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

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Data in support of the identification of neuronal and astrocyte proteins interacting with extracellularly applied oligomeric and fibrillar α-synuclein assemblies by mass spectrometry.

Identifieur interne : 000177 ( PubMed/Checkpoint ); précédent : 000176; suivant : 000178

Data in support of the identification of neuronal and astrocyte proteins interacting with extracellularly applied oligomeric and fibrillar α-synuclein assemblies by mass spectrometry.

Auteurs : Amulya Nidhi Shrivastava [France] ; Virginie Redeker [France] ; Nicolas Fritz [Suède] ; Laura Pieri [France] ; Leandro G. Almeida [France] ; Maria Spolidoro [France] ; Thomas Liebmann [Suède] ; Luc Bousset [France] ; Marianne Renner [France] ; Clément Léna [France] ; Anita Aperia [Suède] ; Ronald Melki [France] ; Antoine Triller [France]

Source :

RBID : pubmed:26958642

Abstract

α-Synuclein (α-syn) is the principal component of Lewy bodies, the pathophysiological hallmark of individuals affected by Parkinson disease (PD). This neuropathologic form of α-syn contributes to PD progression and propagation of α-syn assemblies between neurons. The data we present here support the proteomic analysis used to identify neuronal proteins that specifically interact with extracellularly applied oligomeric or fibrillar α-syn assemblies (conditions 1 and 2, respectively) (doi: 10.15252/embj.201591397[1]). α-syn assemblies and their cellular partner proteins were pulled down from neuronal cell lysed shortly after exposure to exogenous α-syn assemblies and the associated proteins were identified by mass spectrometry using a shotgun proteomic-based approach. We also performed experiments on pure cultures of astrocytes to identify astrocyte-specific proteins interacting with oligomeric or fibrillar α-syn (conditions 3 and 4, respectively). For each condition, proteins interacting selectively with α-syn assemblies were identified by comparison to proteins pulled-down from untreated cells used as controls. The mass spectrometry data, the database search and the peak lists have been deposited to the ProteomeXchange Consortium database via the PRIDE partner repository with the dataset identifiers PRIDE: PXD002256 to PRIDE: PXD002263 and doi: 10.6019/PXD002256 to 10.6019/PXD002263.

DOI: 10.1016/j.dib.2016.02.018
PubMed: 26958642


Affiliations:


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<Affiliation>Department of Women and Children׳s Health, Karolinska Institutet, 171 76 Stockholm, Sweden.</Affiliation>
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<Affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France.</Affiliation>
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<Affiliation>Department of Women and Children׳s Health, Karolinska Institutet, 171 76 Stockholm, Sweden.</Affiliation>
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<Affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France.</Affiliation>
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<name sortKey="Shrivastava, Amulya Nidhi" sort="Shrivastava, Amulya Nidhi" uniqKey="Shrivastava A" first="Amulya Nidhi" last="Shrivastava">Amulya Nidhi Shrivastava</name>
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<name sortKey="Pieri, Laura" sort="Pieri, Laura" uniqKey="Pieri L" first="Laura" last="Pieri">Laura Pieri</name>
<name sortKey="Redeker, Virginie" sort="Redeker, Virginie" uniqKey="Redeker V" first="Virginie" last="Redeker">Virginie Redeker</name>
<name sortKey="Renner, Marianne" sort="Renner, Marianne" uniqKey="Renner M" first="Marianne" last="Renner">Marianne Renner</name>
<name sortKey="Spolidoro, Maria" sort="Spolidoro, Maria" uniqKey="Spolidoro M" first="Maria" last="Spolidoro">Maria Spolidoro</name>
<name sortKey="Triller, Antoine" sort="Triller, Antoine" uniqKey="Triller A" first="Antoine" last="Triller">Antoine Triller</name>
</country>
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<name sortKey="Fritz, Nicolas" sort="Fritz, Nicolas" uniqKey="Fritz N" first="Nicolas" last="Fritz">Nicolas Fritz</name>
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<name sortKey="Aperia, Anita" sort="Aperia, Anita" uniqKey="Aperia A" first="Anita" last="Aperia">Anita Aperia</name>
<name sortKey="Liebmann, Thomas" sort="Liebmann, Thomas" uniqKey="Liebmann T" first="Thomas" last="Liebmann">Thomas Liebmann</name>
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