Gerstmann-Sträussler-Scheinker disease amyloid protein polymerizes according to the "dock-and-lock" model.
Identifieur interne : 002126 ( PubMed/Checkpoint ); précédent : 002125; suivant : 002127Gerstmann-Sträussler-Scheinker disease amyloid protein polymerizes according to the "dock-and-lock" model.
Auteurs : Marco Gobbi [Italie] ; Laura Colombo ; Michela Morbin ; Giulia Mazzoleni ; Elena Accardo ; Marco Vanoni ; Elena Del Favero ; Laura Cantù ; Daniel A. Kirschner ; Claudia Manzoni ; Marten Beeg ; Paolo Ceci ; Paolo Ubezio ; Gianluigi Forloni ; Fabrizio Tagliavini ; Mario SalmonaSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2006.
Descripteurs français
- KwdFr :
- Amyloïde (), Animaux, Cinétique, Cricetinae, Dénaturation des protéines, Facteurs temps, Humains, Liaison aux protéines, Microscopie électronique, Modèles chimiques, Peptides (), Pliage des protéines, Polymères (), Propriétés de surface, Résonance plasmonique de surface, Syndrome de Gerstmann-Sträussler-Scheinker (métabolisme), Épitopes.
- MESH :
- métabolisme : Syndrome de Gerstmann-Sträussler-Scheinker.
- Amyloïde, Animaux, Cinétique, Cricetinae, Dénaturation des protéines, Facteurs temps, Humains, Liaison aux protéines, Microscopie électronique, Modèles chimiques, Peptides, Pliage des protéines, Polymères, Propriétés de surface, Résonance plasmonique de surface, Épitopes.
English descriptors
- KwdEn :
- Amyloid (chemistry), Animals, Cricetinae, Epitopes, Gerstmann-Straussler-Scheinker Disease (metabolism), Humans, Kinetics, Microscopy, Electron, Models, Chemical, Peptides (chemistry), Polymers (chemistry), Protein Binding, Protein Denaturation, Protein Folding, Surface Plasmon Resonance, Surface Properties, Time Factors.
- MESH :
- chemical , chemistry : Amyloid, Peptides, Polymers.
- metabolism : Gerstmann-Straussler-Scheinker Disease.
- Animals, Cricetinae, Epitopes, Humans, Kinetics, Microscopy, Electron, Models, Chemical, Protein Binding, Protein Denaturation, Protein Folding, Surface Plasmon Resonance, Surface Properties, Time Factors.
Abstract
Prion protein (PrP) amyloid formation is a central feature of genetic and acquired prion diseases such as Gerstmann-Sträussler-Scheinker disease (GSS) and variant Creutzfeldt-Jakob disease. The major component of GSS amyloid is a PrP fragment spanning residues approximately 82-146, which when synthesized as a peptide, readily forms fibrils featuring GSS amyloid. The present study employed surface plasmon resonance (SPR) to characterize the binding events underlying PrP82-146 oligomerization at the first stages of fibrillization, according to evidence suggesting a pathogenic role of prefibrillar oligomers rather than mature amyloid fibrils. We followed in real time the binding reactions occurring during short term (seconds) addition of PrP82-146 small oligomers (1-5-mers, flowing species) onto soluble prefibrillar PrP82-146 aggregates immobilized on the sensor surface. SPR data confirmed very efficient aggregation/elongation, consistent with the hypothesis of nucleation-dependent polymerization process. Much lower binding was observed when PrP82-146 flowed onto the scrambled sequence of PrP82-146 or onto prefibrillar Abeta42 aggregates. As previously found with Abeta40, SPR data could be adequately fitted by equations modeling the "dock-and-lock" mechanism, in which the "locking" step is due to sequential conformational changes, each increasing the affinity of the monomer for the fibril until a condition of irreversible binding is reached. However, these conformational changes (i.e. the locking steps) appear to be faster and easier with PrP82-146 than with Abeta40. Such differences suggest that PrP82-146 has a greater propensity to polymerize and greater stability of the aggregates.
