{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074975/3332_using_predicted_HUMANc_MC1_NoVarMods_350_1250_mbr-lib.tsv.speclib","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074975/3332_using_predicted_HUMANc_MC1_NoVarMods_350_1250_mbr.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074975/3332_PRIDE.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074975/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074975/3332_using_predicted_HUMANc_MC1_NoVarMods_350_1250_mbr.log.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074975/RAWFiles_3332.zip"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["alexander.quaas@uk-koeln.de"],"submitter":["Proteomics Facility"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"disease":["Esophagus Adenocarcinoma"],"software":[""],"submitter_keywords":["smarca2","swi/snf complex","smarca4","proteomics","complement system","Esophageal adenocarcinoma; swi/snf complex; proteomics; smarca2; smarca4; complement system; cd55; cd59; dna repair","cd59","dna repair","Esophageal adenocarcinoma","cd55"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074975"],"tissue":["Inflammatory Cell","Esophagus","Interstitial Cell"],"sample_protocol":["FFPE tissue scrolls (roughly 100mm2 x 5 µm) were transferred to 100 µl tissue lysis buffer (TLB, Covaris) in an AFA-TUBE TPX 96 well Plate (Covaris). After sealing with strip caps, the plates were incubated at 95°C for 10 min in a thermocycler. For subsequent deparaffinization plates were transferred to a Covaris LE220-plus Focused-ultrasonicator and processed with 450 W peak power, 50% duty cycle and 200 cycles at 20°C for 5 min. To de-crosslink proteins, the samples were subsequently incubated at 95° for 90 min in a thermocycler and proteins were finally extracted by a second ultrasonication step in the Covaris LE220 using the settings described above. TCEP and chloroacetamide were added to final concentrations of 5 mM and 20 mM respectively to reduced disulfide bonds and alkylate cysteines. Samples were incubated for 20 min at 55°C in a Thermocycler. 50 µl of protein lysates were used for protein digestion following a modifies version of the single-pot solid phase enhanced sample preparation protocol (Hughes 2019). Hydrophilic and hydrophobic Sera-Mag carboxylate-modified magnetic particles (GE Healthcare) were combined 1:1, washed two times with 10 volumes of water and stored at 10 µg/µl. 2 µl of the bead mix were added to the samples and acetonitrile (ACN) was added to a final percentage of 50%. The mixture was incubated at 25°C for 8 min with shaking at 1400 rpm. The plates were placed on a magnetic rack for 2 min, supernatants were removed and the beads were washed with 180 µl prewarmed isopropanol at 55°C and 1400 rpm for 10 min. Supernatants were removed on a magnetic rack and the isopropanol washes were repeated four more times. Finally, the trapped beads were washed with 200 µl acetonitrile on the magnetic rack, air dried and reconstituted in 50 µl 50mM Triethylammonium bicarbonate (TEAB) containing 1 µg Trypsin. Proteins were digested for 16 h at 37°C in a Thermocycler. After digestion samples were acidified with 50 µl 5 % formic acid. Beads were trapped on a magnetic rack for 3 min and 90 µl supernatant containing the digested proteins were transferred to fresh plates. 5 µl of each sample were diluted with 15 ul 0.1 % formic acid and loaded on Evotips (Evosep) according to the manufacturer instructions."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Data processing A predicted spectral library was generated using a human canonical Swissprot fasta and DIA-NN 1.8.1 (Demichev 2020) using the following settings: Trypsin, up to 1 missed cleavage, precursor ion range 350 m/z – 1250 m/z, fragment ion range 200 m/z – 1700 m/z, charge states 2+, 3+ and 4+. Sample files were searched using this library in match between run (MBR) mode with default settings. Data Analysis Identifier and quantitative columns were extracted from the main DIA-NN output file and filtered. Normalised precursor quantities were used for MaxLFQ protein quantification in the DIANN R-package. Sample runs with precursor ID numbers above or below the upper or lower quartile +/- inter quartile range (4 out of 128) were regarded as outliers and removed. The protein LFQ intensities were imported into Perseus 1.6.15.0 and filtered for at least 50% data completeness. Missing values were imputed with random values from the lower end of the intensity distribution using Perseus defaults."],"omics_type":["Proteomics"],"labhead":["Alexander Quaas"],"instrument_platform":[""],"labhead_affiliation":["Institut für Pathologie Uniklinik Köln, Kerpener Straße 62, 50937 Cologne, Germany"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["proteomics-facility@uni-koeln.de"],"publication":["Not available"],"submitter_affiliation":["CECAD Research Center"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic Characterization of SMARCA-Deficient Esophageal Adenocarcinoma Reveals Complement Evasion and DNA Repair-Associated Prognostic Subgroups","description":"Background Esophageal adenocarcinoma (EAC) is an aggressive malignancy in which the SWI/SNF catalytic subunits SMARCA2 and SMARCA4 are frequently lost, yet the biological and clinical impact of these deficiencies remains unclear. Methods We analyzed 113 EAC specimens using mass spectrometry–based proteomics, including 89 SMARCA-deficient and 24 SMARCA-proficient tumors. Additional immunohistochemical studies were conducted on 98 cases. Differential expression, pathway enrichment, and survival analyses were used to characterize proteomic alterations and identify prognostic features. Results SMARCA-deficient tumors showed frequent expression of complement-inactivating proteins CD55 and CD59 with distinctive apical and membranous localization. SMARCA4-deficient patients had significantly poorer survival than both SMARCA2-deficient and SMARCA-proficient patients. Among neoadjuvantly treated SMARCA-deficient tumors, coordinated upregulation of DNA repair proteins separated patients into two prognostic subgroups. The DNA repair–low subgroup had markedly worse survival than both the DNA repair–high subgroup and SMARCA-proficient controls, whereas the DNA repair–high subgroup showed a trend toward improved outcomes. This DNA repair–associated pattern was not observed in neoadjuvantly treated SMARCA-proficient tumors. Conclusions SMARCA-deficient EAC comprises biologically distinct subgroups with prognostic proteomic signatures. CD55 and CD59 expression may contribute to resistance to antibody-based immunotherapies by complement evasion, while DNA repair profiles could guide post-surgical treatment in neoadjuvantly treated 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