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<title lang=en>Differential analysis of glioblastoma multiforme proteome by a 2D-DIGE approach.</title>
<creator>Collet, Brigitte</creator>
<creator>Guitton, Nathalie</creator>
<creator>Saikali, Stephan</creator>
<creator>Avril, Tony</creator>
<creator>Pineau, Charles</creator>
<creator>Hamlat, Abderrahmane</creator>
<creator>Mosser, Jean</creator>
<creator>Quillien, Véronique</creator>
<contributor>Service de Biologie ; CRLCC Eugène Marquis (CRLCC)</contributor>
<contributor>Plateforme Protéomique-Biogenouest (PPB) ; Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ) - Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ) - Proteomics Core Facility (Protim) ; Université de Rennes 1 (UR1) - Plateforme Génomique Santé Biogenouest® - Plateforme Génomique Santé Biogenouest®</contributor>
<contributor>Service d'anatomie et cytologie pathologiques [Rennes] ; Université de Rennes 1 (UR1) - Hôpital Pontchaillou - CHU Pontchaillou [Rennes]</contributor>
<contributor>Institut de Génétique et Développement de Rennes (IGDR) ; Université de Rennes 1 (UR1) - IFR140 - Centre National de la Recherche Scientifique (CNRS)</contributor>
<contributor>This work was supported by PRIR grants, and was conducted with facilities of the High-Throughput Proteomics Platform Biogenouest (Rennes) and Histopathological Platform (Rennes I University).</contributor>
<description>International audience</description>
<source>ISSN: 1477-5956</source>
<source>Proteome Science</source>
<publisher>BioMed Central</publisher>
<identifier>inserm-00585020</identifier>
<identifier>http://www.hal.inserm.fr/inserm-00585020</identifier>
<identifier>http://www.hal.inserm.fr/inserm-00585020/document</identifier>
<identifier>http://www.hal.inserm.fr/inserm-00585020/file/1477-5956-9-16.pdf</identifier>
<source>http://www.hal.inserm.fr/inserm-00585020</source>
<source>Proteome Science, BioMed Central, 2011, 9 (1), pp.16. 〈10.1186/1477-5956-9-16〉</source>
<identifier>DOI : 10.1186/1477-5956-9-16</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1186/1477-5956-9-16</relation>
<identifier>PUBMED : 21470419</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/21470419</relation>
<language>en</language>
<subject>[SDV.CAN] Life Sciences [q-bio]/Cancer</subject>
<subject>[SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN]</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>UNLABELLED: ABSTRACT: BACKGROUND: Genomics, transcriptomics and proteomics of glioblastoma multiforme (GBM) have recently emerged as possible tools to discover therapeutic targets and biomarkers for new therapies including immunotherapy. It is well known that macroscopically complete surgical excision, radiotherapy and chemotherapy have therapeutic limitations to improve survival in these patients. In this study, we used a differential proteomic-based technique (2D-Difference Gel Electrophoresis) coupled with matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry to identify proteins that may serve as brain tumor antigens in new therapeutic assays. Five samples of patients presenting a GBM and five samples of microscopically normal brain tissues derived from brain epileptic surgery specimen were labeled and run in 2D-PAGE (Two-Dimensional Polyacrylamide Gel Electrophoresis) with an internal pool sample on each gel. Five gels were matched and compared with DIA (Difference In-gel Analysis) software. Differential spots were picked, in-gel digested and peptide mass fingerprints were obtained. RESULTS: From 51 protein-spots significantly up-regulated in GBM samples, mass spectrometry (MS) identified twenty-two proteins. The differential expression of a selected protein set was first validated by western-blotting, then tested on large cohorts of GBM specimens and non-tumor tissues, using immunohistochemistry and real-time RT-PCR. CONCLUSIONS: Our results confirmed the importance of previously described proteins in glioma pathology and their potential usefulness as biological markers but also revealed some new interesting targets for future therapies.</description>
<date>2011</date>
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