DOI: 10.1074/jbc.M506164200
PubMed: 16286452
Affiliations:
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pubmed:16286452Le document en format XML
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Gobbi@marionegri.it</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Istituto di Ricerche Farmacologiche Mario Negri, Milano</wicri:regionArea><wicri:noRegion>Milano</wicri:noRegion></affiliation></author><author><name sortKey="Colombo, Laura" sort="Colombo, Laura" uniqKey="Colombo L" first="Laura" last="Colombo">Laura Colombo</name></author><author><name sortKey="Morbin, Michela" sort="Morbin, Michela" uniqKey="Morbin M" first="Michela" last="Morbin">Michela Morbin</name></author><author><name sortKey="Mazzoleni, Giulia" sort="Mazzoleni, Giulia" uniqKey="Mazzoleni G" first="Giulia" last="Mazzoleni">Giulia Mazzoleni</name></author><author><name sortKey="Accardo, Elena" sort="Accardo, Elena" uniqKey="Accardo E" first="Elena" last="Accardo">Elena Accardo</name></author><author><name sortKey="Vanoni, Marco" sort="Vanoni, Marco" uniqKey="Vanoni M" first="Marco" last="Vanoni">Marco Vanoni</name></author><author><name sortKey="Del Favero, Elena" sort="Del Favero, Elena" uniqKey="Del Favero E" first="Elena" last="Del Favero">Elena Del Favero</name></author><author><name sortKey="Cantu, Laura" sort="Cantu, Laura" uniqKey="Cantu L" first="Laura" last="Cantù">Laura Cantù</name></author><author><name sortKey="Kirschner, Daniel A" sort="Kirschner, Daniel A" uniqKey="Kirschner D" first="Daniel A" last="Kirschner">Daniel A. Kirschner</name></author><author><name sortKey="Manzoni, Claudia" sort="Manzoni, Claudia" uniqKey="Manzoni C" first="Claudia" last="Manzoni">Claudia Manzoni</name></author><author><name sortKey="Beeg, Marten" sort="Beeg, Marten" uniqKey="Beeg M" first="Marten" last="Beeg">Marten Beeg</name></author><author><name sortKey="Ceci, Paolo" sort="Ceci, Paolo" uniqKey="Ceci P" first="Paolo" last="Ceci">Paolo Ceci</name></author><author><name sortKey="Ubezio, Paolo" sort="Ubezio, Paolo" uniqKey="Ubezio P" first="Paolo" last="Ubezio">Paolo Ubezio</name></author><author><name sortKey="Forloni, Gianluigi" sort="Forloni, Gianluigi" uniqKey="Forloni G" first="Gianluigi" last="Forloni">Gianluigi Forloni</name></author><author><name sortKey="Tagliavini, Fabrizio" sort="Tagliavini, Fabrizio" uniqKey="Tagliavini F" first="Fabrizio" last="Tagliavini">Fabrizio Tagliavini</name></author><author><name sortKey="Salmona, Mario" sort="Salmona, Mario" uniqKey="Salmona M" first="Mario" last="Salmona">Mario Salmona</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amyloid (chemistry)</term><term>Animals</term><term>Cricetinae</term><term>Epitopes</term><term>Gerstmann-Straussler-Scheinker Disease (metabolism)</term><term>Humans</term><term>Kinetics</term><term>Microscopy, Electron</term><term>Models, Chemical</term><term>Peptides (chemistry)</term><term>Polymers (chemistry)</term><term>Protein Binding</term><term>Protein Denaturation</term><term>Protein Folding</term><term>Surface Plasmon Resonance</term><term>Surface Properties</term><term>Time Factors</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Amyloïde ()</term><term>Animaux</term><term>Cinétique</term><term>Cricetinae</term><term>Dénaturation des protéines</term><term>Facteurs temps</term><term>Humains</term><term>Liaison aux protéines</term><term>Microscopie électronique</term><term>Modèles chimiques</term><term>Peptides ()</term><term>Pliage des protéines</term><term>Polymères ()</term><term>Propriétés de surface</term><term>Résonance plasmonique de surface</term><term>Syndrome de Gerstmann-Sträussler-Scheinker (métabolisme)</term><term>Épitopes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amyloid</term><term>Peptides</term><term>Polymers</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Gerstmann-Straussler-Scheinker Disease</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Syndrome de Gerstmann-Sträussler-Scheinker</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cricetinae</term><term>Epitopes</term><term>Humans</term><term>Kinetics</term><term>Microscopy, Electron</term><term>Models, Chemical</term><term>Protein Binding</term><term>Protein Denaturation</term><term>Protein Folding</term><term>Surface Plasmon Resonance</term><term>Surface Properties</term><term>Time Factors</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Amyloïde</term><term>Animaux</term><term>Cinétique</term><term>Cricetinae</term><term>Dénaturation des protéines</term><term>Facteurs temps</term><term>Humains</term><term>Liaison aux protéines</term><term>Microscopie électronique</term><term>Modèles chimiques</term><term>Peptides</term><term>Pliage des protéines</term><term>Polymères</term><term>Propriétés de surface</term><term>Résonance