MALDI Imaging of Formalin-Fixed Paraffin-Embedded Tissues: Application to Model Animals of Parkinson Disease for Biomarker Hunting.
Identifieur interne : 000650 ( Hal/Corpus ); précédent : 000649; suivant : 000651MALDI Imaging of Formalin-Fixed Paraffin-Embedded Tissues: Application to Model Animals of Parkinson Disease for Biomarker Hunting.
Auteurs : J. Stauber ; R. Lemaire ; M. Wisztorski ; Julien Franck ; Bonnel David ; R. Day ; I. Fournier ; M. SalzetSource :
- Journal of Proteome Research [ 1535-3893 ] ; 2008-03-07.
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Abstract
A common technique for the long-term storage of tissues in hospitals and clinical laboratories is preservation in formalin-fixed paraffin-embedded (FFPE) blocks. Such tissues stored for more than five years have not been useful for proteomic studies focused on biomarker discovery. Recently, MS-based proteomic analyses of FFPE showed positive results on blocks stored for less than 2 days. However, most samples are stored for more than one year, and thus our objective was to establish a novel strategy using as a model system 6-hydroxydopamine (6-OHDA) treated rat brain tissues stored in FFPE blocks for more than 9 years. We examined MALDI tissue profiling combining the use of automatic spotting of the MALDI matrix with in situ tissue enzymatic digestion. On adjacent sections, the identification of compounds is carried out by tissue digestion followed by nanoLC/MS-MS analysis. The combination of these approaches provides MALDI direct analysis, MALDI/MS imaging, as well as the localization of a large number of proteins. This method is validated since the analyses confirmed that ubiquitin, trans-elongation factor 1, hexokinase, and the Neurofilament M are down-regulated as previously shown in human or Parkinson animal models. In contrast, peroxidoredoxin 6, F1 ATPase, and alpha-enolase are up-regulated. In addition, we uncovered three novel putative biomarkers, the trans-elongation factor 1 (eEF1) and the collapsin response mediator 1 and 2 from protein libraries. Finally, we validate the CRMP-2 protein using immunocytochemistry and MALDI imaging based on the different ions from trypsic digestion of the protein. The access to archived FFPE tissue using MALDI profiling and imaging opens a whole new area in clinical studies and biomarker discovery from hospital biopsy libraries
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Stauber</name><affiliation><hal:affiliation type="laboratory" xml:id="struct-1186" status="VALID"> <orgName>Neuroimmunologie des annélides</orgName> <orgName type="acronym">NA</orgName> <desc> <address> <addrLine>Bat. 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Lemaire</name><affiliation><hal:affiliation type="laboratory" xml:id="struct-1186" status="VALID"> <orgName>Neuroimmunologie des annélides</orgName> <orgName type="acronym">NA</orgName> <desc> <address> <addrLine>Bat. 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Day</name><affiliation><hal:affiliation type="laboratory" xml:id="struct-42330" status="INCOMING"> <orgName>Département de Pharmacologie</orgName> <desc> <address> <country key="CA"></country> </address> </desc> <listRelation> <relation active="#struct-310318" type="direct"></relation> </listRelation><tutelles><tutelle active="#struct-310318" type="direct"><org type="institution" xml:id="struct-310318" status="INCOMING"> <orgName>sherbrooke</orgName> <desc> <address> <country key="CA"></country> </address> </desc></org></tutelle></tutelles></hal:affiliation></affiliation></author><author><name sortKey="Fournier, I" sort="Fournier, I" uniqKey="Fournier I" first="I." last="Fournier">I. Fournier</name><affiliation><hal:affiliation type="laboratory" xml:id="struct-1186" status="VALID"> <orgName>Neuroimmunologie des annélides</orgName> <orgName type="acronym">NA</orgName> <desc> <address> <addrLine>Bat. SN3 59655 VILLENEUVE D ASCQ CEDEX</addrLine> <country key="FR"></country> </address> <ref type="url">http://www.univ-lille1.fr/lea/</ref> </desc> <listRelation> <relation name="UMR8017" active="#struct-441569" type="direct"></relation> <relation active="#struct-92973" type="direct"></relation> </listRelation><tutelles><tutelle name="UMR8017" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"><idno type="IdRef">02636817X</idno><idno type="ISNI">0000000122597504</idno><orgName>Centre National de la Recherche Scientifique</orgName><orgName type="acronym">CNRS</orgName><date