{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079145/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079145/proteinGroups.txt"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079145/UP000005640_9606_additional.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079145/UP000005640_9606.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079145/C1-FASP-12797.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079145/C2-FASP-12798.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["m.mousa@campus.fct.unl.pt"],"submitter":["Muath Mousa"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["proteomics","urine","metabolomics","Fasp; proteomics; metabolomics; multi-omics; bladder cancer; urine; sample preparation","bladder cancer","multi-omics","Fasp","sample preparation"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD079145"],"sample_protocol":["The Bradford assay was performed on the raw, flow-through, and concentrate fractions of the assessment sample to determine total protein content. However, the raw and flow-through fractions had larger volumes (approximately 15 mL) but protein concentrations below the Bradford assay detection limit, so they were not detected. In contrast, the 10 kDa MWCO membrane retained and concentrated proteins, yielding a detectable protein concentration in the concentrate fraction (approximately 1 mL). As a result, protein extraction was performed only on the concentrate fraction. Ultrasonic-based filter-aided sample preparation (US-FASP) was used on the concentrated portion of urine samples. Briefly, about 300 µL (100 µg protein) was loaded onto the VivaSpin 500 (10 kDa MWCO, Sartorius) and centrifuged for 20 min at 10,000 × g. The loaded proteins in the membrane were washed with 200 μL of 8 M urea 25 mM ammonium bicarbonate (AmBic) solution, then centrifuged for 20 min.  The reduction process for protein disulphide bonds was done by adding 200 μL of 50 mM dithiothreitol (DTT) in 8 M urea and 25 mM AmBic and sonicated using Q500 Sonicator (20 kHz frequency and 500 W maximum power) equipped with cup-horn 431C2 accessory (Qsonica, USA) for 5.25 min (30 s sonication period and 15 s intervals) at 25% amplitude. The solution was then removed by centrifuging at 10,000 × g for 20 min. The sample was washed with 200 μL of 8 M urea, 25 mM AmBic. The alkylation was performed by adding 100 μL 50 mM iodoacetamide in 8 M urea and 25 mM AmBic solution, then sonicated and centrifuged as reported for the reduction step. The sample was washed twice with 200 μL 25 mM AmBic. The protein extract was finally digested by adding 100 μL of trypsin solution (1:30 trypsin-to-protein ratio) prepared in 12.5 mM AmBic. The trypsin digestion was performed using the same sonication parameters as before. The peptides were collected by centrifugation at 10,000 × g for 10 min, followed by two additional membrane washing steps with 100 μL of 3% (v/v) acetonitrile that contained 0.1% (v/v) aqueous formic acid and centrifugation for 10 min at 10,000 × g. Finally, peptides were transferred to a 500 μL microtube and stored at −80 °C until further analysis by Nano-LC‒MS/MS."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For protein analysis, label-free quantification (LFQ) was performed using MaxQuant V2.2.0.0 with standard parameters, integrated with the Andromeda search engine, against the human UniProt reference proteome (UP5640)"],"omics_type":["Proteomics"],"labhead":["Muath Khairi Mousa"],"instrument_platform":[""],"labhead_affiliation":["1) OMICS and Analytical Development Group, BIOSCOPE Research Group, LAQV REQUIMTE, Chemistry Department, NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829-516, Caparica, Portugal"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["m.mousa@campus.fct.unl.pt"],"submitter_affiliation":["BIOSCOPE Research Group, LAQV-REQUIMTE, Department of Chemistry, NOVA School of Science and Technology, NOVA University Lisbon 2829-516, Caparica, Portugal.\n    Country: Portugal"],"submitter_country":["Portugal"],"additional_accession":[]},"is_claimable":false,"name":"Evaluation of FASP for mass spectrometry-based untargeted metabolomics analysis of urine samples","description":"Filter-Aided Sample Preparation (FASP) is a well-established method in proteomics, yet its potential for the parallel recovery of metabolites remains largely unexplored. Herein, we evaluate the performance of FASP as a straightforward workflow for the simultaneous isolation of protein and corresponding metabolite fractions from a single urine sample. The FASP-based LC-MS/MS approach for both proteomics and metabolomics analysis identified 3,163 non-redundant peptides corresponding to 957 unique protein groups. The metabolomic profile comparison of three urine fractions, specifically FASP-concentrated, FASP flow-through, and raw samples, resulted in the identification of 176 common metabolites. Next, as a proof-of-concept, the FASP protocol was applied to compare the metabolomic profiles of clinical urine samples from healthy individuals (n=13) and patients with Ta bladder cancer (n=12). The metabolomic modulation was consistent with previously reported findings, highlighting perturbations in phenylacetate, purine, and tryptophan metabolism, as reflected by changes in metabolites such as adenosine monophosphate (AMP), phenylacetic acid, glutamine, cytosine, and L-tryptophan. FASP protocol can be effectively adapted for the concurrent profiling of both proteomic and metabolomic fractions from urine samples. Thus, FASP-based workflow represents a viable alternative for single-step sample preparation, facilitating subsequent quantitative multi-omics data 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