plasmonique de surface</term><term>Épitopes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Prion protein (PrP) amyloid formation is a central feature of genetic and acquired prion diseases such as Gerstmann-Sträussler-Scheinker disease (GSS) and variant Creutzfeldt-Jakob disease. The major component of GSS amyloid is a PrP fragment spanning residues approximately 82-146, which when synthesized as a peptide, readily forms fibrils featuring GSS amyloid. The present study employed surface plasmon resonance (SPR) to characterize the binding events underlying PrP82-146 oligomerization at the first stages of fibrillization, according to evidence suggesting a pathogenic role of prefibrillar oligomers rather than mature amyloid fibrils. We followed in real time the binding reactions occurring during short term (seconds) addition of PrP82-146 small oligomers (1-5-mers, flowing species) onto soluble prefibrillar PrP82-146 aggregates immobilized on the sensor surface. SPR data confirmed very efficient aggregation/elongation, consistent with the hypothesis of nucleation-dependent polymerization process. Much lower binding was observed when PrP82-146 flowed onto the scrambled sequence of PrP82-146 or onto prefibrillar Abeta42 aggregates. As previously found with Abeta40, SPR data could be adequately fitted by equations modeling the "dock-and-lock" mechanism, in which the "locking" step is due to sequential conformational changes, each increasing the affinity of the monomer for the fibril until a condition of irreversible binding is reached. However, these conformational changes (i.e. the locking steps) appear to be faster and easier with PrP82-146 than with Abeta40. Such differences suggest that PrP82-146 has a greater propensity to polymerize and greater stability of the aggregates.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16286452</PMID><DateCompleted><Year>2006</Year><Month>02</Month><Day>28</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>281</Volume><Issue>2</Issue><PubDate><Year>2006</Year><Month>Jan</Month><Day>13</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>Gerstmann-Sträussler-Scheinker disease amyloid protein polymerizes according to the "dock-and-lock" model.</ArticleTitle><Pagination><MedlinePgn>843-9</MedlinePgn></Pagination><Abstract><AbstractText>Prion protein (PrP) amyloid formation is a central feature of genetic and acquired prion diseases such as Gerstmann-Sträussler-Scheinker disease (GSS) and variant Creutzfeldt-Jakob disease. The major component of GSS amyloid is a PrP fragment spanning residues approximately 82-146, which when synthesized as a peptide, readily forms fibrils featuring GSS amyloid. The present study employed surface plasmon resonance (SPR) to characterize the binding events underlying PrP82-146 oligomerization at the first stages of fibrillization, according to evidence suggesting a pathogenic role of prefibrillar oligomers rather than mature amyloid fibrils. We followed in real time the binding reactions occurring during short term (seconds) addition of PrP82-146 small oligomers (1-5-mers, flowing species) onto soluble prefibrillar PrP82-146 aggregates immobilized on the sensor surface. SPR data confirmed very efficient aggregation/elongation, consistent with the hypothesis of nucleation-dependent polymerization process. Much lower binding was observed when PrP82-146 flowed onto the scrambled sequence of PrP82-146 or onto prefibrillar Abeta42 aggregates. As previously found with Abeta40, SPR data could be adequately fitted by equations modeling the "dock-and-lock" mechanism, in which the "locking" step is due to sequential conformational changes, each increasing the affinity of the monomer for the fibril until a condition of irreversible binding is reached. However, these conformational changes (i.e. the locking steps) appear to be faster and easier with PrP82-146 than with Abeta40. Such differences suggest that PrP82-146 has a greater propensity to polymerize and greater stability of the aggregates.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gobbi</LastName><ForeName>Marco</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Istituto di Ricerche Farmacologiche Mario Negri, Milano, Italy. Gobbi@marionegri.it</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Colombo</LastName><ForeName>Laura</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Morbin</LastName><ForeName>Michela</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Mazzoleni</LastName><ForeName>Giulia</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Accardo</LastName><ForeName>Elena</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Vanoni</LastName><ForeName>Marco</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Del