{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD070917/report.pg_matrix.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD070917/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD070917/EV006731_VR_SCPC059-09_Sweeney_EVs_DIA-PASEF_30SPD_S2_8127.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD070917/EV006747_VR_SCPC059-09_Sweeney_EVs_DIA-PASEF_30SPD_S3_8143.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD070917/EV006732_VR_SCPC059-09_Sweeney_EVs_DIA-PASEF_30SPD_S6_8128.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD070917/EV006752_VR_SCPC059-09_Sweeney_EVs_DIA-PASEF_30SPD_S4_8148.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD070917/EV006735_VR_SCPC059-09_Sweeney_EVs_DIA-PASEF_30SPD_S1_8131.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD070917/EV006745_VR_SCPC059-09_Sweeney_EVs_DIA-PASEF_30SPD_S8_8141.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD070917/EV006741_VR_SCPC059-09_Sweeney_EVs_DIA-PASEF_30SPD_S5_8137.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD070917/EV006744_VR_SCPC059-09_Sweeney_EVs_DIA-PASEF_30SPD_S7_8140.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["christoph.borchers@mcgill.ca"],"submitter":["Vincent Richard"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Proteomics","Extracellular vesicles","Metabolism","Skeletal muscle","Adiponectin"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070917"],"tissue":["Skeletal Muscle Cell"],"sample_protocol":["Size-exclusion chromatography isolation of Plasma-EV Size-exclusion chromatography (SEC) using the qEV columns (IZON, Cambridge, MA) was the primary method to isolate EV from plasma samples. In all experiments, fractions 3 to 6 were collected and used for subsequent EV characterization and downstream applicationsas per manufacturer’s recommendations. The isolated EV were either used immediately or stored at -80°C until usage.  Proteomic analysis Isolated EV were lysed in 5% SDS (Fisher Chemical), 200 mM TRIS (Fisher BioReagnetsTM) pH 8.5 with 10 mM TCEP (60C x 25 minutes). Free disulfides were alkylated with 40 mM IAA (RT, dark, 30 minutes) prior to proteolytic digestion by S-TRAP micro (see attached for the SOP from the vendor that we use). Peptide containing eluates were lyophilized and rehydrated at 10 ng/uL prior to loading on EvoTips and analysis by library free DIA using an Evosep One system coupled to a Bruker timsTOF HT MS operated in DIA-PASEF mode. Samples were separated on an EV1137 column @ 30SPD. For recipient cell proteomics, wild-type L6 cells were seeded on 6-well plate until reaching 80-90% confluency. Confluent cells were treated with EV isoalted from mice plasma, at the concentration of 10 µg/ mL . After 24 h of EV treatment, cells were trypsinized and centrifuged for 5 minutes at 2000 rpm. Cell pellets were collected and lysed in NP40 lysis buffer for 30 min on ice. Cell lysate was then subjected to in-solution digestion following protocol by Promega (Cat# V5280)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data was analyzed in DIA-NN v2.0 searching against an in-silico predicted spectral library based on the canonical human proteome (UniProt) with mouse adiponectin and common contaminants as added sequences.Gene ontology (GO) enrichment and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway enrichemnt analysis was performed using gProfiler, and further analysis and visualization were used metaboanalyst and R-studio."],"omics_type":["Proteomics"],"labhead":["Christoph H Borchers"],"instrument_platform":[""],"labhead_affiliation":["Segal Cancer Proteomics Centre, Lady Davis Institute for Medical Research, Jewish General Hospital, McGill University, Montreal, Québec, Canada"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)","Mus Musculus (mouse)"],"submitter_mail":["vincentroyrichard@gmail.com"],"publication":["37025182 Lopez K, Lai SWT, Lopez Gonzalez EJ, Dávila RG, Shuck SC. Extracellular vesicles: A dive into their role in the tumor microenvironment and cancer progression. Front Cell Dev Biol. 2023 11:1154576 10.3389/fcell.2023.1154576"],"submitter_affiliation":["Lady Davis Institute for Medical Research, Jewish General Hospital, McGill University"],"submitter_country":["Canada"],"pubmed_abstract":["Extracellular vesicles (EVs) encompass a diverse set of membrane-derived particles released from cells and are found in numerous biological matrices and the extracellular space. Specific classes of EVs include apoptotic bodies, exosomes, and microvesicles, which vary in their size, origin, membrane protein expression, and interior cargo. EVs provide a mechanism for shuttling cargo between cells, which can influence cell physiology by transporting proteins, DNA, and RNA. EVs are an abundant component of the tumor microenvironment (TME) and are proposed to drive tumor growth and progression by communicating between fibroblasts, macrophages, and tumor cells in the TME. The cargo, source, and type of EV influences the pro- or anti-tumoral role of these molecules. Therefore, robust EV isolation and characterization techniques are required to ensure accurate elucidation of their association with disease. Here, we summarize different EV subclasses, methods for EV isolation and characterization, and a selection of current clinical trials studying EVs. We also review key studies exploring the role and impact of EVs in the TME, including how EVs mediate intercellular communication, drive cancer progression, and remodel the TME."],"pubmed_title":["Extracellular vesicles: A dive into their role in the tumor microenvironment and cancer progression."],"pubmed_authors":["Lopez Kassandra K, Lai Seigmund Wai Tsuen SWT, Lopez Gonzalez Edwin De Jesus EJ, Dávila Raúl G RG, Shuck Sarah C SC"],"additional_accession":[]},"is_claimable":false,"name":"Extracellular Vesicles from Adiponectin-Deficient Mice Mediate Skeletal Muscle Metabolic Dysfunction and Insulin Resistance","description":"Adiponectin regulates systemic metabolism and enhances extracellular vesicle (EV) biogenesis, but the impact of adiponectin deficiency on circulating EV composition and their impact on muscle metabolism remains unclear. Here, we integrated proteomic analyses of plasma EVs from wild-type (WT) and adiponectin-knockout (KO) mice fed chow or high-fat diet (HFD) with metabolomic profiling of quadriceps from these mice and functional analyses in skeletal muscle cells treated with these EVs. Plasma EVs showed altered size distribution and distinct proteomic signatures: KO-HFD EVs were depleted of mitochondrial and glycolytic enzymes (CS, MDH2, ALDOA, TPI1) that were enriched in WT-HFD EVs. We observed that KO EVs blunted insulin-stimulated Akt phosphorylation, glucose uptake, and mitochondrial respiration in L6 myotubes, whereas WT-HFD EVs improved these responses. Proteomic profiling of recipient cells revealed compensatory up-regulation of metabolic and stress-response pathways overlapping with those diminished in KO EVs, suggesting adaptive remodeling of cellular metabolism. Furthermore, quadricep muscle metabolomics revealed genotype- and diet-specific reductions in amino acid-derived intermediates of the tricarboxylic-acid (TCA) and urea cycles, indicating altered catabolic flux in KO mice. These findings identify an adiponectin-EV axis coordinating muscle metabolic homeostasis, offering insight into inter-organ metabolic communication under dietary 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