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":["alessandra.altomare@unimi.it"],"submitter":["Alessandra Altomare"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Ulcerative Colitis"],"software":[""],"submitter_keywords":["nf-κb","4-hydroxy-2-nonenal (hne)","nrf2 activation","Carnosine; 4-hydroxy-2-nonenal (hne); nrf2 activation; nf-κb; anti-inflammatory; anti-oxidant.","anti-inflammatory","Carnosine","anti-oxidant."],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075159"],"tissue":["Colon"],"sample_protocol":["Tissue samples were processed using a standardized bottom-up proteomics workflow designed to maximize extraction efficiency and ensure comparability across experimental groups. Briefly, frozen tissue specimens were transferred to dedicated microvials preloaded with zirconia beads and homogenized on a benchtop bead-mill system to achieve rapid and reproducible mechanical disruption. The resulting tissue lysates/homogenates were collected and, where necessary, clarified to remove insoluble debris. Total protein yield was then determined by protein quantification, and equal protein amounts were normalized prior to digestion to minimize technical variability introduced at the sample preparation stage.  For proteolytic digestion, proteins were processed using the S-Trap approach, which enables efficient detergent removal and rapid enzymatic digestion. Protein extracts were loaded onto S-Trap micro spin columns following the manufacturer’s recommendations, allowing protein capture within the quartz-fiber matrix and subsequent on-column cleanup. Bound proteins were then digested by on-column trypsinization, generating peptides under controlled conditions that support high digestion efficiency and reduced carryover of matrix components. Following digestion, peptides were eluted from the S-Trap columns and subjected to an additional cleanup/desalting step using C18 ZipTip solid-phase extraction. This step was performed to remove salts and residual contaminants and to concentrate peptide mixtures, thereby improving chromatographic performance and electrospray stability.  Purified peptides were analyzed by nano-flow liquid chromatography coupled to high-resolution tandem mass spectrometry (nanoLC–HRMS/MS) using an Orbitrap Fusion Tribrid mass spectrometer (Thermo Scientific). Peptide separation was performed under nanoLC conditions prior to ionization by nano-electrospray. The mass spectrometer was operated in data-dependent acquisition (DDA) mode, selecting the top 20 most intense precursor ions detected in each MS1 survey scan for fragmentation and MS/MS acquisition (Top20 method). Raw LC–MS/MS files were subsequently processed through the established bioinformatics pipeline for peptide/protein identification and downstream quantitative analysis."],"repository":["pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw LC–MS/MS files acquired in DDA mode were processed according to a standard label-free quantitative (LFQ) proteomics workflow. Data were analyzed using MaxQuant for peptide/protein identification and LFQ intensity extraction. Spectra were searched against the Mus musculus reference proteome database (target–decoy strategy enabled) to support reliable error estimation. Peptide-spectrum matches and protein identifications were filtered at a 1% false discovery rate (FDR) at both PSM and protein levels. Protein inference was performed using MaxQuant protein grouping, and quantitative values were obtained as LFQ intensities computed with the MaxLFQ algorithm, including across-run normalization. The Match Between Runs feature was enabled to increase identification depth by transferring peptide IDs across LC–MS runs based on accurate mass and aligned retention time. Only proteins supported by unique and/or razor peptides were retained for quantification, while common contaminants, reverse (decoy) entries, and “only identified by site” features were excluded prior to statistical evaluation. Downstream statistical analysis was performed in Perseus using the MaxQuant output tables. LFQ intensities were log2-transformed, and proteins were filtered to retain those quantified in the majority of replicates in at least one condition. Where required for comparative statistics, missing values were imputed (e.g., using a left-shifted normal distribution to model values close to the detection limit). Differential abundance testing was carried out using standard approaches (e.g., two-sample t-test with multiple-testing correction such as Benjamini–Hochberg FDR), accompanied by exploratory multivariate analyses including