{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067365/experimentaldesign.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067365/060924_Fazeli_Suhashini_MEV_proteinGroups.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067365/240904_10_Orbi3_MS_SER_G60_T85_Fazeli_Subhashini_MEV_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067365/240904_26_Orbi3_MS_SER_G60_T85_Fazeli_Subhashini_MEV_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067365/240904_14_Orbi3_MS_SER_G60_T85_Fazeli_Subhashini_MEV_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067365/240904_22_Orbi3_MS_SER_G60_T85_Fazeli_Subhashini_MEV_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067365/240904_24_Orbi3_MS_SER_G60_T85_Fazeli_Subhashini_MEV_09.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067365/240904_12_Orbi3_MS_SER_G60_T85_Fazeli_Subhashini_MEV_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067365/240904_16_Orbi3_MS_SER_G60_T85_Fazeli_Subhashini_MEV_06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067365/240904_20_Orbi3_MS_SER_G60_T85_Fazeli_Subhashini_MEV_10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067365/240904_18_Orbi3_MS_SER_G60_T85_Fazeli_Subhashini_MEV_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067365/240904_04_Orbi3_MS_SER_G60_T85_Fazeli_Subhashini_MEV_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067365/240904_06_Orbi3_MS_SER_G60_T85_Fazeli_Subhashini_MEV_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067365/240904_08_Orbi3_MS_SER_G60_T85_Fazeli_Subhashini_MEV_12.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["alireza.fazeli@emu.ee"],"submitter":["Madhusha Prasadani"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Cows","Insulin resistance","Extarcellular vesicles","Milk"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067365"],"tissue":["Milk"],"sample_protocol":["Proteins were precipitated by adding a 20% (v/v) precipitation solution (Sodium deoxycholate (SD) 4 mg/mL in 100% trichloroacetic acid), incubating for 30 minutes at 4 °C, and then pelleted by centrifuging at 17,000 ×g for 15 min at RT. Pellets were washed once with acetone and once with methanol, and air dried. Protein concentrations were estimated using a total protein measuring kit  (Micro BCA assay kit, Thermo Fisher Scientific, Rockford, United States). Precipitated proteins were then solubilized in 7 M urea, 2 M thiourea, 100 mM ammonium bicarbonate buffer (ABC), and 20 mM methylamine. For protein reduction, samples were incubated with 10 mM dithiothreitol for 30 minutes at 30 oC and alkylated with 30 mM chloroacetamide in the dark for 30 minutes. for pre-digestion of proteins with a 1:100 (enzyme to protein ratio), Protease Lys-C (Fujifilm Wako Pure Chemical, Osaka, Japan) was added and incubated for 2 h at 25 °C. Next, the solution was further diluted five times with 100 mM ABC and with a 1:50 enzyme/substrate ratio using trypsin (Sigma Aldrich, Saint Louis, United States) overnight at 25 oC. Digested samples were acidified with trifluoroacetic acid at a concentration of 1% and desalted using in-house octadecyl alkyl substituent (C18) solid phase extraction tips. Finally, the purified peptides were reconstituted in 0.5% trifluoroacetic acid for nano-LC/MS/MS analysis."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["LC-MS/MS analysis was carried out by injecting 1 µg of peptide in to an Easy-nLC 1000 system® (Thermo Fisher Scientific, Rockford, United States) and eluted at 250 nL/min from the trap to a 75 µm ID × 50 cm emitter column (New Objective, Massachusetts, USA) packed with C18 material (3 µm, 300 Å particles, Dr Maisch, Ammerbuch, Germany). Peptides were eluted to an in-house packed (3 µm C18 particles, Dr Maisch, Ammerbuch, Germany) analytical 50 cm × 75 µm emitter-column (MS Wil, CoAnn Technologies, the Netherlands) and separated with a 60 min 8-40% buffer B gradient (buffer A: 0.1% formic acid, buffer B: 80% acetonitrile + 0.1% formic acid). then the separated peptides were nano-sprayed into a Q Exactive Plus® (Thermo Fisher Scientific, Rockford, United States) quadrupole orbitrap mass spectrometer via a nano-electrospray source (positive mode, spray voltage of 2.5 kV). The MS was operated with a top-12 data-dependent acquisition strategy. Finally, a 350-1,400 m/z full MS scan at a resolution setting of R = 60,000 at 200 m/z was conducted, followed by higher-energy collisional dissociation fragmentation (normalized collision