{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067743/XA04307DA_DB_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067743/XA05659DA_Con_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067743/XA04307DA_DB_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067743/XA04307DA_EVS_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067743/XA04307DA_DB_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067743/XA04307DA_EVS_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067743/XA05659DA_Con_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067743/XA05659DA_Con_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067743/XA04307DA_EVS_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067743/XA04307DA_DB_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067743/XA04307DA_EVS_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067743/XA05659DA_Con_3.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067743/result.zip"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["lonva@live.cn"],"submitter":["Qianfa Long"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Extracellular vesicles；diabetic peripheral neuropathy"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067743"],"tissue":["Sciatic Nerve"],"sample_protocol":["Samples were retrieved from -80°C, and an appropriate amount was weighed and transferred to a liquid nitrogen-pre-cooled mortar. The samples were thoroughly ground into powder under liquid nitrogen. Each group of samples was mixed with four times the volume of lysis buffer (8 M urea, 1% protease inhibitor) and sonicated for lysis. The lysate was centrifuged at 4°C and 12,000 g for 10 minutes to remove cell debris. The supernatant was transferred to a new centrifuge tube, and the protein concentration was determined using a BCA assay kit.  Equal amounts of protein from each sample were taken for digestion. The volume was adjusted to be consistent using lysis buffer. One volume of pre-cooled acetone was added, followed by vortex mixing, and then four volumes of pre-cooled acetone were added. The mixture was precipitated at -20°C for 2 hours. The sample was centrifuged at 4,500 g for 5 minutes, and the supernatant was discarded. The precipitate was washed 2–3 times with pre-cooled acetone. After drying, the precipitate was resuspended in 200 mM TEAB and dispersed via sonication. Trypsin was added at a ratio of 1:50 (enzyme:protein, m/m) for overnight digestion. Dithiothreitol (DTT) was added to a final concentration of 5 mM and incubated at 56°C for 30 minutes for reduction. Subsequently, iodoacetamide (IAA) was added to a final concentration of 11 mM and incubated at room temperature in the dark for 15 minutes."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Liquid Chromatography-Mass Spectrometry (LC-MS/MS) Analysis  Peptides were dissolved in mobile phase A (0.1% formic acid, 2% acetonitrile in water) and separated using an EASY-nLC 1200 ultra-high-performance liquid chromatography system. Mobile phase B consisted of 0.1% formic acid and 90% acetonitrile in water. The liquid chromatography gradient was set as follows: 0–22.5 min, 6%–22% B; 22.5–26.5 min, 22%–34% B; 26.5–28.5 min, 34%–80% B; 28.5–30 min, 80% B, with a constant flow rate of 700 nl/min.   After separation, the peptides were ionized using an NSI ion source and analyzed with an Orbitrap Exploris 480 mass spectrometer. The ion source voltage was set to 2,300 V, and the FAIMS compensation voltage (CV) was set to -45 V. Both the parent ions and their secondary fragments were detected and analyzed using a high-resolution Orbitrap. The primary mass spectrometry scan range was set to 350–1400 m/z with a resolution of 60,000. The secondary mass spectrometry scan range started at 120 m/z with a resolution of 15,000. Data were acquired using a data-independent acquisition (DIA) mode, where primary scans were followed by fragmentation of peptide ions in multiple consecutive m/z windows in the HCD collision cell with 27% fragmentation energy, followed by secondary mass spectrometry analysis. To improve mass spectrometry efficiency, the automatic gain control (AGC) was set to 1E6, and the maximum injection time was set to 22 ms."],"omics_type":["Proteomics"],"labhead":["qianfa Long"],"instrument_platform":[""],"labhead_affiliation":["Xi'an Central Hospital"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["lonva@live.cn"],"submitter_affiliation":["Xi’an Central Hospital, Xi’an Jiaotong University"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"Extracellular vesicle‑mediated restraint of hepatic CD74–NF‑κB repairs diabetic neuropathy","description":"Diabetic peripheral neuropathy (DPN) is a common and devastating complication of diabetes mellitus, leading to progressive degeneration of peripheral nerves and resulting in chronic pain, sensory loss, and disability. Despite its high prevalence and significant burden, current treatments are largely palliative, as the multifaceted metabolic, inflammatory, and vascular mechanisms that underlie DPN have proven challenging to target with disease-modifying therapies. Extracellular vesicles (EVs, including exosomes) are increasingly recognized for their capacity to mediate intercellular communication and promote tissue repair in various disease contexts. While previous studies have suggested the therapeutic potential of EVs on DPN, the systemic fate of administered EVs and the mechanisms by which they orchestrate repair multiorgan systems remain unclear. Mesenchymal stromal/stem cells (MSCs) are notable for their immunoregulatory properties, making them an attractive and practical source of EVs for translational research. Here, we investigate the action and mechanism of therapeutic EVs derived from MSCs in a mouse model of DPN. Using in vivo imaging, multi-omics analyses, and functional assessments, we define how liver-trophic EVs elicit cross-organ immunomodulation and promote neural repair in diabetic 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