PCA, hierarchical clustering, and volcano plots. Functional interpretation of the resulting regulated protein sets was subsequently performed using dedicated bioinformatics tools for pathway enrichment and network-based analyses."],"omics_type":["Proteomics"],"labhead":["Alessandra Altomare"],"instrument_platform":[""],"labhead_affiliation":["University of MIlan - Department of Pharmaceutical Sciences"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["alessandra.altomare@unimi.it"],"publication":["41897532 Altomare A, Baron G, Gado F, Vedova LD, Ferrario G, Davani L, Gilardoni E, Ferrisi R, Mocchetti C, Singh L, Courten B, Carini M, Siracusa R, D'Amico R, Di Paola R, Dallanoce C, Impellizzeri D, Aldini G. The Carnosine-HNE Michael Adduct as a Redox-Active Species Associated with Nrf2-Dependent Antioxidant and Anti-Inflammatory Responses. Antioxidants (Basel). 2026 15(3):388 10.3390/antiox15030388"],"submitter_affiliation":["University of Milan (DISFARM)"],"submitter_country":["Italy"],"additional_accession":[]},"is_claimable":false,"name":"The Carnosine–HNE Michael Adduct as a Redox-Active Species Associated with Nrf2-Dependent Antioxidant and An-ti-Inflammatory Responses","description":"Carnosine (CAR), an endogenous histidine-containing dipeptide, exhibits antioxidant and anti-inflammatory activity in various experimental models; however, its molecular mechanism of action remains poorly understood. Here, we demonstrate that the Michael adduct between CAR and 4-hydroxy-2-nonenal (HNE), which has been detected in previ-ous studies in both in vitro and in vivo settings, mediates its bioactivity, particularly anti-oxidant and anti-inflammatory responses through Nrf2 activation. CAR-HNE adduct was synthesized and its physicochemical, metabolic, and biological properties were evaluated. CAR-HNE exhibited high stability in biological matrices and retained the ability to trans-fer HNE to thiol nucleophiles at a slow rate under physiologically relevant conditions, consistent with electrophile-mediated Nrf2 activation. This kinetic behavior limits the cy-totoxicity typically associated with free HNE while preserving redox signaling capacity. CAR-HNE induced dose-dependent Nrf2 activation and NF-κB inhibition in cell-based assays without the hormetic toxicity observed for free HNE. Mechanistically, CAR-HNE may act as a redox-tunable electrophilic reservoir, restoring nucleophilic tone and modu-lating redox-sensitive transcription factors. In vivo, CAR-HNE attenuated DSS-induced colitis more effectively than equimolar doses of either carnosine or HNE alone. Proteomic analyses revealed modulation of canonical Nrf2-dependent antioxidant pathways. Our findings suggest a conceptual shift in carnosine biology: rather than acting as a classical antioxidant or carbonyl quencher, carnosine functions as a precursor of redox-active elec-trophilic adducts that transduce anti-inflammatory and antioxidant responses via con-trolled RCS signaling.","dates":{"publication":"2026-04-06","submission":"2026-03-03"},"accession":"PXD075159","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:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:351581","NEWT:43186","NEWT:428146","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:43150","NEWT:263737","NEWT:224326","NEWT:1333499","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:5702","NEWT:95648","NEWT:1589","NEWT:135622","NEWT:1349","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:7719","NEWT:7959","NEWT:2261","NEWT:868565","NEWT:135674","NEWT:94323","NEWT:31156","NEWT:3112","NEWT:79329","NEWT:4442","NEWT:192875","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: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: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:1603293","NEWT:408169","NEWT:44664","NEWT:47946","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:9238","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:9483","NEWT:333760","NEWT:485","NEWT:34607","NEWT:56636","NEWT:1513458","NEWT:1233681","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: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:1748","NEWT:109760","NEWT:29031","NEWT:943274","NEWT:644223","NEWT:1263082","NEWT:235443","NEWT:108458","NEWT:5936","NEWT:272623","NEWT:272624","NEWT:320637","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:1154756","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:1499105","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:1872122","NEWT:1308","NEWT:7091","NEWT:1034015","NEWT:760568","NEWT:141262","NEWT:108931","NEWT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