Favero</LastName><ForeName>Elena</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Cantù</LastName><ForeName>Laura</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Kirschner</LastName><ForeName>Daniel A</ForeName><Initials>DA</Initials></Author><Author ValidYN="Y"><LastName>Manzoni</LastName><ForeName>Claudia</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Beeg</LastName><ForeName>Marten</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Ceci</LastName><ForeName>Paolo</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Ubezio</LastName><ForeName>Paolo</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Forloni</LastName><ForeName>Gianluigi</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Tagliavini</LastName><ForeName>Fabrizio</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Salmona</LastName><ForeName>Mario</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>11</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000682">Amyloid</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000939">Epitopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011108">Polymers</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000682" MajorTopicYN="N">Amyloid</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006224" MajorTopicYN="N">Cricetinae</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000939" MajorTopicYN="N">Epitopes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016098" MajorTopicYN="N">Gerstmann-Straussler-Scheinker Disease</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008854" MajorTopicYN="N">Microscopy, Electron</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008956" MajorTopicYN="N">Models, Chemical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011108" MajorTopicYN="N">Polymers</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011489" MajorTopicYN="N">Protein Denaturation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020349" MajorTopicYN="N">Surface Plasmon Resonance</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013499" MajorTopicYN="N">Surface Properties</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013997" MajorTopicYN="N">Time Factors</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>11</Month><Day>16</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>3</Month><Day>1</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>11</Month><Day>16</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16286452</ArticleId><ArticleId IdType="pii">M506164200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M506164200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country></list><tree><noCountry><name sortKey="Accardo, Elena" sort="Accardo, Elena" uniqKey="Accardo E" first="Elena" last="Accardo">Elena Accardo</name><name sortKey="Beeg, Marten" sort="Beeg, Marten" uniqKey="Beeg M" first="Marten" last="Beeg">Marten Beeg</name><name sortKey="Cantu, Laura" sort="Cantu, Laura" uniqKey="Cantu L" first="Laura" last="Cantù">Laura Cantù</name><name sortKey="Ceci, Paolo" sort="Ceci, Paolo" uniqKey="Ceci P" first="Paolo" last="Ceci">Paolo Ceci</name><name sortKey="Colombo, Laura" sort="Colombo, Laura" uniqKey="Colombo L" first="Laura" last="Colombo">Laura Colombo</name><name sortKey="Del Favero, Elena" sort="Del Favero, Elena" uniqKey="Del Favero E" first="Elena" last="Del Favero">Elena Del Favero</name><name sortKey="Forloni, Gianluigi" sort="Forloni, Gianluigi" uniqKey="Forloni G" first="Gianluigi" last="Forloni">Gianluigi Forloni</name><name sortKey="Kirschner, Daniel A" sort="Kirschner, Daniel A" uniqKey="Kirschner D" first="Daniel A" last="Kirschner">Daniel A. Kirschner</name><name sortKey="Manzoni, Claudia" sort="Manzoni, Claudia" uniqKey="Manzoni C" first="Claudia" last="Manzoni">Claudia Manzoni</name><name sortKey="Mazzoleni, Giulia" sort="Mazzoleni, Giulia" uniqKey="Mazzoleni G" first="Giulia" last="Mazzoleni">Giulia Mazzoleni</name><name sortKey="Morbin, Michela" sort="Morbin, Michela" uniqKey="Morbin M" first="Michela" last="Morbin">Michela Morbin</name><name sortKey="Salmona, Mario" sort="Salmona, Mario" uniqKey="Salmona M" first="Mario" last="Salmona">Mario Salmona</name><name sortKey="Tagliavini, Fabrizio" sort="Tagliavini, Fabrizio" uniqKey="Tagliavini F" first="Fabrizio" last="Tagliavini">Fabrizio Tagliavini</name><name sortKey="Ubezio, Paolo" sort="Ubezio, Paolo" uniqKey="Ubezio P" first="Paolo" last="Ubezio">Paolo Ubezio</name><name sortKey="Vanoni, Marco" sort="Vanoni, Marco" uniqKey="Vanoni M" first="Marco" last="Vanoni">Marco Vanoni</name></noCountry><country name="Italie"><noRegion><name sortKey="Gobbi, Marco" sort="Gobbi, Marco" uniqKey="Gobbi M" first="Marco" last="Gobbi">Marco Gobbi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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