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proteomics; liquid biopsy; biomarker; bladder cancer","proteomics","bladder cancer","Extracellular vesicles","biomarker","liquid biopsy"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD062618"],"tissue":["Urine","Prostate Gland","Blood Plasma","Extracellular Vesicle","Bladder","Kidney"],"sample_protocol":["Approximately 40µg of total protein EVs were processed for each sample for proteomic analysis. Following the solid-phase-enhanced sample-preparation (SP3) protocol, samples were enzymatically digested with trypsin/LysC as previously described. Protein identification and quantification was performed by nanoLC-MS/MS equipped with a Field Asymmetric Ion Mobility Spectrometry - FAIMS interface. A Vanquish neo liquid chromatography system coupled to an Eclipse Tribrid Quadrupole Ion trap Orbitrap mass spectrometer together with a High-field asymmetric waveform ion mobility spectrometry – FAIMS equipment (Thermo Scientific) was used.  250 nanograms of peptides of each sample were loaded onto a trapping cartridge (PepMap Neo C18, 300 μm x 5 mm i.d., 174500, Thermo Scientific, Bremen, Germany). Afterwards, the trap column was switched in-line to a μPAC Neo 50 cm column (COL-nano050NeoB) coupled to an EASY-Spray nano flow emitter with 10 μm i.d. (ES993, Thermo Scientific, Bremen, Germany). A 130 min separation was achieved by mixing A: 0.1% FA and B: 80% ACN, 0.1% FA with the following gradient at a flow of 750 nL/min: 0.1 min (1% B to 4% B) and 1.9 min (4% B to 7% B). Next, the flow was reduced to 250 nL/min with the following gradient: 0.1 min (7.0 to 7.1% B), 80 min (7.1% B to 22.5% B), 30 min (22.5% B to 40% B), 8 min (40%B to 99% B) and 9.9 min at 99% B. Next, the column was equilibrated with 1% B. Data acquisition was controlled by Xcalibur 4.6 and Tune 4.0.4091 software (Thermo Scientific, Bremen, Germany).  Data Dependent Acquisition (DDA) procedure was used to obtain MS results. MS acquisition was performed with the Orbitrap detector at 120 000 resolution in positive mode, quadrupole isolation, scan range (m/z) 375-1500, RF Lens 30%, standard AGC target, maximum injection time was set to auto, 1 microscan, data type profile and without source fragmentation. FAIMS mode: standard resolution, total carrier gas flow: static 4L/min, FAIMS CV: -45, -60 and -75 (cycle time, 1 s).  Internal Mass calibration: Run-Start Easy-IC. Filters: MIPS, monoisotopic peak determination: peptide, charge state: 2-7, dynamic exclusion 30s, intensity threshold, 5.0e3. MS/MS data acquisition parameters: quadrupole isolation window 1.8 (m/z), activation type: HCD (30% CE), detector: ion trap, IT scan rate: rapid, mass range: normal, scan range mode: auto, normalized AGC target 100%, maximum injection time: 35 ms, data type centroid."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Data was processed using Proteome Discoverer 3.1.0.638 software (Thermo Scientific) and searched against the UniProt database for the Homo sapiens proteome reviewed proteome (2024_01 with 20,418 entries). A common protein contaminant list search from MaxQuant was also included in the analysis.  The Sequest HT search engine was used to identify tryptic peptides. The ion mass tolerance was 10 ppm for precursor ions and 0.5 Da for fragment ions. The maximum allowed missing cleavage sites was set to two. Cysteine carbamidomethylation was defined as constant modification. Methionine oxidation, deamidation of glutamine and asparagine, peptide terminus glutamine to pyroglutamate, and protein N-terminus acetylation, Met-loss, and Met-loss+acetyl were defined as variable modifications. Peptide confidence was set to high. The processing node Percolator was enabled with the following settings: maximum delta Cn 0.05; target FDR (strict) was set to 0.01 and target FDR (relaxed) was set to 0.05, validation based on q-value. Protein label-free quantitation was performed with the Minora feature detector node at the processing step. Precursor ions quantification was performed at the consensus step with the following parameters: inclusion of unique plus razor peptides, precursor abundance based on intensity, and normalization based on total peptide amount. Proteins with a High FDR confidence (0.01%), absent from the contaminant list and with at least two unique peptides were further filtered. Moreover, only proteins with at least two peptide spectrum matches (PSMs; “High”) were considered as identified by MS/MS. Abundancies from proteins with PSMs <2 (“Peak found” or “N/A”) were set to 0 and missing values of identified proteins were set to a minimum abundance of 150. Furthermore, to be considered as valid, a protein needed to be identified and quantified in at least 50% of samples per experimental group. To identify enriched