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Then, the supernatant was transferred to a new centrifuge tube. The top 14 high abundance proteins were removed by Pierce™ Top 14 Abundant Protein Depletion Spin Columns Kit (Thermo Fisher). Finally, the protein concentration was determined with BCA kit according to the manufacturer’s instructions. 2.Trypsin Digestion The protein solution was reduced with 5 mM dithiothreitol for 30 min at 56 °C and alkylated with 11 mM iodoacetamide for 15 min at room temperature in darkness. The alkylated samples were transferred to ultrafiltration tubes for FASP digestion. The samples were firstly replaced with 8 M urea for 3 times at 12000 g at room temperature for 20 min, and then replaced with 200 mM TEAB for 3 times. Trypsin was added at 1:50 trypsin-to-protein mass ratio for digestion overnight. The peptide was recovered by centrifugation at 12000 g for 10 min at room temperature, and repeated for two times. Finally, the combined peptides were desalted by Strata X SPE column. 3.TMT Labeling The project did not do TMT labeling. 4. HPLC Fractionation The project is not HPLC rated. 5. Affinity Enrichment There is no enrichment method for this project."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["1. LC-MS/MS Analysis For protein extraction, the samples were stored at -80°C and centrifuged at 4°C at 12,000 × g for 10 min to remove cellular debris. The supernatant was then transferred to a new centrifuge tube. High-abundance proteins were depleted using the Pierce™ Top 14 Abundant Protein Depletion Spin Column Kit (Thermo Scientific), following the manufacturer's instructions. The total protein concentration was determined using a BCA assay kit. Equal amounts of protein from each sample were used for enzymatic digestion. The sample volume was adjusted for consistency using lysis buffer. Dithiothreitol (DTT) was added to a final concentration of 5 mM, and protein reduction was performed at 56°C for 30 min. Subsequently, iodoacetamide (IAA) was added at a final concentration of 11 mM, and the alkylation reaction proceeded at room temperature in the dark for 15 min. The alkylated samples were transferred to ultrafiltration tubes, centrifuged at 12,000 × g for 20 min at room temperature, and exchanged three times with 8 M urea, followed by three exchanges with replacement buffer. Trypsin was then added at a proteinase-to-protein ratio of 1:50 (m/m), and digestion was performed overnight. Peptides were recovered by centrifugation at 12,000 × g for 10 min at room temperature, followed by an additional recovery wash with ddH2O. The combined peptide solutions were stored for further use. 2. Mass Spectrometry Analysis Tryptic peptides were dissolved in solvent A (0.1% formic acid, 2% acetonitrile in water) and directly loaded onto a custom-made reversed-phase analytical column (25-cm length, 100 μm i.d.). The mobile phase consisted of solvents A and B (0.1% formic acid and 90% acetonitrile in water). Peptide separation was achieved using a sophisticated gradient on an EASY-nLC 1200 UPLC system (Thermo Fisher Scientific, Waltham, MA, USA) at a constant flow rate of 500 nl/min. The gradient program was as follows: 0-16 min, 7%-20%B; 16-24 min, 20%-32%B; 24-27 min, 32%-80%B; 27-30 min, 80%B. The separated peptides were analyzed using an Orbitrap Exploris 480 mass spectrometer equipped with a nanoelectrospray ion source. An electrospray voltage of 2300 V was applied. High-Field Asymmetric-waveform Ion Mobility Spectrometry (FAIMS) compensation voltages (CV) were precisely set at -45V and -70V. Both the precursors and fragments were analyzed using an Orbitrap detector. The full MS scan resolution was set to 30000 for the scan range of 390-810 m/z. MS/MS scanning was performed with a fixed first mass of 200 m/z at a resolution of 30000. Higher-energy Collisional Dissociation (HCD) fragmentation was performed at normalized collision energies (NCE) of 25%, 30%, and 35%. The automatic gain control (AGC) target was set at 3E6, with the maximum injection time set to Auto. 3.Database processing The Data-Independent Acquisition (DIA) data were meticulously processed using Spectronaut (v.17) software. Tandem mass spectra were searched against H. sapiens_9606_SP_20230103. fasta database contains 20389 entries. This database was concatenated with a reverse decoy database. Trypsin/P was specified as the cleavage enzyme, allowing for up to two missing cleavages. Carbamidomethylation of cysteine residues was specified as a fixed modification, while acetylation of protein N-terminals and oxidation of methionine residues were specified as variable modifications. A stringent false discovery rate (FDR) of less than 1% was applied at the protein, peptide, and Peptide Spectrum Match (PSM) levels."],"omics_type":["Proteomics"],"labhead":["Yueying Wang"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Clinical Laboratory, The First People’s Hospital of Zhaoqing"],"species":["Homo Sapiens (human)"],"publication":["42365246 Lin Z, Song W, Liang W, Liu J, Gan R, Wang Y. Potential evaluation of SULT1A3 as an early diagnostic marker for nasopharyngeal carcinoma: a study based on serum proteomics screening and ELISA validation. BMC Cancer. 