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 : 000102 ( Pmc/Checkpoint ); précédent : 000101; suivant : 000103

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 : PMC:4773484

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.


Url:
DOI: 10.1016/j.dib.2016.02.018
PubMed: 26958642
PubMed Central: 4773484


Affiliations:


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<p>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:
<ext-link ext-link-type="uri" xlink:href="http://" id="ir0005">10.15252/embj.201591397</ext-link>
<xref rid="bib1" ref-type="bibr">[1]</xref>
). 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
<italic>PRIDE:</italic>
PXD002256 to
<italic>PRIDE:</italic>
PXD002263 and doi:
<ext-link ext-link-type="uri" xlink:href="http://" id="ir0010">10.6019/PXD002256</ext-link>
to
<ext-link ext-link-type="uri" xlink:href="http://" id="ir0015">10.6019/PXD002263</ext-link>
.</p>
</div>
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<name sortKey="Shrivastava, A N" uniqKey="Shrivastava A">A.N. Shrivastava</name>
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<author>
<name sortKey="Redeker, V" uniqKey="Redeker V">V. Redeker</name>
</author>
<author>
<name sortKey="Fritz, N" uniqKey="Fritz N">N. Fritz</name>
</author>
<author>
<name sortKey="Pieri, L" uniqKey="Pieri L">L. Pieri</name>
</author>
<author>
<name sortKey="Almeida, L G" uniqKey="Almeida L">L.G. Almeida</name>
</author>
<author>
<name sortKey="Spolidoro, M" uniqKey="Spolidoro M">M. Spolidoro</name>
</author>
<author>
<name sortKey="Liebmann, T" uniqKey="Liebmann T">T. Liebmann</name>
</author>
<author>
<name sortKey="Bousset, L" uniqKey="Bousset L">L. Bousset</name>
</author>
<author>
<name sortKey="Renner, M" uniqKey="Renner M">M. Renner</name>
</author>
<author>
<name sortKey="Lena, C" uniqKey="Lena C">C. Léna</name>
</author>
<author>
<name sortKey="Aperia, A" uniqKey="Aperia A">A. Aperia</name>
</author>
<author>
<name sortKey="Melki, R" uniqKey="Melki R">R. Melki</name>
</author>
<author>
<name sortKey="Triller, A" uniqKey="Triller A">A. Triller</name>
</author>
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<name sortKey="Aramuni, G" uniqKey="Aramuni G">G. Aramuni</name>
</author>
<author>
<name sortKey="Hammer, R E" uniqKey="Hammer R">R.E. Hammer</name>
</author>
<author>
<name sortKey="Sudhof, T C" uniqKey="Sudhof T">T.C. Südhof</name>
</author>
<author>
<name sortKey="Missler, M" uniqKey="Missler M">M. Missler</name>
</author>
</analytic>
</biblStruct>
<biblStruct>
<analytic>
<author>
<name sortKey="Hartmann, U" uniqKey="Hartmann U">U. Hartmann</name>
</author>
<author>
<name sortKey="Maurer, P" uniqKey="Maurer P">P. Maurer</name>
</author>
</analytic>
</biblStruct>
<biblStruct>
<analytic>
<author>
<name sortKey="Siegel, D A" uniqKey="Siegel D">D.A. Siegel</name>
</author>
<author>
<name sortKey="Davies, P" uniqKey="Davies P">P. Davies</name>
</author>
<author>
<name sortKey="Dobrenis, K" uniqKey="Dobrenis K">K. Dobrenis</name>
</author>
<author>
<name sortKey="Huang, M" uniqKey="Huang M">M. Huang</name>
</author>
</analytic>
</biblStruct>
<biblStruct>
<analytic>
<author>
<name sortKey="Gonzalez Gronow, M" uniqKey="Gonzalez Gronow M">M. Gonzalez-Gronow</name>
</author>
<author>
<name sortKey="Ray, R" uniqKey="Ray R">R. Ray</name>
</author>
<author>
<name sortKey="Wang, F" uniqKey="Wang F">F. Wang</name>
</author>
<author>
<name sortKey="Pizzo, S V" uniqKey="Pizzo S">S.V. Pizzo</name>
</author>
</analytic>
</biblStruct>
</listBibl>
</div1>
</back>
</TEI>
<pmc article-type="other">
<pmc-dir>properties open_access</pmc-dir>
<front>
<journal-meta>
<journal-id journal-id-type="nlm-ta">Data Brief</journal-id>
<journal-id journal-id-type="iso-abbrev">Data Brief</journal-id>
