{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/Controle_Rep3_20211128225604.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/EVStreated_Rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/EVStreated_Rep2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/EVStreated_Rep1_20211127112039.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/EVStreated_Rep2_20211128131750.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/EVStreated_Rep2_20211128104208.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/Controle_Rep1_20211127024857.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/Controle_Rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/Controle_Rep2_20211128021033.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/EVStreated_Rep3_20211129100319.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/Controle_Rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/EVStreated_Rep1_20211127135622.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/EVStreated_Rep3_20211129123900.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/Controle_Rep1_20211127001313.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/Controle_Rep3_20211129013147.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/Controle_Rep2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/Controle_Rep2_20211127233440.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/EVStreated_Rep1.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/andromeda.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD039279/Results.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["richard.tomasini@inserm.fr"],"submitter":["AUDEBERT Stephane"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"disease":["Pancreatic Ductal Adenocarcinoma"],"software":[""],"submitter_keywords":["Pdac","Lc-msms","Extracellular vesicles","Extracellular matrix","Matrisome"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD039279"],"tissue":["Pancreas","Epithelium Of Pancreatic Duct","Fibroblast"],"sample_protocol":["Biological sample Preparation: Small pancreatic tissue blocks were obtained during pancreatic surgery from patients with resectable pancreatic. Human primary CAFs were isolated as followed: Briefly, the tumors were cut into small pieces of 1 mm3 using a razor blade. The tissue pieces were dissociated using the Tumor Dissociation Kit (Miltenyi Biotec) according to the manufacturer’s recommendations. Cells were then resuspended, passed through a cell strainer (100 μM), and finally plated and cultured in DMEM F-12 medium (Gibco) supplemented with 10% fetal bovine serum, 1% L-glutamine, 1% antibiotic-antimycotic, and 0.5% sodium pyruvate (Gibco). Cells were then detached and passaged using StemPro accutase cell dissociation reagent (Gibco). Human primary CAFs were used between passages 4 and 9. Primary CAF features were verified by flow cytometry with a positive α-SMA and FAP staining.  For treatment with EVs, recipient cells were cultured in EVs-free media, where medium was supplemented with FBS previously ultra-centrifuged at 100,000 x g for 18 hours to remove FBS-sourced EVs.  To produce CAF-derived ECMs, Primary CAFs were plated on pre-treated cell-culture plates with 0.2% gelatin at 100% confluency, approximately 200,000 cells in a 12-well plate. Following 24 hours of plating, primary CAF medium was changed to CAF-EVs depleted medium supplemented with 50μg/mL of L-ascorbic acid (Sigma-Aldrich). Medium was refreshed every 48 hours for a total duration of 9 days, starting from the first medium change, to allow for ECM production. CAFs were treated with tumor-cell (PANC-1) derived EVs during 2 consecutive days, for a total of 4 treatments, twice during the 9-day period. Decellularization of CAF-derived ECM was performed by incubation with extraction buffer (20mM ammonium-hydroxide, 0.5% Triton-X100) for 5 minutes at 37°C and 5% CO2 until no living cells could be observed. The decellularized ECMs were washed three times with 1x PBS carefully to not dislodge the matrix from the well and subsequently prepared for proteomics analysis.   Sample processing and LC-MSMS  Proteomic analysis of decellularized ECMs was performed as described: Briefly, ECM proteins in culture wells were solubilized in 8M urea, reduced with 10mM DTT (56°C, 45mn) and alkylated with 50 mM iodoacetamide (30mn, RT). Proteins were thereafter digested with first PNGase F (1500 units/ml, 37°C, 2h, New England BioLabs), endoproteinase Lys-C (1µg/ml, 37°C, 2h, Promega) and high-sequencing-grade trypsin (2µg/ml, 37°C, 16h, Promega). Peptides were desalted on Sep-Pak C18 ligh-cartridge (Waters), dried under speed vacuum and were reconstituted with 15µl 0.1% trifluoroacetic acid in 2% acetonitrile for LC-MSMS analysis. Each biological condition were prepared in triplicates and further injected thrice for LC-MS/MS analysis using an Orbitrap Fusion Lumos Tribrid Mass Spectrometer (ThermoFisher Scientific, San Jose, CA) online with a nanoRSLC Ultimate 3000 chromatography system ThermoFisher Scientific, Sunnyvale, CA). 