{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_ALL_022820.xlsx"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_1_022820.msfView","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_1_022820.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_3_022920.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_4_022620.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_7_022820.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_2_022820.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_9_022920.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_6_022920.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_12_022920.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_1_022820.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_5_022820.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_10_022620.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_11_022820.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_8_022920.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_ALL_022820.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075094/Retino_TP_ALL_022820.pdResultView"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["sailaja.elchuri@gmail.com"],"submitter":["Gajanan Sathe"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Ctg repeat","Fuchs endothelial corneal dystrophy (fecd)","Retina"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075094"],"sample_protocol":["Cultured iFECD and iFECD TCF4ΔCTG cells were prepared for proteomic analysis by first washing with PBS and detaching using TrypLE reagent (Thermo Fisher Scientific). After three additional PBS washes, the cell pellets were rapidly frozen in liquid nitrogen and stored at -80°C until processing. For protein extraction, cells were disrupted by sonication in a lysis buffer consisting of 2% sodium dodecyl sulfate (SDS) and 50 mM triethylammonium bicarbonate containing Halt™ Protease and Phosphatase Inhibitor Cocktail (Thermo Fisher Scientific). Following clarification by centrifugation, the protein concentration in the supernatant was determined using the bicinchoninic acid (BCA) protein assay. Sample quality was assessed by separating 20 µg aliquots on 10% SDS-PAGE gels. Prior to enzymatic digestion, proteins underwent reduction with 5 mM dithiothreitol (60°C, 1 h), followed by alkylation with 10 mM iodoacetamide (room temperature, 30 min, protected from light). Proteins were then precipitated overnight (12 h) in ice-cold acetone at 4°C, collected by centrifugation, and reconstituted in 50 mM triethylammonium bicarbonate buffer. Enzymatic digestion was performed using sequencing-grade trypsin (Promega, Madison, WI) over a 12 h period. The resulting peptide mixtures were purified using Sep-Pak C18 Plus Light cartridges (Waters, Milford, MA). Briefly, peptides were acidified with 1% formic acid, loaded onto activated Sep-Pak columns (preconditioned with acetonitrile followed by 0.1% formic acid), washed with 0.1% formic acid, and finally eluted with 40% acetonitrile containing 0.1% formic acid. The purified peptides were subsequently dried, reconstituted in 100 mM triethylammonium bicarbonate (TEAB), and labeled using TMT10plex™ reagents (Thermo Fisher Scientific) according to the manufacturer's protocol for quantitative proteomic analysis. TMT-labeled peptide samples were dissolved in 1 mL of high-pH reverse phase chromatography (bRPLC) buffer A (7 mM TEAB, pH 8.5) and subjected to fractionation using an XBridge BEH C18 column . Peptides were reconstituted in 0.1% formic acid and analyzed using LC-MS/MS on an Orbitrap Fusion Lumos instrument (Thermo Fisher Scientific) interfaced with an Easy-nLC™ 1200 nanoflow system (Thermo Fisher Scientific). The samples were first loaded onto a nanoViper™ precolumn (100 μm × 20 mm) at a flow rate of 3 µL/min for concentration and cleanup. They were then resolved on an Acclaim RSLC 120 C18 analytical column (75 µm × 50 cm, Thermo Fisher Scientific) with a flow rate of 280 nL/min. Peptides were resolved using a step gradient: solvent B (0.1% formic acid in 95% acetonitrile) was increased from 8% to 22% over the first 70 min, then further raised to 35% between 70 and 103 min, with a total run time of 