energy of 26) of the 12 most intense ions (z: +2 to +5) at R = 30,000. MS and MS/MS ion target values were 3 × 106 and 1 ×105 ions with 50 and 45 ms injection times, respectively. MS/MS isolation was carried out with 1.6 m/z isolation windows and dynamic exclusion was limited to 30 s.Mass spectrometry raw files were processed with the MaxQuant software package (version 2,2,0,0). Methionine oxidation, and protein N-terminal acetylation were set as variable modifications, while cysteine carbamidomethylation was defined as a fixed modification. A protein search was performed against UniProt (www.uniprot.org) Bos taurus proteome database (downloaded: 2024 August) using the tryptic digestion rule (cleavages after lysine and arginine without proline restriction). The common contaminating proteins database was also included in the search, excluding the bovine serum proteins. Only identifications with at least 1 peptide ≥ 7 amino acids long (with up to 2 missed cleavages) were accepted and transfer of identifications between runs based on accurate mass and retention time was enabled. Label-free protein quantification (LFQ) was performed with the MaxQuant LFQ algorithm, with the LFQ ratio count (number of quantified peptides for reporting a protein intensity) set to 2. Peptide-spectrum match and protein false discovery rate (FDR) were kept below 1% using a target-decoy approach. All other parameters were default."],"omics_type":["Proteomics"],"labhead":["Prof. Alireza Fazeli"],"instrument_platform":[""],"labhead_affiliation":["Institute of Veterinary Medicine and Animal Sciences, Estonian University of Life Sciences, Estonia"],"submission_type":["PARTIAL"],"species":["Bos Taurus (bovine)"],"submitter_mail":["madhusha@emu.ee"],"publication":["42065931 Prasadani M, Jaakson H, Karis P, Muhandiram S, Henno M, Kuusik S, Ling K, Rajapaksha H, Ots M, Andronowska A, Pradeep Kodithuwakku S, Volke V, Fazeli A. Milk extracellular vesicles reveal insulin resistance status in peripartum dairy cows. Vet Q. 2026 46(1):2665485 10.1080/01652176.2026.2665485"],"submitter_affiliation":["Junior research fellow"],"submitter_country":["Estonia"],"pubmed_abstract":["The transition from gestation to lactation is a critical period that leads to insulin resistance (IR) in dairy cows. IR detection requires invasive sampling and laborious methods; therefore, novel and non-invasive approaches are essential. Extracellular vesicles (EVs) are nano-sized particles released by cells and are linked to disease pathophysiology. Hence, the present study aimed to explore the potential application of cow milk EVs (MEVs) in detecting IR in dairy cows. An intravenous glucose tolerance test (IVGTT) was performed (<i>n</i> = 12), and the cows were classified as low, moderate, or high IR based on prepartum area under the curve insulin values. MEVs were enriched using double-size exclusion chromatography and physico-chemically characterized. The results revealed that the particle diameter of MEVs was significantly higher (<i>p</i> ≤ 0.05) in the high-IR group compared to other groups. Out of 26 fatty acids (FAs) detected in MEVs, three long-chain FAs differed significantly in abundance (<i>p</i> ≤ 0.05) in high-IR group. Proteomic analysis revealed a correlation of inflammation and the IR-related proteins; Annexin A1 and Rab proteins, to IR severity. Overall, this study identified promising predictors of IR in cows, supporting the development of non-invasive biomarkers for early detection, facilitating improved herd and disease management, and reducing economic losses."],"pubmed_title":["Milk extracellular vesicles reveal insulin resistance status in peripartum dairy cows."],"pubmed_authors":["Prasadani Madhusha M, Jaakson Hanno H, Karis Priit P, Muhandiram Subhashini S, Henno Merike M, Kuusik Sirje S, Ling Katri K, Rajapaksha Harinda H, Ots Meelis M, Andronowska Aneta A, Pradeep Kodithuwakku Suranga S, Volke Vallo V, Fazeli Alireza A"],"additional_accession":[]},"is_claimable":false,"name":"proteomic analysis of cow milk derived extracellular vesicles from cows with different insulin resistance stages","description":"Cows were classified into dofferent insulin resisitance (IR) groups as low, moderate and high IR. Milk samples were collected and extracellular vesicles were isolated and proteomic cargo files were studies and compard among diffrent IR groups to identigy potential 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