2026 26(1):1091 10.1186/s12885-026-16428-x"],"submitter_mail":["wangyueyinggd@126.com"],"submitter_affiliation":["The First People’s Hospital of Zhaoqing"],"submitter_country":["China"],"pubmed_abstract":["<h4>Background</h4>Nasopharyngeal carcinoma (NPC) represents a highly prevalent and aggressive malignancy endemic to Southeast Asia. Early and accurate diagnosis is critical to improving survival outcomes; however, the absence of robust, stage-specific biomarkers remains a key obstacle to clinical implementation of early screening strategies.<h4>Methods</h4>We performed untargeted serum proteomic profiling using mass spectrometry in 15 treatment-naïve early-stage NPC patients and 15 VCA-IgA-positive healthy controls. Bioinformatics analyses were conducted to identify differentially expressed proteins (DEPs). Machine learning (random forest combined with recursive feature elimination) was employed to prioritize candidate biomarkers, which were subsequently verified using enzyme-linked immunosorbent assay (ELISA) in independent sample cohorts.<h4>Results</h4>In total, 1,428 serum proteins were identified, among which 1,410 were reliably quantified. We observed 31 upregulated and 189 downregulated proteins in NPC patients relative to controls. Spearman correlation analysis revealed significant associations: LTA4H (leukotriene A4 hydrolase) levels correlated with serum cell infiltration (r = 0.383, p = 0.032) and CD8 + T-cell abundance (r = 0.408, p = 0.021); both SULT1A3 (sulfotransferase family 1 A member 3) and FGL1 (fibrinogen-like protein 1) levels were positively associated with M1 macrophage infiltration (r = 0.510, p = 0.003 and r = 0.430, p = 0.015, respectively). In a preliminary validation cohort (n = 80), ELISA yielded AUC values of 0.631 (95% CI: 0.515-0.736, p = 0.04) for LTA4H, 0.787 (95% CI: 0.681-0.871, p < 0.001) for SULT1A3, and 0.688 (95% CI: 0.575-0.787, p = 0.002) for FGL1. In large-scale independent validation, SULT1A3 achieved an AUC of 0.826 (95% CI: 0.766-0.876; sensitivity = 78.89%, specificity = 75.47%) in cohort 1 (n = 196) and 0.796 (95% CI: 0.723-0.857; sensitivity = 76.67%, specificity = 76.67%) in cohort 2 (n = 150).<h4>Conclusions</h4>Through an integrated workflow combining proteomic screening, machine learning prioritization, and multi-stage ELISA validation, we identified SULT1A3 as a candidate serum-based biomarker for early detection of NPC. Preliminary findings suggest that SULT1A3 may have potential utility in clinical screening, though further validation in independent, multi‑center cohorts is required."],"pubmed_title":["Potential evaluation of SULT1A3 as an early diagnostic marker for nasopharyngeal carcinoma: a study based on serum proteomics screening and ELISA validation."],"pubmed_authors":["Lin Zhifang Z, Song Wei W, Liang Wenhai W, Liu Jian J, Gan Ruiwei R, Wang Yueying Y"],"additional_accession":[]},"is_claimable":false,"name":"Early Diagnostic Marker for Nasopharyngeal Carcinoma: A Study Based on Serum Proteomics Screening and ELISA Validation","description":"This study focuses on the critical challenge of early NPC detection, underscored by the observation that only 15.8% of newly diagnosed cases were identified at an early stage in our institution between 2019 and 2020. Current screening methods, especially those relying on EBV antibody detection, demonstrate suboptimal sensitivity and low positive predictive value. These limitations not only cause unnecessary psychological distress in healthy individuals but also lead to the inefficient allocation of healthcare resources. Consequently, improving the sensitivity and positive predictive value of early NPC screening is of utmost clinical significance. We propose an innovative methodological framework that integrates state-of-the-art mass spectrometry and proteomic technologies for the systematic identification of potential serum biomarkers in NPC. Our approach incorporates the \"Blood+\" detection platform, which synergistically combines Field Asymmetric Ion Mobility Spectrometry (FAIMS) with advanced machine learning algorithms, thereby enhancing both detection sensitivity and analytical reliability for large-scale sample processing. The research methodology was structured into three sequential phases: (1) initial biomarker discovery using high-throughput small-sample screening techniques, (2) preliminary validation via small-scale ELISA analysis, and (3) comprehensive confirmation through large-scale ELISA validation. This systematic investigation is expected to provide robust data to support NPC screening initiatives with the potential to improve early detection accuracy, reduce