120 min. The mass spectrometer was operated in data-dependent acquisition mode, capturing full MS scans (m/z 350–1600) in the Orbitrap at a resolution of 120,000 (at 200 m/z). For MS1, the automatic gain control (AGC) target was set to 4 × 10⁵, with a maximum ion injection time of 50 ms. MS/MS fragmentation was conducted on the most abundant precursor ions (charge states ≥2) using higher-energy collisional dissociation (HCD) at 34% normalized collision energy. Fragment ions were detected in the Orbitrap at a resolution of 50,000, with a maximum injection time of 100 ms. Precursors were isolated using a 1.6 m/z window, and dynamic exclusion was applied within a 3 s cycle time."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Mass spectrometric data were analyzed for protein identification and quantification using the SEQUEST™ algorithm within the Proteome Discoverer software, with searches conducted against the Human RefSeq protein database. Search parameters were designed to allow up to two missed cleavage sites, with fixed modifications including cysteine carbamidomethylation and TMT 10-plex labeling (+229.163 Da) at peptide N-termini and lysine residues. Methionine oxidation was considered a variable modification. Mass tolerance was set to 10 ppm for precursor ions and 0.1 Da for fragment ions. Strict filtering criteria were applied, maintaining a false discovery rate of 1% for both peptide–spectrum matches and protein identifications. Quantitative analysis was performed using Perseus software 55 to calculate fold changes and statistical significance. Protein abundance ratios were converted to the log2 scale, and DEPs were defined using dual thresholds of |log2 fold change| ≥ 0.5 and P-value < 0.05."],"omics_type":["Proteomics"],"labhead":["Sailaja Elchuri, Ph.D."],"instrument_platform":[""],"labhead_affiliation":["Department of Nanobiotechnology, Vision Research Foundation, Sankara Nethralaya, 18 College Road, Chennai, Tamil Nadu, 600 006, India."],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["gsathe001@dundee.ac.uk"],"publication":["41865104 Yuasa T, Nakagawa T, Honda T, Nishiuchi G, Sato M, Tokunaga A, Nakahara M, Tourtas T, Schlötzer-Schrehardt U, Kruse F, Padmanabhan P, Chatterjee A, Sathe G, Ghose V, Janakiraman N, Koizumi N, Elchuri SV, Okumura N. TCF4 trinucleotide repeat expansion drives distinct proteomic signatures in Fuchs endothelial corneal dystrophy. Sci Rep. 2026 16(1):14446 10.1038/s41598-026-43789-x"],"submitter_affiliation":["Centre for Targeted Protein Degradation (CeTPD)\nUniversity of Dundee"],"submitter_country":["United Kingdom"],"pubmed_abstract":["The aims of this study were to use an isogenic cell model system to investigate the proteomic consequences of TCF4 trinucleotide repeat expansion in Fuchs endothelial corneal dystrophy (FECD) and to identify potential molecular pathways contributing to disease pathogenesis. We used our previously established immortalized FECD cells (iFECD) that harbor CTG repeat expansion in TCF4 and CRISPR/Cas9 genome editing to generate an isogenic counterpart (iFECD TCF4ΔCTG) in which the expansion was deleted. Comprehensive proteomic analysis was then performed using tandem mass tag (TMT)-labeled quantitative LC-MS/MS. The resulting data were subjected to differential expression analysis, functional enrichment analysis, and protein-protein interaction network construction to elucidate the molecular impact of the CTG repeat expansion. Deletion of the CTG repeat expansion significantly altered the corneal endothelial proteome, with 90 upregulated and 111 downregulated proteins (|log<sub>2</sub> fold change| ≥ 0.5, P-value < 0.05). Functional enrichment analysis revealed that the downregulated proteins were predominantly associated with extracellular matrix organization and cell-substrate adhesion pathways, while the upregulated proteins were enriched in interferon signaling and antigen-processing pathways. The most significantly upregulated proteins included neuropilin-1, Cip1-interacting zinc finger protein, and protein-glutamine gamma-glutamyltransferase 2, while protein phosphatase 1 regulatory subunit 14 C, alpha-crystallin B chain, and 14-3-3 protein sigma showed