{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/peptides.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/proteinGroups.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/20260408_HB_8_MVR_Batch1_sample8_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/20260408_HB_16_MVR_Batch1_sample16_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/20260408_HB_7_MVR_Batch1_sample7_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/20260408_HB_16_MVR_Batch1_sample16_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/20260408_HB_7_MVR_Batch1_sample7_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/20260408_HB_8_MVR_Batch1_sample8_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/20260408_HB_12_MVR_Batch1_sample12_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/20260408_HB_7_MVR_Batch1_sample7_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/20260408_HB_8_MVR_Batch1_sample8_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/20260408_HB_12_MVR_Batch1_sample12_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/20260408_HB_12_MVR_Batch1_sample12_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/20260408_HB_16_MVR_Batch1_sample16_3.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/uniprotkb_proteome_UP000005640_2026_04_26.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080543/Skyline_KEAP.sky"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["marcusn@ruc.dk"],"submitter":["Marcus Nielsen"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Human","Qe-plus"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD080543"],"tissue":["Hepatocyte","Cell Culture"],"sample_protocol":["Sample preparation. Protein extraction was performed using a denaturing lysis buffer containing 6 M GndHCl, 5 mM TCEP, 10 mM CAA, and 100 mM Tris-HCl at pH 8.5 and heated to 99 °C prior to use. Protein pellets were resuspended in 200 µL of the hot denaturation buffer and the samples were sonicated. Protein content was measured by NanoDrop (Thermo Fisher Scientific) at 280 nm. Samples were diluted with 25 mM Tris-HCl (pH 8.0) to a final protein content 200 µg, and trypsin was added at a ratio of 1:50 (w/w), corresponding to 4 µg. Digestion was carried out overnight at 37 °C with shaking. The reaction was quenched by adding 10% formic acid to a final concentration of 0.1% (v/v), followed by centrifugation at 14,000 rpm for 20 minutes to remove insoluble material. Peptide cleanup was performed using SepPak 1cc C18 SPE cartridges, which were conditioned with 1 mL ACN followed by 2 × 1 mL of 0.1% FA. The sample supernatant was loaded onto the cartridge, followed by washing with 2 × 500 µL of 0.1% FA, and peptides were eluted using 400 µL of 40% ACN followed by 400 µL of 60% ACN. Eluted peptides were dried completely using SpeedVac (Thermo Fisher Scientific) and stored at 4°C until further processing. Dried peptides were dissolved in 50 µL of aqueous 3% ACN and 0.1% FA, the peptide content was measured, and the solution was diluted to 250 ng/ul in the same diluent. Adjusted samples were then transferred to MS vials and placed in the autosampler for subsequent MS analysis. LC-MS analysis. Peptides were trapped on a PepMap™ C18 column (5 μm, 300 μm, 5 mm; Thermo Fisher Scientific) with 100 Å pores and separated on a RP EASY-Spray C18 column (2 μm, 75 μm, 50 cm; Thermo Scientific™) with 100 Å pores on an Ultimate 3000™ RSLCnano UHPLC system connected to a Q Exactive™ Plus Hybrid Quadrupole-Orbitrap™ mass spectrometer (Thermo Fisher Scientific). Two mobile phases were utilized: Buffer A (0.1% formic acid in MilliQ H2O) and buffer B (90% ACN, 0.1% formic acid in MilliQ H2O). Technical triplicates were run with a sample injection volume of 2 µL and the peptides were trapped for 3 min with 100% buffer A at a flow rate of 30 µL/min. The peptides were then separated on the analytical column with a 110 min gradient with increasing ratio of buffer B going from 1% to 40% in 80 min, 40% to 95% in 10 min, remain at 95% for 5 min, 95 to 5% in 50 min followed by a 10 min wash and re-equilibrating step. All steps were performed at a flow rate of 250 nL/min. The Q Exactive™ Plus Hybrid Quadrupole-Orbitrap™ was operated in data-dependent top 20 mode. Full scan mass spectra were recorded in the Orbitrap™ at a resolution of 70,000 at m/z 200 over the m/z range 375–1600 with a target AGC value of 3 × 10E6 and a maximum injection time of 15 ms. HCD-generated product ions were recorded with a maximum ion injection time set to 45 ms and an AGC target value set to 1 × 10E5. Spray voltage was set to 2.2 kV, S-lens RF level at 50, and heated capillary at 280°C. Normalized collision energy was set at 30 and the isolation window was 1.2 m/z."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data was processed using MaxQuant v.2.8.0.0 using the uniprot reference human proteome, and an FDR of 0.05. MGO-H1, MGO-DH, and CEL were added as variable modifications and otherwise standard settings were used. Further processing was done in Perseus v.2.1.6.0.  Manual analysis was done in Skyline 26.1.0.057 55. Standard settings were used, except carbamidomethyl was added as a non-variable modification, and MGO-H1, MGO-DH, CEL, and oxidation as variable modifications, with a maximum of 5 modification/peptide. Precursor charges of 2, 3, and 4 were searched, with up to 2 missed cleavages. Peptides were sorted descendingly by idotp values, and isotopic patterns, retention times, mass accuracies, in-source fragmented transitions, etc., were manually reviewed to identify the likelihood of correct identification of the peptides."],"omics_type":["Proteomics"],"labhead":["Marcus Nielsen"],"instrument_platform":[""],"labhead_affiliation":["Roskilde University, Department of Science and Environment, Denmark"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["marcusn@ruc.dk"],"publication":["Not available"],"submitter_affiliation":["Roskilde university"],"submitter_country":["Denmark"],"additional_accession":[]},"is_claimable":false,"name":"Crosstalk between S-nitrosylation and glycation defines a novel  metabolic vulnerability in liver and renal cancers","description":"Methylglyoxal (MGO)-derived advanced glycation end products (AGEs) are hallmarks of carbonyl stress and contribute to cancer progression. Here, we established and validated an LC–MS/MS workflow to detect MGO-induced protein modifications in wild-type (WT) and AKR1A1 knockout (KO) Huh7 cells. Following MGO treatment, proteins were digested and analyzed by liquid chromatography–tandem mass spectrometry to identify characteristic glycation products, including methylglyoxal-derived hydroimidazolone (MG-H1) and Nε-(1-carboxyethyl)-L-lysine (CEL). Comparative analysis demonstrated increased accumulation of MGO-derived modifications in AKR1A1 KO cells compared with WT cells, consistent with impaired detoxification of reactive dicarbonyl species. These findings validate a robust LC–MS/MS workflow for profiling MGO-mediated protein glycation and support its application for investigating carbonyl stress in cancer 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