{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/checksum.txt"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/mqpar.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_448_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_450_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_442_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_444_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_451_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_452_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_443_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_442_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_456_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_454_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_447_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_446_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_455_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_451_F3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_450_F3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_452_F3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_455_F3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_456_F3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_446_F3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_447_F3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_454_F3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_448_F3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_452_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_450_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_455_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_454_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_451_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_446_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_444_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_443_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_444_F3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_443_F3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_447_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_456_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_448_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/20211107_EXO_442_F3.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055260/results.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["hdh03@snu.ac.kr"],"submitter":["Dohyun Han"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Hptec","Exosome","Tgfbeta"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD055260"],"tissue":["Kidney"],"sample_protocol":["Exosome samples for mass spectrometry analysis were prepared as the described previously with some modifications (PMID: 38014595). Briefly, extraction buffer (2% sodium dodecyl sulfate, 5 mM Tris (2-carboxyethyl) phosphine, and 20 mM chloroacetamide in 50 mM ammonium bicarbonate) was added to the exosome pellets. Digestion and desalting of the eluted proteins were performed using the filter-aided sample preparation and StageTip methods, respectively, as previously described (PMID:37999974). The mixture was heated for 15 min at 95℃ to reduce and alkylate the sample. The mixture was loaded onto a 30K Amicon filter (Millipore, MA, USA). Buffer exchanges were performed with the UA solution (8M urea in 0.1 M Tris pH 8.5) via centrifugation at 14,000 × g for 15 min. Following an exchange of the buffer with 40 mM ammonium bicarbonate, protein digestion was performed overnight at 37 ℃ using trypsin/Lys-C Mix (Promega) at a 100:1 protein-to-protease ratio. All resulting peptides were acidified with 10% trifluoroacetic acid and desalted using a homemade C18 Styrenedivinylbenzene (SDB)-Reveres Phase Sulfonate (RPS) StageTip column. The peptides were eluted with elution buffers (40%, 60%, and 80% acetonitrile) into three fractions (PMID:34707096). All the eluted peptides were dried in a speed vacuum."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["MS spectra were processed using MaxQuant software version 1.6.1.0 (PMID:27809316). The MS/MS spectra were searched against the UniProt human protein sequence database (December 2014 release; 88,657 entries), including forward and reverse sequences and common contaminants. Primary searches were performed using a 6-ppm precursor ion tolerance for total protein level analysis. The MS/MS ion tolerance was set to 20 ppm. Cysteine carbamidomethylation was set as a fixed modification. N-acetylation of protein and oxidation of methionine (M) were set as variable modifications. Enzyme specificity was set to full tryptic digestion. Peptides with a minimum length of six amino acids and up to two missed cleavages were considered as search parameters. The false discovery rate (FDR) was set to 1% for peptide and protein identification. For label-free quantification, the Intensity Based Absolute Quantification (iBAQ) algorithm (PMID:21593866) was used as part of the MaxQuant platform."],"omics_type":["Proteomics"],"labhead":["Dohyun Han"],"instrument_platform":[""],"labhead_affiliation":["Proteomics core facility, Biomedical Research Institute, Seoul National University Hospital"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["42291738 Kim Y, Kim K, Park HB, Lee S, Yu MY, Kim YJ, Choi SB, Park WY, Jin K, Kim DK, Kim YS, Han D, Yang SH. A comprehensive approach to elucidating the pathophysiology of kidney fibrosis based on extracellular vesicle proteomics. Front Physiol. 2026 17:1786999 10.3389/fphys.2026.1786999"],"submitter_mail":["hdh03@snu.ac.kr"],"submitter_affiliation":["Proteomics Core Facility, Biomedical Research Institute, Seoul National University Hospital"],"submitter_country":["South Korea"],"pubmed_abstract":["<h4>Introduction</h4>Transglutaminase 2 (TG2) plays a profibrotic role in chronic kidney disease (CKD), but its role in the exosomal proteome remains unexplored. Here, we aimed to evaluate biological processes specifically involved in CKD progression through exosomal proteomic profiling following TG2 inhibition.<h4>Materials and methods</h4>Human proximal tubular epithelial cells (hPTECs) were treated with recombinant transforming growth factor-β (rTGF-β) to induce fibrosis and cysteamine to inhibit TG2. A unilateral ureteral obstruction (UUO) mouse model was used for <i>in vivo</i> validation. EVs were isolated and analyzed using LC-MS/MS analysis. Bioinformatics tools, including enrichGO and STRING, were used to identify key biological pathways and protein interactions. Findings were validated in the UUO mouse model.<h4>Results</h4>TG2 inhibition attenuated the expression of fibrosis- and inflammation-associated proteins in hPTECs and fibroblasts. EV proteomic analysis revealed distinct protein expression patterns following rTGF-β treatment and TG2 inhibition. Altered proteins were primarily extracellular matrix components such as connective tissue growth factor, IGF-binding protein, laminin, plasminogen activator inhibitor, periostin, and collagen.<h4>Conclusions</h4>TG2 inhibition modulated EV-associated proteins involved in fibrosis and inflammation, highlighting its therapeutic potential in CKD. Identifying reversible fibrosis-related factors may provide new targets for CKD treatment."],"pubmed_title":["A comprehensive approach to elucidating the pathophysiology of kidney fibrosis based on extracellular vesicle proteomics."],"pubmed_authors":["Kim Yaerim Y, Kim Kyuhyeon K, Park Hong-Beom HB, Lee Sunwha S, Yu Mi-Yeon MY, Kim Young Joo YJ, Choi Soo Bin SB, Park Woo Yeong WY, Jin Kyubok K, Kim Dong Ki DK, Kim Yon Su YS, Han Dohyun D, Yang Seung Hee SH"],"additional_accession":[]},"is_claimable":false,"name":"Exosomal proteome profiling of human proximal tubular epithelial cells in treatment with TGF-beta","description":"Understanding of the pathophysiology of chronic kidney disease (CKD), characterized by kidney fibrosis, through exosome-derived proteomics has been a challenge. We aimed to evaluate the specific biological process revealed by exosome-derived proteomics to gain insights into CKD progression and therapeutic 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