false-positive rates associated with EBV antibody testing, alleviate patient psychological distress, and optimize clinical outcomes.","dates":{"publication":"2026-09-21","submission":"2026-04-29"},"accession":"PXD077783","cross_references":{"TAXONOMY":["NEWT:3555","NEWT:71647","NEWT:330879","NEWT:260201","NEWT:35554","NCBITaxon:12939","NEWT:32046","NEWT:544496","NEWT:59529","NEWT:2042546","NEWT:32049","NEWT:1392696","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:45351","NEWT:445974","NEWT:43179","NEWT:180454","NEWT:5722","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:10245","NEWT:55153","NEWT:89184","NEWT:10244","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:351581","NEWT:43186","NEWT:428146","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:498019","NEWT:1351","NEWT:1438992","NEWT:1352","NEWT:2649997","NEWT:1147161","NEWT:661410","NEWT:638632","NEWT:263737","NEWT:224326","NEWT:1333499","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:5702","NEWT:95648","NEWT:1589","NEWT:135622","NEWT:1349","NEWT:67352","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:383379","NEWT:1401257","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:44491","NEWT:641809","NEWT:27933","NEWT:556484","NEWT:317447","NEWT:4688","NEWT:7955","NEWT:111225","NEWT:7719","NEWT:7959","NEWT:2261","NEWT:868565","NEWT:94323","NEWT:31156","NEWT:3112","NEWT:79329","NEWT:4442","NEWT:31155","NEWT:192875","NEWT:1214915","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:284218","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:1316931","NEWT:224308","NEWT:3347","NEWT:511145","NEWT:160621","NEWT:212790","NEWT:931281","NEWT:4432","NEWT:5762","NEWT:5763","NEWT:658457","NEWT:1310161","NEWT:77133","NEWT:295358","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:2246","NEWT:2652724","NEWT:1912919","NEWT:5757","NEWT:68415","NCBITaxon:4563","NEWT:5755","NEWT:44688","NEWT:44689","NEWT:44447","NEWT:752555","NEWT:498211","NEWT:5759","NEWT:347256","NEWT:1736231","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:1392","NEWT:498217","NEWT:498216","NEWT:2242","NEWT:11320","NEWT:286","NEWT:391619","NEWT:246196","NEWT:287","NEWT:246197","NEWT:1367269","NEWT:145458","NEWT:633149","NEWT:1149786","NEWT:10239","NEWT:68895","NEWT:44685","NEWT:161934","NEWT:4897","NEWT:1148","NEWT:5744","NEWT:72901","NEWT:213863","NEWT:5508","NEWT:3329","NEWT:5507","NEWT:410661","NEWT:55571","NEWT:35500","NEWT:1235816","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:4896","NEWT:1287689","NEWT:1390","NEWT:11557","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:294","NEWT:1773","NEWT:1182590","NEWT:3712","NEWT:82380","NEWT:3711","NEWT:935293","NEWT:375146","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:1772","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:263","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:11988","NEWT:284812","NEWT:8175","NEWT:400667","NEWT:43330","NEWT:980415","NEWT:1603293","NEWT:408169","NEWT:44664","NEWT:47946","NEWT:459758","NEWT:3702","NEWT:1245466","NEWT:243277","NEWT:1246791","NEWT:7067","NEWT:118694","NEWT:586722","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:274","NEWT:7070","NCBITaxon:287","NEWT:408172","NEWT:408170","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1436733","NEWT:460519","NEWT:1247411","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1303443","NEWT:9483","NEWT:333760","NEWT:34607","NEWT:56636","NEWT:1513458","NEWT:1233681","NEWT:2709072","NCBITaxon:40559","NEWT:506599","NEWT:2853422","NEWT:81077","NEWT:84588","NEWT:1679718","NEWT:480","NEWT:65349","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:300852","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:508771","NEWT:1883446","NEWT:253","NCBITaxon:2759","NEWT:1233435","NEWT:93061","NEWT:93062","NEWT:34613","NCBITaxon:4932","NEWT:109760","NEWT:29031","NEWT:943274","NEWT:644223","NEWT:235443","NEWT:108458","NEWT:5936","NEWT:272623","NEWT:272624","NEWT:320637","NEWT:2719099","NEWT:886559","NEWT:3750","NEWT:55521","NEWT:983964","NEWT:118499","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:1130798","NEWT:55529","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:476272","NEWT:3747","NEWT:195051","NEWT:3988","NEWT:1116234","NEWT:561007","NEWT:1255228","NEWT:649908","NEWT:410289","NEWT:373153","NEWT:3983","NEWT:203696","NEWT:472","NEWT:352472","NEWT:97441","NEWT:1071661","NEWT:1202531","NEWT:1202532","NEWT:360094","NEWT:1408223","NEWT:470","NEWT:1408224","NEWT:41364","NEWT:5911","NEWT:1313","NEWT:1218097","NEWT:1080348","NCBITaxon:50557","NEWT:1314","NEWT:39251","NEWT:39491","NEWT:212142","NCBITaxon:5811","NEWT:29491","NEWT:101841","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:571256","NEWT:40483","NEWT:63366","NEWT:63367","NEWT:688333","NEWT:215402","NCBITaxon:548681","NEWT:318586","NCBITaxon:5820","NEWT:1547","NEWT:272634","NEWT:198107","NEWT:9031","NEWT:27292","NEWT:1872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