<journal-title-group>
<journal-title>Data in Brief</journal-title>
</journal-title-group>
<issn pub-type="epub">2352-3409</issn>
<publisher>
<publisher-name>Elsevier</publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id pub-id-type="pmid">26958642</article-id>
<article-id pub-id-type="pmc">4773484</article-id>
<article-id pub-id-type="publisher-id">S2352-3409(16)30040-3</article-id>
<article-id pub-id-type="doi">10.1016/j.dib.2016.02.018</article-id>
<article-categories>
<subj-group subj-group-type="heading">
<subject>Data Article</subject>
</subj-group>
</article-categories>
<title-group>
<article-title>Data in support of the identification of neuronal and astrocyte proteins interacting with extracellularly applied oligomeric and fibrillar α-synuclein assemblies by mass spectrometry</article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname>Shrivastava</surname>
<given-names>Amulya Nidhi</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Redeker</surname>
<given-names>Virginie</given-names>
</name>
<email>Virginie.redeker@cnrs.fr</email>
<xref rid="aff0010" ref-type="aff">b</xref>
<xref rid="cor1" ref-type="corresp"></xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Fritz</surname>
<given-names>Nicolas</given-names>
</name>
<xref rid="aff0015" ref-type="aff">c</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Pieri</surname>
<given-names>Laura</given-names>
</name>
<xref rid="aff0010" ref-type="aff">b</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Almeida</surname>
<given-names>Leandro G.</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Spolidoro</surname>
<given-names>Maria</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Liebmann</surname>
<given-names>Thomas</given-names>
</name>
<xref rid="aff0015" ref-type="aff">c</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Bousset</surname>
<given-names>Luc</given-names>
</name>
<xref rid="aff0010" ref-type="aff">b</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Renner</surname>
<given-names>Marianne</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Léna</surname>
<given-names>Clément</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Aperia</surname>
<given-names>Anita</given-names>
</name>
<xref rid="aff0015" ref-type="aff">c</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Melki</surname>
<given-names>Ronald</given-names>
</name>
<xref rid="aff0010" ref-type="aff">b</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Triller</surname>
<given-names>Antoine</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
</contrib>
</contrib-group>
<aff id="aff0005">
<label>a</label>
École Normale Supérieure, Institut de Biologie de l’ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France</aff>
<aff id="aff0010">
<label>b</label>
Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France</aff>
<aff id="aff0015">
<label>c</label>
Department of Women and Children׳s Health, Karolinska Institutet, 171 76 Stockholm, Sweden</aff>
<author-notes>
<corresp id="cor1">
<label></label>
Corresponding author.
<email>Virginie.redeker@cnrs.fr</email>
</corresp>
</author-notes>
<pub-date pub-type="pmc-release">
<day>12</day>
<month>2</month>
<year>2016</year>
</pub-date>
<pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="collection">
<month>6</month>
<year>2016</year>
</pub-date>
<pub-date pub-type="epub">
<day>12</day>
<month>2</month>
<year>2016</year>
</pub-date>
<volume>7</volume>
<fpage>221</fpage>
<lpage>228</lpage>
<history>
<date date-type="received">
<day>9</day>
<month>10</month>
<year>2015</year>
</date>
<date date-type="rev-recd">
<day>8</day>
<month>12</month>
<year>2015</year>
</date>
<date date-type="accepted">
<day>4</day>
