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

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• 作者：Amulya Nidhi Shrivastava^a ; Virginie Redeker^b ; ^{Virginie.redeker@cnrs.fr" class="auth_mail" title="E-mail the corresponding author} ; Nicolas Fritz^c ; Laura Pieri^b ; Leandro G. Almeida^a ; Maria Spolidoro^a ; Thomas Liebmann^c ; Luc Bousset^b ; Marianne Renner^a ; Clé ; ment Lé ; na^a ; Anita Aperia^c ; Ronald Melki^b ; Antoine Triller^a
• 关键词：Parkinson׳s disease ; Alpha-synuclein assemblies ; Proteomic Analysis ; Pull down
• 刊名：Data in Brief
• 出版年：2016
• 出版时间：June 2016
• 年：2016
• 卷：7
• 期：Complete
• 页码：221-228
• 全文大小：957 K

文摘

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:2256">http://www.ebi.ac.uk/pride/archive/projects/PXD002256 to PRIDE:http://www.ebi.ac.uk/pride/archive/projects/PXD002263 and doi: 10.6019/2256">http://www.ebi.ac.uk/pride/archive/projects/PXD002256 to 10.6019/http://www.ebi.ac.uk/pride/archive/projects/PXD002263.