd></kwd-group></article-meta></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Lange, Reinhard" sort="Lange, Reinhard" uniqKey="Lange R" first="Reinhard" last="Lange">Reinhard Lange</name><name sortKey="Torrent, Joan" sort="Torrent, Joan" uniqKey="Torrent J" first="Joan" last="Torrent">Joan Torrent</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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