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Core Facility"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"disease":["Colon Cancer"],"software":[""],"submitter_keywords":["Tumor microenvironment","Proteomics","Colorectal cancer","Biomarkers","Extracellular vesicles","Interstitial vesicles","Exosomes"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD033236"],"tissue":["Colon"],"sample_protocol":["Protein digestion, peptide labeling, and fractionation In total, 10 mucosa and 10 tumor tissue samples from 10 patients were used for the proteomic analysis (Figure 1). The paired samples from patient 1-5 and patient 6-11 were analysed in two separate and independent TMT-studies, study 1 (February 2018) and the confirmative Study 2 (October 2018), respectively. A representative and identical reference pool were analysed in both study. The reference pool was made up of equal parts from all 10 samples in study 1. The EV samples were lysed by addition of SDS to a final concentration of 2%. The samples (50 μg) were digested with trypsin using the filter-aided sample preparation method (23). Briefly, samples were reduced with 100 mM dithiothreitol at 60°C for 30 min, transferred to 30 kDa MWCO Pall Nanosep centrifugation filters (Sigma-Aldrich) and washed repeatedly with 8 M urea and once with digestion buffer (1% sodium deoxycholate in 50 mM TEAB) prior to alkylation with 10 mM methyl methanethiosulfonate in digestion buffer for 30 minutes. Digestion was performed in digestion buffer by addition of 0.5 µg Pierce MS-grade trypsin (Thermo Fisher Scientific) at 37°C and incubated overnight. An additional portion of trypsin was added and incubated for another 2 hours. Peptides were collected by centrifugation.  Digested peptides were labelled using TMT 11-plex isobaric mass tagging reagents (Thermo Scientific) according to the manufacturer’s instructions, and sodium deoxycholate was removed by acidification with 10% trifluoroacetic acid solution. The combined samples were pre-fractionated with basic reversed-phase chromatography using a Dionex Ultimate 3000 UPLC system (Thermo Fischer Scientific). Peptide separations were performed using a reversed-phase XBridge BEH C18 column (3.5 μm, 3.0 mm × 150 mm, Waters Corporation) and a linear gradient from 3% to 40% solvent B over 17 min followed by an increase to 100% B over 5 min. Solvent A was 10 mM ammonium formate buffer at pH 10.00, and solvent B was 90% acetonitrile and 10% 10 mM ammonium formate at pH 10.00. The fractions were concatenated into 20 fractions, dried, and reconstituted in 15 uL of 3% acetonitrile and 0.2% formic acid."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Nanoflow liquid chromatography/mass spectrometry analysis and database search Each fraction (2 uL  Study1, 3 uL study 2) was analyzed on an Orbitrap Fusion Tribrid mass spectrometer interfaced with an Easy-nLC 1200 nanoflow liquid chromatography system (Thermo Fisher Scientific). Peptides were trapped on an Acclaim Pepmap 100 C18 trap column (100 μm × 2 cm, particle size 5 μm, Thermo Fischer Scientific) and separated on an in-house packed analytical column (, particle size 3 μm, Reprosil-Pur C18, Dr. Maisch, 75 μm × 300 mm (study1) or 360 mm (study 2)) using a linear gradient from 6% to 32% B over 75 min followed by an increase to 50% B over 5 min and then 100% B for 5 min at a flow rate of 300 nL/min. Solvent A was 0.2% formic acid and solvent B was 80% acetonitrile in 0.2% formic acid. Precursor ion mass spectra were acquired at 120 000 resolution, and MS2analysis was performed in a data-dependent mode where the most intense doubly or multiply charged precursor ions were isolated in the quadrupole with a 0.7 m/z isolation window and dynamic exclusion within 10 ppm for 45s (study 1) or 60 s (study 2). The isolated precursors were fragmented by collision induced dissociation (CID) at 30% collision energy for 3 s (‘top speed’ setting) and detected in the ion trap, followed by multinotch (simultaneous) isolation of the top 7 (study 1) or 10 (study 2) MS2 fragment ions were fragmentated (MS3) by higher-energy collision dissociation (HCD) at 65% collision energy and detection in the Orbitrap at 50 000 resolution.  