proteins, a cut-off of 2 was applied to the log2 of the fold change, in order to select tumor-specific markers (FDR < 0.05). For pairwise comparison of BlCa and NA tissues, proteins were considered as tumor exclusive if they were detected and quantified in at least three BlCa samples and not detected in any of the NA samples. The same criteria were applied for identifying exclusive markers across plasma and urine samples. For analyzing EV protein frequency between EV sources, only presence and absence of the proteins was used, protein abundance was not considered, and proteins were classified as detected or not detected across samples."],"omics_type":["Proteomics"],"labhead":["Carmen Jerónimo"],"instrument_platform":[""],"labhead_affiliation":["Cancer Biology and Epigenetics Group, Research Center of IPO Porto (CI-IPOP), Portuguese Oncology Institute of Porto, Porto, Portugal"],"species":["Homo Sapiens (human)"],"submission_type":["PARTIAL"],"publication":["41957654 Lourenço C, Constâncio V, Tavares NT, Monteiro-Reis S, Silva-Santos R, Lobo J, Carvalho Â, Jerónimo C. From cell lines to the clinic: identifying a urinary BlCa-EV signature through comparative proteomics of bladder cancer lysates and extracellular vesicles. Cell Commun Signal. 2026 24(1):317 10.1186/s12964-026-02868-2"],"submitter_mail":["hosorio@i3s.up.pt"],"submitter_affiliation":["i3S - Institute for Research and Innovation in Health, University of Porto"],"submitter_country":["Portugal"],"pubmed_abstract":["<h4>Background</h4>There is an urgent need for the development of innovative diagnostic and therapeutic strategies in bladder cancer (BlCa) management, due to its significant incidence, mortality, and morbidity. Extracellular vesicles (EVs) constitute promising candidates as biomarkers, as their cargo is highly protected from degradation, and they can be isolated non-invasively from urine. Furthermore, they play a pivotal role in intercellular communication that drives disease progression, making them suitable candidates for tailored therapy approaches.<h4>Methods</h4>We employed high-throughput mass-spectrometry to perform a comprehensive proteomic analysis of cell lysates and matched EVs. EVs were isolated from six distinct human BlCa cell lines, representatives of the complete disease spectrum, to identify a BlCa-EV associated signature. The translational ability of this signature was analyzed in urinary EV (uEV) samples from BlCa patients and healthy controls.<h4>Results</h4>This study established a new lysate-to-EV signature that is common to all malignant cell lines. Afterwards, this profile was analyzed in BlCa uEVs, identifying a robust and novel 13-protein BlCa-enriched signature, which includes ITGA2, ITGA6, SCRIB, and TFRC.<h4>Conclusion</h4>We unveiled a novel, EV-derived protein signature that has potential to be further applied for future functional studies, non-invasive diagnostic assays and targeted therapeutic interventions against BlCa."],"pubmed_title":["From cell lines to the clinic: identifying a urinary BlCa-EV signature through comparative proteomics of bladder cancer lysates and extracellular vesicles."],"pubmed_authors":["Lourenço Catarina C, Constâncio Vera V, Tavares Nuno Tiago NT, Monteiro-Reis Sara S, Silva-Santos Rui R, Lobo João J, Carvalho Ângela Â, Jerónimo Carmen C"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic Profiling Of Bladder Cancer Patients-Derived Extracellular Vesicles","description":"Extracellular vesicle (EV) proteomics holds great promise for non-invasive cancer biomarker discovery. This study presents the first comprehensive proteomic characterization of EVs from tissue, plasma, and urine, focusing on bladder cancer BlCa. EVs were isolated via ultracentrifugation, and their cargo was analyzed, comparing BlCa patients to controls and patients with clear cell renal cell carcinoma (ccRCC) and prostate cancer (PCa), to identify BlCa-specific markers. Urine proved to be a rich source of BlCa EVs, enabling tissue-to-urine molecular tracking and insights into BlCa communication. Differential proteomic analysis revealed distinct BlCa EV profiles compared to healthy donors (HDs), ccRCC, and PCa. Importantly, we identified several candidate biomarkers, including ADAM8 and MMP12, exclusively present in BlCa tissue (50% and 64%, respectively) and urine EVs (83% each). Furthermore, six BlCa urinary EV proteins – ACKR1 (66%) and DHCR7, ERMAP, PTGS2, UBXN4, and GYPC (50% each) – were absent in HDs, ccRCC, and PCa. This study identifies several BlCa-derived EV proteins with strong potential for the development of non-invasive EV-based diagnostics and monitoring strategies for BlCa, potentially contributing to advancing precision medicine approaches for this malignancy 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