the greatest downregulation. Our findings demonstrate that TCF4 CTG repeat expansion significantly impacts the corneal endothelial proteome, particularly affecting the extracellular matrix and cell adhesion proteins that likely contribute to guttae formation. These proteomic alterations provide mechanistic insights connecting trinucleotide repeat expansion to endothelial dysfunction and suggest potential therapeutic targets for FECD."],"pubmed_title":["TCF4 trinucleotide repeat expansion drives distinct proteomic signatures in Fuchs endothelial corneal dystrophy."],"pubmed_authors":["Yuasa Taichi T, Nakagawa Tatsuya T, Honda Tetsuro T, Nishiuchi Go G, Sato Masakazu M, Tokunaga Ayumi A, Nakahara Makiko M, Tourtas Theofilos T, Schlötzer-Schrehardt Ursula U, Kruse Friedrich F, Padmanabhan Prema P, Chatterjee Amit A, Sathe Gajanan G, Ghose Vivek V, Janakiraman Narayanan N, Koizumi Noriko N, Elchuri Sailaja V SV, Okumura Naoki N"],"additional_accession":[]},"is_claimable":false,"name":"TCF4 trinucleotide repeat expansion drives distinct proteomic signatures in Fuchs endothelial corneal dystrophy","description":"The aims of this study were to use an isogenic cell model system to investigate the proteomic consequences of TCF4 trinucleotide repeat expansion in Fuchs endothelial corneal dystrophy (FECD) and to identify potential molecular pathways contributing to disease pathogenesis. We used our previously established immortalized FECD cells (iFECD) that harbor CTG repeat expansion in TCF4 and CRISPR/Cas9 genome editing to generate an isogenic counterpart (iFECD TCF4ΔCTG) in which the expansion was deleted. Comprehensive proteomic analysis was then performed using tandem mass tag (TMT)-labeled quantitative LC-MS/MS. The resulting data were subjected to differential expression analysis, functional enrichment analysis, and protein-protein interaction network construction to elucidate the molecular impact of the CTG repeat expansion. Deletion of the CTG repeat expansion significantly altered the corneal endothelial proteome, with 90 upregulated and 111 downregulated proteins (|log2 fold change| ≥ 0.5, P-value < 0.05). Functional enrichment analysis revealed that the downregulated proteins were predominantly associated with extracellular matrix organization and cell–substrate adhesion pathways, while the upregulated proteins were enriched in interferon signaling and antigen-processing pathways. The most significantly upregulated proteins included neuropilin-1, Cip1-interacting zinc finger protein, and protein-glutamine gamma-glutamyltransferase 2, while protein phosphatase 1 regulatory subunit 14C, alpha-crystallin B chain, and 14-3-3 protein sigma showed the greatest downregulation. Our findings demonstrate that TCF4 CTG repeat expansion significantly impacts the corneal endothelial proteome, particularly affecting the extracellular matrix and cell adhesion proteins that likely contribute to guttae formation. These proteomic alterations provide mechanistic insights connecting trinucleotide repeat expansion to endothelial dysfunction and suggest potential therapeutic targets for FECD.","dates":{"publication":"2026-06-08","submission":"2026-03-02"},"accession":"PXD075094","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:317447","NEWT:4688","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:235443","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:472","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:8655","NEWT:5147","NEWT:28104","NEWT:407821","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:6063","NEWT:1328388","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:380394","NEWT:226900","NEWT:1266738","NEWT:231490","NEWT:244704","NEWT:7725","NEWT:430615","NEWT:72664","NEWT:326423","NEWT:452467","NEWT:198822","NEWT:36111","NEWT:326424","NEWT:1678078","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:150847","NEWT:431947","NEWT:69014","NEWT:142809","NEWT:302409","NEWT:130821","NEWT:27606","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:13443","NEWT:8644","NEWT:5141","NEWT:46360","NCBITaxon:3044782","NEWT:202914","NEWT:160235","NEWT:502779","NEWT:297246","NEWT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