type="start">1939-10-19</date><desc><address><country key="FR"></country></address><ref type="url">http://www.cnrs.fr/</ref></desc></org></tutelle><tutelle active="#struct-92973" type="direct"><org type="institution" xml:id="struct-92973" status="VALID"> <idno type="IdRef">026404184</idno> <orgName>Université de Lille, Sciences et Technologies</orgName> <desc> <address> <addrLine>Cité Scientifique - 59655 Villeneuve d'Ascq Cedex</addrLine> <country key="FR"></country> </address> <ref type="url">http://www.univ-lille1.fr/</ref> </desc></org></tutelle></tutelles></hal:affiliation></affiliation></author><author><name sortKey="Salzet, M" sort="Salzet, M" uniqKey="Salzet M" first="M." last="Salzet">M. Salzet</name><affiliation><hal:affiliation type="laboratory" xml:id="struct-1186" status="VALID"> <orgName>Neuroimmunologie des annélides</orgName> <orgName type="acronym">NA</orgName> <desc> <address> <addrLine>Bat. SN3 59655 VILLENEUVE D ASCQ CEDEX</addrLine> <country key="FR"></country> </address> <ref type="url">http://www.univ-lille1.fr/lea/</ref> </desc> <listRelation> <relation name="UMR8017" active="#struct-441569" type="direct"></relation> <relation active="#struct-92973" type="direct"></relation> </listRelation><tutelles><tutelle name="UMR8017" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"><idno type="IdRef">02636817X</idno><idno type="ISNI">0000000122597504</idno><orgName>Centre National de la Recherche Scientifique</orgName><orgName type="acronym">CNRS</orgName><date type="start">1939-10-19</date><desc><address><country key="FR"></country></address><ref type="url">http://www.cnrs.fr/</ref></desc></org></tutelle><tutelle active="#struct-92973" type="direct"><org type="institution" xml:id="struct-92973" status="VALID"> <idno type="IdRef">026404184</idno> <orgName>Université de Lille, Sciences et Technologies</orgName> <desc> <address> <addrLine>Cité Scientifique - 59655 Villeneuve d'Ascq Cedex</addrLine> <country key="FR"></country> </address> <ref type="url">http://www.univ-lille1.fr/</ref> </desc></org></tutelle></tutelles></hal:affiliation></affiliation></author></analytic><series><title level="j">Journal of Proteome Research</title><idno type="ISSN">1535-3893</idno><imprint><date type="datePub">2008-03-07</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="mix" xml:lang="en"><term>CRMP2</term><term>FFPE tissues</term><term>MALDI IMAGING</term><term>Parkinson</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A common technique for the long-term storage of tissues in hospitals and clinical laboratories is preservation in formalin-fixed paraffin-embedded (FFPE) blocks. Such tissues stored for more than five years have not been useful for proteomic studies focused on biomarker discovery. Recently, MS-based proteomic analyses of FFPE showed positive results on blocks stored for less than 2 days. However, most samples are stored for more than one year, and thus our objective was to establish a novel strategy using as a model system 6-hydroxydopamine (6-OHDA) treated rat brain tissues stored in FFPE blocks for more than 9 years. We examined MALDI tissue profiling combining the use of automatic spotting of the MALDI matrix with in situ tissue enzymatic digestion. On adjacent sections, the identification of compounds is carried out by tissue digestion followed by nanoLC/MS-MS analysis. The combination of these approaches provides MALDI direct analysis, MALDI/MS imaging, as well as the localization of a large number of proteins. This method is validated since the analyses confirmed that ubiquitin, trans-elongation factor 1, hexokinase, and the Neurofilament M are down-regulated as previously shown in human or Parkinson animal models. In contrast, peroxidoredoxin 6, F1 ATPase, and alpha-enolase are up-regulated. In addition, we uncovered three novel putative biomarkers, the trans-elongation factor 1 (eEF1) and the collapsin response mediator 1 and 2 from protein libraries. Finally, we validate the CRMP-2 protein using immunocytochemistry and MALDI imaging based on the different ions from trypsic digestion of the protein. The access to archived FFPE tissue using MALDI profiling and imaging opens a whole new area in clinical studies and biomarker discovery from hospital biopsy libraries</div></front></TEI><hal api="V3"> <titleStmt> <title xml:lang="en">MALDI Imaging of Formalin-Fixed Paraffin-Embedded Tissues: Application to Model Animals of Parkinson Disease for Biomarker Hunting.