<month>2</month>
<year>2016</year>
</date>
</history>
<permissions>
<copyright-statement>© 2016 The Authors</copyright-statement>
<copyright-year>2016</copyright-year>
<license license-type="CC BY" xlink:href="http://creativecommons.org/licenses/by/4.0/">
<license-p>This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).</license-p>
</license>
</permissions>
<abstract>
<p>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:
<ext-link ext-link-type="uri" xlink:href="http://" id="ir0005">10.15252/embj.201591397</ext-link>
<xref rid="bib1" ref-type="bibr">[1]</xref>
). 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
<italic>PRIDE:</italic>
PXD002256 to
<italic>PRIDE:</italic>
PXD002263 and doi:
<ext-link ext-link-type="uri" xlink:href="http://" id="ir0010">10.6019/PXD002256</ext-link>
to
<ext-link ext-link-type="uri" xlink:href="http://" id="ir0015">10.6019/PXD002263</ext-link>
.</p>
</abstract>
<kwd-group>
<title>Keywords</title>
<kwd>Parkinson׳s disease</kwd>
<kwd>Alpha-synuclein assemblies</kwd>
<kwd>Proteomic Analysis</kwd>
<kwd>Pull down</kwd>
</kwd-group>
</article-meta>
</front>
<floats-group>
<fig id="f0005">
<label>Fig. 1</label>
<caption>
<p>Experimental strategy for proteomic identification of proteins interacting specifically with extracellularly applied oligomeric and fibrillar α-syn. Rat cortical neurons (left panel) or astrocytes (right panel) were incubated for 10 min with oligomeric or fibrillar α-syn-S-tag (at a particle concentration of 1 µM and 4.8 nM, respectively, equivalent to 40 µM monomeric α-syn). After cell lysis, fresh protein extracts from those cells were incubated with S-protein agarose beads to pull down α-syn-S-tag assemblies together with their specific protein partners. Unexposed cell extracts incubated with S-protein agarose beads were used as a control. Proteins bound to the S-protein agarose beads were subjected to trypsin digestion and subsequently identified and quantified by nanoLC-MS/MS analysis, using a nanoLC-LTQ-Orbitrap. The complete list of identified proteins is shown in
<xref rid="s0055" ref-type="fn">Supplementary Tables 1–4</xref>
. Our data mining analysis highlighted a list of interacting protein partners of oligomeric (blue frame) or fibrillar α-syn (orange frame) described as extracellularly exposed in peer-reviewed articles: in blue transmembrane proteins with extracellular domains, in green proteoglycans and in black proteins that can be secreted or extracellularly localized.</p>
</caption>
<alt-text id="at0005">Fig. 1</alt-text>
<graphic xlink:href="gr1"></graphic>
</fig>
</floats-group>
</pmc>
<affiliations>
<list>
<country>
<li>France</li>
<li>Suède</li>
</country>
<region>
<li>Île-de-France</li>
</region>
</list>
<tree>
<country name="France">
<region name="Île-de-France">
<name sortKey="Shrivastava, Amulya Nidhi" sort="Shrivastava, Amulya Nidhi" uniqKey="Shrivastava A" first="Amulya Nidhi" last="Shrivastava">Amulya Nidhi Shrivastava</name>
</region>
<name sortKey="Almeida, Leandro G" sort="Almeida, Leandro G" uniqKey="Almeida L" first="Leandro G." last="Almeida">Leandro G. Almeida</name>
<name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name>
<name sortKey="Lena, Clement" sort="Lena, Clement" uniqKey="Lena C" first="Clément" last="Léna">Clément Léna</name>
<name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name>
<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>
<country name="Suède">
<noRegion>
<name sortKey="Fritz, Nicolas" sort="Fritz, Nicolas" uniqKey="Fritz N" first="Nicolas" last="Fritz">Nicolas Fritz</name>
</noRegion>
<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>
</country>
</tree>
</affiliations>
</record>

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