1µl corresponding to 7 % of the sample was injected. First, peptides were concentrated and purified on a pre-column PepMap100 C18, 2cm × 100µm I.D, 100Å pore size, 5µm particle size in solvent A (0.1% formic acid in 2% acetonitrile). In the second step, peptides were separated on a reverse phase LC EASY-Spray C18 column PepMap RSLC C18, 50cm × 75µm I.D, 100Å pore size, 2µm particle size (ThermoFisher) at 300nL/min flow rate and 40°C. After column equilibration using 4% of solvent B (20% water - 80% acetonitrile - 0.1% formic acid), peptides were eluted from the analytical column by a two-step linear gradient (2-20% acetonitrile/H2O; 0.1% formic acid for 90min and 20-45% acetonitrile/H2O; 0.1% formic acid for 20min). For peptide ionization in the EASY-Spray nanosource in front of mass spectrometer, spray voltage was set at 2.2 kV and the capillary temperature at 275 °C. The Orbitrap Lumos was used in data dependent mode to switch consistently between MS and MS/MS. Time between Masters Scans was set to 3 seconds. MS spectra were acquired with the Orbitrap in the range of m/z 400-1600 at a FWHM resolution of 120 000 measured at 400 m/z. AGC target was set at 4.0e5 with a 50 ms Maximum Injection Time. For internal mass calibration the 445.120025 ions was used as lock mass. The more abundant precursor ions were selected and collision-induced dissociation fragmentation was performed in the ion trap to have maximum sensitivity and yield a maximum amount of MS/MS data. Number of precursor ions was automatically defined along run in 3s windows using the “Inject Ions for All Available parallelizable time option” with a maximum injection time of 300 ms. The signal threshold for an MS/MS event was set to 5000 counts. Charge state screening was enabled to exclude precursors with 0 and 1 charge states. Dynamic exclusion was enabled with a repeat count of 1 and duration of 60 s."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Relative intensity-based label-free quantification (LFQ) was processed using the MaxLFQ algorithm from the freely available MaxQuant computational proteomics platform, version 1.6.3.4. Spectra were searched against the Human database extracted from UniProt on the 24th of April 2021 and containing 20395 entries (reviewed). The following parameters were used for searches: (i) trypsin allowing cleavage before proline; (ii) two missed cleavages were allowed; (ii) monoisotopic precursor tolerance of 20 ppm in the first search used for recalibration, followed by 4.5 ppm for the main search and 0.5 Da for fragment ions from MS/MS ; (iii) cysteine carbamidomethylation (+57.02146) as a fixed modification and methionine, proline oxidation (+15.99491), asparagine deamination  (+0.984016) and N-terminal acetylation (+42.0106) as variable modifications; (iv) a maximum of five modifications per peptide allowed; and (v) minimum peptide length was 7 amino acids and a maximum mass of 4,600 Da. The match between runs option was enabled to transfer identifications across different LC-MS/MS replicates based on their masses and retention time within a match time window of 0.7 min and using an alignment time window of 20 min. The quantification was performed using a minimum ratio count of 1 (unique+razor) and the second peptide option to allow identification of two co-fragmented co-eluting peptides with similar masses. The false discovery rate (FDR) at the peptide and protein levels were set to 1% and determined by searching a reverse database. For protein grouping, all proteins that cannot be distinguished based on their identified peptides were assembled into a single entry according to the MaxQuant rules.  The statistical analysis was done with Perseus program (version 1.6.15.0) from the MaxQuant environment (www.maxquant.org). Quantifiable proteins were defined as those detected in above 70% of samples in one condition or more. Protein LFQ normalized intensities were base 2 logarithmized to obtain a normal distribution. Missing values were replaced using data imputation by randomly selecting from a normal distribution centered on the lower edge of the intensity values that simulates signals of low abundant proteins using default parameters (a downshift of 1.8 standard deviation and a width of 0.3 of the original distribution). To determine whether a given detected protein was specifically differential, a two-sample t-test was done using permutation-based FDR-controlled at 0.05 and employing 250 permutations. The p value was adjusted using a scaling factor s0 with a value of 1. Analysis was done on biological triplicates, each injected three times on mass spectrometers."],"omics_type":["Proteomics"],"labhead":["Richard Tomasini, PhD"],"instrument_platform":[""],"labhead_affiliation":["INSERM U1068/UMR7258 CNRS - Cancer Research Center of Marseille \"Pancreatic Cancer\" Team Group leader of the \"Microenvironment and inter-cellular dialogue\" Parc Scientifique de Luminy, 163 avenue de Luminy, case 915, 13288 Marseille Cedex 9 FRANCE"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["stephane.audebert@inserm.fr"],"publication":["Not available"],"submitter_affiliation":["Marseille Proteomic, Centre de Recherche en Cancérologie de Marseille, Inserm UMR1068, CNRS UMR7258, Aix Marseille Université U105, Institut Paoli Calmettes, 27 Boulevard Leï Roure CS30059 13273 Marseille Cedex 09 France"],"submitter_country":["France"],"additional_accession":[]},"is_claimable":false,"name":"The impact of tumor cell-derived extracellular vesicles on primary PDAC cancer-associated fibroblast matrisomes","description":"To investigate the impact of tumor-cell derived extracellular vesicles (EVs) on cancer-associated fibroblasts (CAFs) secretory phenotypes, CAFs were treated with pancreatic cancer cell line-derived EVs and produced extracellular matrices (ECM). ECMs denuded of cells were analyzed by mass 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