{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/sdrf.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/checksum.txt"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/mqpar.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/QE33640AUH.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/QE33646AUH.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/QE33664AUH.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/QE33656AUH.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/QE33682AUH.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/QE33684AUH.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/QE33676AUH.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/QE33672AUH.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/QE33662AUH.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/QE33642AUH.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/Mousebovirtsanscontadecoy.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD045388/txt_Maxquant.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["ccarapito@unistra.fr"],"submitter":["Aurélie Hirschler"],"technology_type":["Mass Spectrometry","Shotgun proteomics","Gel-based experiment"],"software":[""],"submitter_keywords":["Trail","Tenascin c","Maremo peptide mp5","Shotgun proteomics"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD045388"],"tissue":["Cell Culture"],"sample_protocol":["Protein precipitation of NT193 culture supernatant was performed according to the protocol as previously described. Briefly, after adding Sodium Lauroyl Sarcosinate (NLS) to a final concentration of 0.1% and TCA trichloroacetic acid to a final concentration of 7.5 %, proteins were precipitated on ice for 2 hours and were pelleted by centrifugation for 30 minutes at 10 000g at 4°C. Supernatant was removed and the pellet was re-suspended in cold tetrahydrofuran to wash the protein pellet. This step was repeated 2 times for 10 min at 10 000 g at 4°C. Finally, the protein pellet was resuspended in Laemmli type buffer (10 mM Tris pH 6.8, 1mM EDTA, 5% SDS, 10 glycerol). Samples were vortexed and sonicated 2 times during 5 minutes in an ice-cold bath. Concentration of all samples was determined using the DC™ Protein Assay (Bio-Rad 5000111). After addition of dithiothreitol (50 mM final concentration), 15 µg of each protein extract were heated at 95°C for 5 minutes and stacked in an in-house prepared 5% acrylamide SDS-PAGE stacking gel. Gel bands were cut, destained, reduced with 10 mM dithiothreitol, alkylated using 55 mM iodoacetamide prior to overnight digestion at 37°C using Sequencing Grade Modified Trypsin (Promega V5111). Extracted tryptic peptides (800 ng) were analyzed by nanoLC-MS/MS on a nanoUPLC system (nanoAcquityUPLC, Waters, USA) coupled to a quadrupole-Orbitrap hybrid mass spectrometer (Q-Exactive plus, Thermo Fisher). Chromatographic separation was conducted over a 79 minutes linear gradient from 1 to 35% of solvent B (0.1 % formic acid in acetonitrile) at a flow rate of 400 nL/min. A Top 10 method was used with automatic switching between MS and MS/MS modes to acquire high resolution MS/MS spectra. All samples were injected using a randomized injection sequence. To minimize carry-over, a solvent blank injection was performed after each sample."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["NanoLC-MS/MS data was interpreted to do label-free extracted ion chromatogram-based differential analysis using MaxQuant software (version 1.6.14). Peaks were assigned with the Andromeda search engine against a concatenated database containing all mouse and bovine entries extracted from UniProtKB-SwissProt (release 19-10-2020; 23 073 sequences, Taxonomy ID 10090 and 9913). No “match between runs” were done between the samples. Carbamidomethylation of cysteines was set as fixed modification whereas oxidation of methionines and protein N-terminal acetylation were defined as variable modifications. The maximum false discovery rate was 1% at peptide and protein levels with the use of a decoy strategy. Only unique mouse peptides were kept and their intensities were summed for a given protein. Non-normalized protein intensity values were exported and used for differential analysis using Prostar software (version 1.18.6). To be considered, proteins must be identified in a minimum of 4 out of 5 replicates in at least one condition. The “det quantile” imputation mode was applied for the missing values. A Limma moderated t-test was applied on the dataset to perform differential analysis. The adaptive Benjamini-Hochberg procedure was applied to adjust the p-values and FDR values under 1%. A volcano plot was generated according to the adjusted p-values cutoff below 0.05."],"omics_type":["Proteomics"],"labhead":["Christine Carapito"],"instrument_platform":[""],"labhead_affiliation":["Laboratoire de Spectrométrie de Masse Bio-Organique (LSMBO), Institut Pluridisciplinaire Hubert Curien (IPHC), UMR 7178, Université de Strasbourg, CNRS, Strasbourg, France"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["aurelie.hirschler@unistra.fr"],"publication":["Not available"],"submitter_affiliation":["LSMBO, IPHC"],"submitter_country":["France"],"additional_accession":[]},"is_claimable":false,"name":"Tenascin-C shapes TRAIL control over tumor immunity","description":"TRAIL cytotoxicity is exploited as anti-cancer therapy since many years, however incomplete knowledge is generating many obstacles. Here, we address whether the highly abundant extracellular matrix molecule tenascin-C (TNC) orchestrating an immune suppressive tumor microenvironment and binding TRAIL impacts TRAIL cytotoxicity. We used an immune competent autologous NT193 breast cancer model with a knockdown (KD) of Tnfsf10 (encoding TRAIL) and observed accelerated tumor growth marked by less apoptosis, more proliferation and less myeloid cell infiltration as seen by flow cytometry. Grafting the same Tnfsf10 KD cells into a TNC knockout host showed repressed tumor growth suggesting that TNC is involved in regulating TRAIL functions. In vitro, we saw reduced macrophage invasion and phagocytosis with conditioned medium from Tnfsf10 KD tumor cells proposing a role of TRAIL in counteracting tumor growth. We further demonstrated that TRAIL increases secretion of TGF2/3 inducing CXCR4 in macrophages. Here, we have discovered regulation of TRAIL cytotoxicity through cell plasticity orchestrated by TNC. The pro-tumorigenic effects of TNC, counteracting TRAIL cytotoxicity, entail repression of Tnfsf10 through integrin  and, abolishing TRAIL-receptor DR5 and E-cadherin expression. As the MAREMO peptide MP5 inhibits TNC actions, we determined whether targeting TNC with MP5 has an impact on TRAIL cytotoxicity. Indeed, MP5 enforces an epithelial phenotype and elevates DR5 expression thus causing sensitization to TRAIL-induced cell death. Moreover, MP5 inhibited tumor growth that was less pronounced in Tnfsf10 KD tumors suggesting MP5 to empower endogenous TRAIL cytotoxicity. Kaplan-Meier analysis demonstrated that a high TRAIL expression correlates with favorable breast and gastric cancer patient survival which is abolished when TNC levels are also high. Our results predict that tumors with lower TNC might be more responsive to therapeutic TRAIL cytotoxicity and that MP5 could be a novel tool for enhancing TRAIL 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