An Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory Materials
Identifieur interne : 005A07 ( Main/Exploration ); précédent : 005A06; suivant : 005A08An Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory Materials
Auteurs : Luc Bousset [France] ; Patrik Brundin [États-Unis] ; Anja Böckmann [France] ; Beat Meier [Suisse] ; Ronald Melki [France]Source :
- Journal of Parkinson's Disease [ 1877-7171 ] ; ????.
Abstract
Url:
DOI: 10.3233/JPD-150691
PubMed: 26639448
PubMed Central: 4927840
Affiliations:
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Le document en format XML
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<author><name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name>
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<country xml:lang="fr">France</country>
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<author><name sortKey="Brundin, Patrik" sort="Brundin, Patrik" uniqKey="Brundin P" first="Patrik" last="Brundin">Patrik Brundin</name>
<affiliation wicri:level="1"><nlm:aff id="aff2"> Van Andel Research Institute,<institution>Center for Neurodegenerative Science</institution>
, Grand Rapids, Michigan,<country>USA</country>
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<country xml:lang="fr">États-Unis</country>
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<author><name sortKey="Bockmann, Anja" sort="Bockmann, Anja" uniqKey="Bockmann A" first="Anja" last="Böckmann">Anja Böckmann</name>
<affiliation wicri:level="1"><nlm:aff id="aff3">Institut de Biologie et Chimie des Proteines,<institution>CNRS/Université de Lyon 1</institution>
, Lyon,<country>France</country>
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<country xml:lang="fr">France</country>
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<author><name sortKey="Meier, Beat" sort="Meier, Beat" uniqKey="Meier B" first="Beat" last="Meier">Beat Meier</name>
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<country xml:lang="fr">Suisse</country>
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<author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">An Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory Materials</title>
<author><name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name>
<affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Paris-Saclay Institute of Neurosciences</institution>
, CNRS, Gif-sur-Yvette,<country>France</country>
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<country xml:lang="fr">France</country>
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<author><name sortKey="Brundin, Patrik" sort="Brundin, Patrik" uniqKey="Brundin P" first="Patrik" last="Brundin">Patrik Brundin</name>
<affiliation wicri:level="1"><nlm:aff id="aff2"> Van Andel Research Institute,<institution>Center for Neurodegenerative Science</institution>
, Grand Rapids, Michigan,<country>USA</country>
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<country xml:lang="fr">États-Unis</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<author><name sortKey="Bockmann, Anja" sort="Bockmann, Anja" uniqKey="Bockmann A" first="Anja" last="Böckmann">Anja Böckmann</name>
<affiliation wicri:level="1"><nlm:aff id="aff3">Institut de Biologie et Chimie des Proteines,<institution>CNRS/Université de Lyon 1</institution>
, Lyon,<country>France</country>
</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<author><name sortKey="Meier, Beat" sort="Meier, Beat" uniqKey="Meier B" first="Beat" last="Meier">Beat Meier</name>
<affiliation wicri:level="1"><nlm:aff id="aff4"><institution>Physical Chemistry</institution>
, ETH Zurich, Zurich,<country>Switzerland</country>
</nlm:aff>
<country xml:lang="fr">Suisse</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name>
<affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Paris-Saclay Institute of Neurosciences</institution>
, CNRS, Gif-sur-Yvette,<country>France</country>
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<country xml:lang="fr">France</country>
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<series><title level="j">Journal of Parkinson's Disease</title>
<idno type="ISSN">1877-7171</idno>
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<front><div type="abstract" xml:lang="en"><p><bold>Background:</bold>
Preformed α-synuclein fibrils seed the aggregation of soluble α-synuclein in cultured cells and <italic>in vivo</italic>
. This, and other findings, has kindled the idea that α-synuclein fibrils possess prion-like properties.</p>
<p><bold>Objective:</bold>
As α-synuclein fibrils should not be considered as innocuous, there is a need for decontamination and inactivation procedures for laboratory benches and non-disposable laboratory material.</p>
<p><bold>Methods:</bold>
We assessed the effectiveness of different procedures designed to disassemble α-synuclein fibrils and reduce their infectivity. We examined different commercially available detergents to remove α-synuclein assemblies adsorbed on materials that are not disposable and that are most found in laboratories (e.g. plastic, glass, aluminum or stainless steel surfaces).</p>
<p><bold>Results:</bold>
We show that methods designed to decrease PrP prion infectivity neither effectively remove α-synuclein assemblies adsorbed to different materials commonly used in the laboratory nor disassemble the fibrillar form of the protein with efficiency. In contrast, both commercial detergents and SDS detached α-synuclein assemblies from contaminated surfaces and disassembled the fibrils.</p>
<p><bold>Conclusions:</bold>
We describe three cleaning procedures that effectively remove and disassemble α-synuclein seeds. The methods rely on the use of detergents that are compatible with most non-disposable tools in a laboratory. The procedures are easy to implement and significantly decrease any potential risks associated to handling α-synuclein assemblies.</p>
</div>
</front>
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