Database search and quantification  The data files for each set were merged for identification and relative quantification using Proteome Discoverer version 2.2 (Thermo Fisher Scientific). The search was against Homo Sapiens Swissprot Database (Nov 2017) using Mascot 2.5 (Matrix Science) as the search engine with a precursor mass tolerance of 5 ppm and a fragment mass tolerance of 0.6 Da. Tryptic peptides were accepted with zero missed cleavages, variable modifications of methionine oxidation, fixed cysteine alkylation, and TMT-labelled modifications of the N-terminus and lysines. Percolator was used to validate the identified proteins, and the quantified proteins were filtered at 1% FDR and grouped by sharing the same sequences in order to minimize redundancy. Only peptides unique for a given protein were considered for quantification of the protein, and ratios were calculated by dividing the samples by the reference sample."],"omics_type":["Proteomics"],"labhead":["Aleksander Cvjetkovic"],"instrument_platform":[""],"labhead_affiliation":["Krefting Research Centre, Institute of Medicine at Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["38939898 Cvjetkovic A, Karimi N, Crescitelli R, Thorsell A, Taflin H, Lässer C, Lötvall J. Proteomic profiling of tumour tissue-derived extracellular vesicles in colon cancer. J Extracell Biol. 2024 3(2):e127 10.1002/jex2.127"],"submitter_mail":["gupcf@outlook.com"],"submitter_affiliation":["SAMBIO Core Facilities, Sahgrenska Academy, University of Gothenburg"],"submitter_country":["Sweden"],"pubmed_abstract":["Colon cancer is one of the most commonly occurring tumours among both women and men, and over the past decades the incidence has been on the rise. As such, the need for biomarker identification as well as an understanding of the underlying disease mechanism has never been greater. Extracellular vesicles are integral mediators of cell-to-cell communication and offer a unique opportunity to study the machinery that drives disease progression, and they also function as vectors for potential biomarkers. Tumour tissue and healthy mucosal tissue from the colons of ten patients were used to isolate tissue-resident EVs that were subsequently subjected to global quantitative proteomic analysis through LC-MS/MS. In total, more than 2000 proteins were identified, with most of the common EV markers being among them. Bioinformatics revealed a clear underrepresentation of proteins involved in energy production and cellular adhesion in tumour EVs, while proteins involved in protein biosynthesis were overrepresented. Additionally, 53 membrane proteins were found to be significantly upregulated in tumour EVs. Among them were several proteins with enzymatic functions that degrade the extracellular matrix, and three of these, Fibroblast activating factor (FAP), Cell surface hyaluronidase (CEMIP2), as well as Ephrin receptor B3 (EPHB3), were validated and found to be consistent with the global quantitative results. These stark differences in the proteomes between healthy and cancerous tissue emphasise the importance of the interstitial vesicle secretome as a major player of disease development."],"pubmed_title":["Proteomic profiling of tumour tissue-derived extracellular vesicles in colon cancer."],"pubmed_authors":["Cvjetkovic Aleksander A, Karimi Nasibeh N, Crescitelli Rossella R, Thorsell Annika A, Taflin Helena H, Lässer Cecilia C, Lötvall Jan J"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic profiling of tumor tissue-derived extracellular vesicles in colon cancer","description":"Colon cancer is one of the most commonly occurring tumors among both women and men, and over the past decades the incidence has been on the rise. As such, the need for biomarker identification as well as an understanding of the underlying disease mechanism has never been greater. Extracellular vesicles are integral mediators of cell-to-cell communication and offer a unique opportunity to study the machinery that drives disease progression, and they also function as vectors for potential biomarkers. Tumor tissue and healthy mucosal tissue from the colons of ten patients were used to isolate tissue-resident EVs that were subsequently subjected to global quantitative proteomic analysis through LC-MS/MS. In total, more than 2000 proteins were identified, with most of the common EV markers being among them. Bioinformatics revealed a clear underrepresentation of proteins involved in energy production and cellular adhesion in tumor EVs, while proteins involved in protein biosynthesis were overrepresented. Additionally, 53 membrane proteins were found to be significantly upregulated in tumor EVs. Among them were several proteins with enzymatic functions that degrade the extracellular matrix, and two of these, FAP and TMEM2, as well as the ephrin receptor EPHB3, were validated and found to be consistent with the global quantitative results. These stark differences in the proteomes between healthy and cancerous tissue emphasize the importance of the interstitial vesicle secretome as a major player of disease development.","dates":{"publication":"2026-06-26","submission":"2022-04-14"},"accession":"PXD033236","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:294671","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:111225","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:3715","NEWT:1538","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:31345","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:299467","NEWT:9541","NEWT:51350","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:100658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