</title> <author role="aut"> <persName> <forename type="first">J.</forename> <surname>Stauber</surname> </persName> <idno type="halauthorid">114325</idno> <affiliation ref="#struct-1186"></affiliation> </author> <author role="aut"> <persName> <forename type="first">R.</forename> <surname>Lemaire</surname> </persName> <idno type="halauthorid">65359</idno> <affiliation ref="#struct-1186"></affiliation> </author> <author role="aut"> <persName> <forename type="first">M.</forename> <surname>Wisztorski</surname> </persName> <idno type="halauthorid">114245</idno> <affiliation ref="#struct-1186"></affiliation> </author> <author role="aut"> <persName> <forename type="first">Julien</forename> <surname>Franck</surname> </persName> <idno type="halauthorid">298800</idno> <affiliation ref="#struct-1186"></affiliation> </author> <author role="aut"> <persName> <forename type="first">Bonnel</forename> <surname>David</surname> </persName> <idno type="halauthorid">298801</idno> <affiliation ref="#struct-1186"></affiliation> </author> <author role="aut"> <persName> <forename type="first">R.</forename> <surname>Day</surname> </persName> <idno type="halauthorid">114248</idno> <affiliation ref="#struct-42330"></affiliation> </author> <author role="crp"> <persName> <forename type="first">I.</forename> <surname>Fournier</surname> </persName> <email type="md5">7ab1cba323f595686a437c92955abec8</email> <email type="domain">univ-lille1.fr</email> <idno type="halauthorid">114258</idno> <affiliation ref="#struct-1186"></affiliation> </author> <author role="crp"> <persName> <forename type="first">M.</forename> <surname>Salzet</surname> </persName> <email type="md5">c9f0db3fec949fa0a801669d02ec93d8</email> <email type="domain">univ-lille1.fr</email> <idno type="halauthorid">114322</idno> <affiliation ref="#struct-1186"></affiliation> </author> <editor role="depositor"> <persName> <forename>Michel</forename> <surname>Salzet</surname> </persName> <email type="md5">89023f216956010e2268e4fec1f582ee</email> <email type="domain">wanadoo.fr</email> </editor> <funder>ANR, INCA</funder> </titleStmt> <editionStmt> <edition n="v1" type="current"> <date type="whenSubmitted">2008-04-09 18:28:38</date> <date type="whenModified">2008-04-09 20:51:38</date> <date type="whenReleased">2008-04-09 20:51:38</date> <date type="whenProduced">2008-03-07</date> <date type="whenEndEmbargoed">2008-04-09</date> <ref type="file" target="https://hal.archives-ouvertes.fr/hal-00268379/document"> <date notBefore="2008-04-09"></date> </ref> <ref type="file" subtype="author" n="1" target="https://hal.archives-ouvertes.fr/hal-00268379/file/Founier.pdf"> <date notBefore="2008-04-09"></date> </ref> </edition> <respStmt> <resp>contributor</resp> <name key="111725"> <persName> <forename>Michel</forename> <surname>Salzet</surname> </persName> <email type="md5">89023f216956010e2268e4fec1f582ee</email> <email type="domain">wanadoo.fr</email> </name> </respStmt> </editionStmt> <publicationStmt> <distributor>CCSD</distributor> <idno type="halId">hal-00268379</idno> <idno type="halUri">https://hal.archives-ouvertes.fr/hal-00268379</idno> <idno type="halBibtex">stauber:hal-00268379</idno> <idno type="halRefHtml">Journal of Proteome Research, American Chemical Society, 2008, 7 (7), pp.969-978</idno> <idno type="halRef">Journal of Proteome Research, American Chemical Society, 2008, 7 (7), pp.969-978</idno> </publicationStmt> <seriesStmt> <idno type="stamp" n="CNRS">CNRS - Centre national de la recherche scientifique</idno> <idno type="stamp" n="UNIV-LILLE1">Université des Sciences et Technologie de Lille - Lille I</idno> </seriesStmt> <notesStmt> <note type="audience" n="2">International</note> <note type="popular" n="0">No</note> <note type="peer" n="1">Yes</note> </notesStmt> <sourceDesc> <biblStruct> <analytic> <title xml:lang="en">MALDI Imaging of Formalin-Fixed Paraffin-Embedded Tissues: Application to Model Animals of Parkinson Disease for Biomarker Hunting.</title> <author role="aut"> <persName> <forename type="first">J.</forename> <surname>Stauber</surname> </persName> <idno type="halauthorid">114325</idno> <affiliation ref="#struct-1186"></affiliation> </author> <author role="aut"> <persName> <forename type="first">R.</forename> <surname>Lemaire</surname> </persName> <idno type="halauthorid">65359</idno> <affiliation ref="#struct-1186"></affiliation> </author> <author role="aut"> <persName> <forename type="first">M.