ParkinsonFranceV1, Main, Exploration, bibRecord, 005A07

An Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory Materials

Identifieur interne : 005A07 ( Main/Exploration ); précédent : 005A06; suivant : 005A08

An 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 ] ; ????.

RBID : PMC:4927840

Abstract

Background: Preformed α-synuclein fibrils seed the aggregation of soluble α-synuclein in cultured cells and in vivo. This, and other findings, has kindled the idea that α-synuclein fibrils possess prion-like properties.

Objective: 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.

Methods: 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).

Results: 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.

Conclusions: 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.

Url:

DOI: 10.3233/JPD-150691
PubMed: 26639448
PubMed Central: 4927840

Affiliations:

France, Suisse, États-Unis

Le document en format XML

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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>
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La maladie de Parkinson en France (serveur d'exploration)

An Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory Materials

An Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory Materials

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