{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067282/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067282/Astral_20241212_ES906_DIA_7min_3-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067282/Astral_20241212_ES906_DIA_7min_0-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067282/Astral_20241212_ES906_DIA_7min_3-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067282/Astral_20241212_ES906_DIA_7min_1-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067282/Astral_20241212_ES906_DIA_7min_3-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067282/Astral_20241212_ES906_DIA_7min_0-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067282/Astral_20241212_ES906_DIA_7min_0-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067282/Astral_20241212_ES906_DIA_7min_1-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067282/Astral_20241212_ES906_DIA_7min_1-1.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067282/search.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["zhougang@whu.edu.cn"],"submitter":["Haoyu Zhou"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Human","Oscc","Migrasomes","Olk"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067282"],"tissue":["Cell Culture"],"sample_protocol":["Proteomic analysis of migrasomes from DOK, DOK-BD and DOK-4NQO cells was performed at Shanghai Hwayen Biotechnological, Inc. in China. Each migrasome sample contained 50 µL of purified migrasomes at approximately 1.5 µg/µL concentration. Briefly, migrasome proteins were extracted using lysis buffer containing 7 M urea, 2% SDS, and protease inhibitor cocktail. Proteins from equal volumes of nine migrasome samples, each 50 µL, were acetone-extracted. Fifty micrograms protein from volume-equivalent dilution was treated with 10 mM DTT at 37°C for 1 h, followed by IAA at a 1:5 ratio to DTT with 40 min dark incubation. Five volumes precipitation reagent were added with 1 h incubation. Samples were centrifuged at 13,000 rpm for 1 h. Peptides were generated by trypsin digestion overnight at 37°C. After desalination using MonoSpin C18 columns, analysis used nano-LC Easy nLC1200 coupled to an Orbitrap Fusion Lumos Tribrid mass spectrometer from Thermo Fisher Scientific in MA, USA. Peptides were redissolved in 0.1% formic acid and separated on a C18 column measuring 50 mm × 15 cm with 1.7 μm particles, at 500 nL/min flow rate. MS/MS analysis employed an Orbitrap Exploris™ 480 + FAIMS Pro™ System (Thermo Fisher Scientific, MA, USA) in data-independent acquisition (DIA) mode with parameters: (1) MS: Scan range (m/z): 350–1500; Resolution: 120,000; AGC target: 48,000; Maximum injection time: 50 ms. (2) HCD-MS/MS: Resolution: 30,000; AGC target: 2×10⁵; Collision energy: 32. DIA data were processed in Spectronaut™ 11.0 (Biognosys AG) using spectral libraries from Proteome Discoverer™ (v2.4, Thermo Scientific®)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw protein expression data were log₂-transformed and analyzed for differential abundance using the limma package (v3.60.6) in R version 4.4.1. Principal component analysis (PCA) was performed with the base prcomp function and visualized in 3D using Plotly (v4.11.0) and geometry (v0.5.2). Volcano plots were generated with ggplot2 (v3.5.2) and annotated using ggrepel (v0.9.6). Heatmaps were created with ComplexHeatmap (v2.21.1) and circlize (v0.4.16). Data import, processing and export used openxlsx (v4.2.8), stringr (v1.5.1) and dplyr (v1.1.4). Significance thresholds were set at fold change >1.5 and adjusted P < 0.05. All plots were generated in R."],"omics_type":["Proteomics"],"labhead":["Gang Zhou"],"instrument_platform":[""],"labhead_affiliation":["Wuhan university"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["zhouhy@whu.edu.cn"],"publication":["41927525 Jiang MJ, Zhou HY, Bai YT, Chen XJ, Zhou G. Migrasome-transported PTGES amplifies the PGE2 cascade in SPP1&lt;sup&gt;+&lt;/sup&gt; macrophages to drive oral leukoplakia carcinogenesis. Nat Commun. 2026 17(1):4753 10.1038/s41467-026-70824-2"],"submitter_affiliation":["Wuhan university"],"submitter_country":["China"],"pubmed_abstract":["Oral leukoplakia (OLK) is a common oral potentially malignant disorder with a significant risk of transforming into oral squamous cell carcinoma (OSCC), yet the mechanisms remain poorly understood. Here we show that migrasomes, membranous organelles released by migrating cells, are detectable in epithelial cells of OLK and OSCC tissues and are more abundant in OSCC. Using carcinogenesis models, we transform human dysplastic oral keratinocyte (DOK) into oral carcinoma (DOK-TC) cells. Migrasomes derived from DOK-TC cells enhance interactions between DOK-TC cells and macrophages to promote carcinogenesis. Mechanistically, the uptake of prostaglandin E synthase (PTGES)-enriched migrasomes by macrophages increases PTGES expression and prostaglandin E2 secretion, which in turn induces an SPP1<sup>+</sup> macrophage phenotype and promotes migration and proliferation. These findings uncover an unexplored migrasome-dependent immunomodulatory mechanism in OLK carcinogenesis and suggest migrasomal PTGES as a promising biomarker for early OSCC detection and a potential therapeutic target."],"pubmed_title":["Migrasome-transported PTGES amplifies the PGE2 cascade in SPP1&lt;sup&gt;+&lt;/sup&gt; macrophages to drive oral leukoplakia carcinogenesis."],"pubmed_authors":["Jiang Ming-Jing MJ, Zhou Hao-Yu HY, Bai Yu-Ting YT, Chen Xiao-Jie XJ, Zhou Gang G"],"additional_accession":[]},"is_claimable":false,"name":"Human 4D-label free quantitative proteomics of migrasomes from DOK, DOK-BD and DOK-4NQO cells","description":"Oral leukoplakia (OLK), a recognized oral potentially malignant disorder, demonstrates significant susceptibility to malignant transformation into oral squamous cell carcinoma (OSCC). This study aimed to investigate the involvement of migrasomes, novel intercellular communication organelles, in the carcinogenesis of OLK. Migrasomes were observed through electron microscopy and multiplex immunofluorescence in OLK and OSCC tissues, and the purified migrasomes were characterized by wheat germ agglutinin staining, long-term imaging, Western blot, and electron microscopy. Single-cell RNA sequencing analysis was conducted to evaluate the effect of migrasomes on the microenvironment. The combined analysis of the quantitative proteome of migrasomes and the transcriptome of recipient cells was used to investigate the involvement of migrasomes in the carcinogenesis of OLK. Xenograft tumors and a mouse model of tongue leukoplakia helped verify migrasomes’ participation in carcinogenesis. Migrasomes were found in both human OLK and OSCC tissues. Notably, migrasomes isolated from dysplastic oral keratinocyte DOK cells, DOK-transformed cells, and OSCC cell lines exhibited characteristic morphological features and distinct molecular signatures. A significant correlation existed between migrasome score and the infiltration of immune cells. Moreover, the protein cargoes within migrasomes promoted leukoplakia carcinogenesis by inducing an immunosuppressive microenvironment. This study reveals that migrasomes drive leukoplakia carcinogenesis. It not only deepens the understanding of the interaction between dysplastic keratinocytes and immune cells during this process but also provides potential diagnostic biomarkers or targets for the treatment of the precancer stage of 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