</forename> <surname>Wisztorski</surname> </persName> <idno type="halauthorid">114245</idno> <affiliation ref="#struct-1186"></affiliation> </author> <author role="aut"> <persName> <forename type="first">Julien</forename> <surname>Franck</surname> </persName> <idno type="halauthorid">298800</idno> <affiliation ref="#struct-1186"></affiliation> </author> <author role="aut"> <persName> <forename type="first">Bonnel</forename> <surname>David</surname> </persName> <idno type="halauthorid">298801</idno> <affiliation ref="#struct-1186"></affiliation> </author> <author role="aut"> <persName> <forename type="first">R.</forename> <surname>Day</surname> </persName> <idno type="halauthorid">114248</idno> <affiliation ref="#struct-42330"></affiliation> </author> <author role="crp"> <persName> <forename type="first">I.</forename> <surname>Fournier</surname> </persName> <email type="md5">7ab1cba323f595686a437c92955abec8</email> <email type="domain">univ-lille1.fr</email> <idno type="halauthorid">114258</idno> <affiliation ref="#struct-1186"></affiliation> </author> <author role="crp"> <persName> <forename type="first">M.</forename> <surname>Salzet</surname> </persName> <email type="md5">c9f0db3fec949fa0a801669d02ec93d8</email> <email type="domain">univ-lille1.fr</email> <idno type="halauthorid">114322</idno> <affiliation ref="#struct-1186"></affiliation> </author> </analytic> <monogr> <idno type="halJournalId" status="VALID">16093</idno> <idno type="issn">1535-3893</idno> <idno type="eissn">1535-3907</idno> <title level="j">Journal of Proteome Research</title> <imprint> <publisher>American Chemical Society</publisher> <biblScope unit="volume">7</biblScope> <biblScope unit="issue">7</biblScope> <biblScope unit="pp">969-978</biblScope> <date type="datePub">2008-03-07</date> </imprint> </monogr> <idno type="pubmed">18247558</idno> </biblStruct> </sourceDesc> <profileDesc> <langUsage> <language ident="en">English</language> </langUsage> <textClass> <keywords scheme="author"> <term xml:lang="en">Parkinson</term> <term xml:lang="en">FFPE tissues</term> <term xml:lang="en">MALDI IMAGING</term> <term xml:lang="en">CRMP2</term> </keywords> <classCode scheme="mesh">Proteomics Maldi Imaging mass spectrometry</classCode> <classCode scheme="halDomain" n="sdv.neu.nb">Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology</classCode> <classCode scheme="halDomain" n="chim.anal">Chemical Sciences/Analytical chemistry</classCode> <classCode scheme="halTypology" n="ART">Journal articles</classCode> </textClass> <abstract xml:lang="en">A common technique for the long-term storage of tissues in hospitals and clinical laboratories is preservation in formalin-fixed paraffin-embedded (FFPE) blocks. Such tissues stored for more than five years have not been useful for proteomic studies focused on biomarker discovery. Recently, MS-based proteomic analyses of FFPE showed positive results on blocks stored for less than 2 days. However, most samples are stored for more than one year, and thus our objective was to establish a novel strategy using as a model system 6-hydroxydopamine (6-OHDA) treated rat brain tissues stored in FFPE blocks for more than 9 years. We examined MALDI tissue profiling combining the use of automatic spotting of the MALDI matrix with in situ tissue enzymatic digestion. On adjacent sections, the identification of compounds is carried out by tissue digestion followed by nanoLC/MS-MS analysis. The combination of these approaches provides MALDI direct analysis, MALDI/MS imaging, as well as the localization of a large number of proteins. This method is validated since the analyses confirmed that ubiquitin, trans-elongation factor 1, hexokinase, and the Neurofilament M are down-regulated as previously shown in human or Parkinson animal models. In contrast, peroxidoredoxin 6, F1 ATPase, and alpha-enolase are up-regulated. In addition, we uncovered three novel putative biomarkers, the trans-elongation factor 1 (eEF1) and the collapsin response mediator 1 and 2 from protein libraries. Finally, we validate the CRMP-2 protein using immunocytochemistry and MALDI imaging based on the different ions from trypsic digestion of the protein. The access to archived FFPE tissue using MALDI profiling and imaging opens a whole new area in clinical studies and biomarker discovery from hospital biopsy libraries</abstract> </profileDesc> </hal></record>Pour manipuler ce document sous Unix (Dilib)
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