PXD005420

PXD005420 is an original dataset announced via ProteomeXchange.

Title	Ovarian serous cancer tumor microenvironment investigated by MALDI MSI associated to Top-down microproteomic: Evidence of a hidden proteome as novel potential target
Description	Top-down tissue microproteomic was performed in order to investigate tumoral tissue microenvironment. 289 proteins with post-translational modifications have been isolated from biospies including Tumor, Borderline and healthy regions of serous ovarian cancers. Tumor tissue displays a majority of proteins from the nucleus and extracellular vesicles. By contrast proteins identified in the healthy tissue or bordeline are related to cellular trafficking and membranes. Global subnetwork analyses confirmed that tumor pathways displayed proteins involved in neoplasm, autophagy, apoptosis, cell proliferation, tumor immunity whereas in healthy tissue pathways are mainly in cell survival, growth, motion, adhesion, differentiation and vascularization. Interestingly, truncated proteins are in majority observed in tumor region reflecting a high level expression of enzymes in this region. Besides the reference proteome, a deeper analysis of the hidden proteome issued from Alternative ORF, led a total of 14 alternative proteins identified i.e. Six Altprot from healthy tissues, 4 from borderline tissues and 4 from tumors. Expression of one of the 4 tumoral alternative protein, AltGNL1 which is translated from an AltORF nested within the GNL1 canonical coding sequence have been performed. Co-expression of annotated and alternative proteins from the same gene, was realized by transfection in HEK 293 and HeLa cells with an expression plasmid containing a GNL1-Flag(V5) construct. Western blot and immunofluorescence experiments with an anti-FLAG confirmed that AltGNL1 is constitutively co-expressed with GNL1. AltGNL1 displays a nuclear localization whereas GNL1 is present in the cytosol. Thus were report here for the first time the co-localization of two proteomes: the one issued from the kozak code and the one from Alternative ORF, so called the Hidden Proteome.
HostingRepository	PRIDE
AnnounceDate	2017-06-23
AnnouncementXML	Submission_2017-06-23_00:35:14.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Julien Franck
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	phosphorylated residue; monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2016-11-22 05:50:48	ID requested
⏵ 1	2017-06-23 00:35:16	announced

Delcourt V, Franck J, Leblanc E, Narducci F, Robin YM, Gimeno JP, Quanico J, Wisztorski M, Kobeissy F, Jacques JF, Roucou X, Salzet M, Fournier I, Combined Mass Spectrometry Imaging and Top-down Microproteomics Reveals Evidence of a Hidden Proteome in Ovarian Cancer. EBioMedicine, 21():55-64(2017) [pubmed]

curator keyword: Biomedical

submitter keyword: Top Down micro-proteomics, MALDI Imaging, Alternative Proteins

Michel Salzet
contact affiliation	Laboratoire Protéomique, Réponse Inflammatoire et Spectrométrie de Masse (PRISM) - INSERM U1192 - Université Lille 1, Bât SN3, 1er étage, Cité Scientifique, F-59655 Villeneuve d’Ascq Cedex
contact email	michel.salzet@univ-lille1.fr
lab head
Julien Franck
contact affiliation	PRISM-INSERM U1192
contact email	julien.franck@univ-lille1.fr
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2017/06/PXD005420

PRIDE project URI

• PRIDE
  1. PXD005420
     1. Label: PRIDE project
     2. Name: Ovarian serous cancer tumor microenvironment investigated by MALDI MSI associated to Top-down microproteomic: Evidence of a hidden proteome as novel potential target