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Vignane"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"software":["Not available"],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD045785"],"tissue":["Brain","Frontal Lobe"],"sample_protocol":["Sulfenylation enrichment for proteomic analysis Brain frontal cortexes were lysed in cold HEN Buffer (50 mM HEPES, 1 mM EDTA, 0.1 mM Neocuproine, 1 % IGEPAL, 2 % SDS, pH 7.4) supplemented with 1 mM Benzo[c][1,2]thiazine-based BTD (BTD). Frozen tissue was disrupted in lysis buffer using the TissueLyser II (Qiagen) and 5 mm Stainless steel beads (Qiagen, # 69989). Lysates were incubated for 2 h at 37 °C followed by two methanol/chloroform precipitations. Pellets were then washed twice with cold methanol and evaporated dry. Samples were then resuspended in HEPES + 2 % SDS and treated with 10 mM DTT for 1 h at 37 °C, followed by 40 mM Iodoacetamide (IAM) for 30 min at RT. Excess DTT and IAM were removed by methanol chloroform precipitation, and cell pellets were resuspended in 50 mM HEPES pH 7.0. 1.5 mg of proteins were incubated for 2 h at 37 °C with 0.2 mM Az-UV-Cleavable-biotin, 1 mM Ascorbic acid, and 0.1 mM Copper-TBTA to perform the click-chemistry reaction. Methanol/chloroform precipitation was performed to stop the reaction and remove excess reagent. After precipitation, pellets were resuspended in Streptavidin Binding buffer (50 mM NaOAc, pH 4.5) and 0.2 % SDS. Protein concentration was performed, and 0.9 mg of proteins were incubated with Pierce™ High Capacity Streptavidin Agarose beads (Thermofisher, #20357). After 3 h of mixing at RT, beads were collected and transferred into 2 mL Pierce™ Disposable Columns (Thermofisher, #29920). To remove unspecific bindings and detergent, beads were washed with Streptavidin washing buffer (50 mM NaOAc and 2 M NaCl, pH 4.5). After washing, sulfenylated proteins were released by incubating beads for 3 h under UV light (365 nm) in 25 mM Ammonium bicarbonate buffer (Sigma, #5.33003). After incubation, supernatants were collected using 2 mL Pierce™ Disposable Columns and subject to lyophilization. Proteins were digested and peptides desalted using Supel™-Select HLB SPE Tube and evaporated under vacuum until dryness. Peptides were dissolved in 0.1 % TFA, and digestion quality control was performed  as described above. Peptides were analyzed by high-resolution LC-MS/MS using an Ultimate 3000 Nano Ultra High-Pressure Chromatography (UPLC) system (Thermo Fisher Scientific) coupled with an Orbitrap Eclipse™ Tribrid™ Mass Spectrometer via an EASY-spray (Thermo Fisher Scientific). Peptide separation was carried out with an Acclaim™ PepMap™ 100 C18 column (Thermo Fisher Scientific) using a 65 min linear gradient from 3 to 35 % of B (84 % Acetonitrile, 0.1 % Formic Acid) at a flow rate of 250 nL/min. The Orbitrap Eclipse™ was operated in a DDA mode, and MS1 survey scans were acquired from m/z 300 to 1,500 at a resolution of 120, 000 using the Orbitrap mode. MS2 scans were carried out for 3 seconds with high-energy collision-induced dissociation (HCD) at 32 % using the Normal speed IonTrap mode.   Total proteome analysis As for PSSH and PSOH, Brain frontal cortexes were disrupted in lysis (50 mM TRIS, 150 mM NaCl, 2% SDS, 1% IGEPAL, pH 7.8) buffer using the Tissuelyser II (Qiagen) and twenty 1.4 mm ceramic beads (Qiagen, #13113). Lysates were then incubated with Benzonase following manufacturer recommendation for 30 min and precipitated using methanol/chloroform. Samples were then resuspended in 50 mM HEPES, 2 % SDS, and incubated with 10 mM DTT at RT followed by 50 mM IAM for 1h at 37°C. To stop the reaction, samples were then precipitated using methanol/chloroform. For tryptic digestion, samples were dissolved in 6 M Guanidine hydrochloride (Gua-HCl)., 250 µg of protein were digested overnight at 37 °C using trypsin with a 1:20 trypsin to sample ratio (Promega, #V5117). The next day, peptides were desalted using Supel™-Select HLB SPE Tube and evaporated under vacuum until dryness as described above.  Peptides were dissolved in 0.1 % TFA, and digestion quality control was performed using an Ultimate 3000 Nano Ultra High-Pressure Chromatography (UPLC) system with a PepSwift Monolithic® Trap 200 µm * 5 mm (Thermo Fisher Scientific). Peptides were analyzed by high-resolution LC-MS/MS using an Ultimate 3000 Nano Ultra High-Pressure Chromatography (UPLC) system (Thermo Fisher Scientific) coupled to a timsTOF Pro (Bruker) equipped with a CaptiveSpray source. Peptide separation was carried out with an Acclaim™ PepMap™ 100 C18 column (Thermo Fisher Scientific) using a 65 min linear gradient from 3 to 35 % of B (84 % Acetonitrile, 0.1 % Formic Acid) at a flow rate of 250 nL/min. The timsTOF Pro (Bruker) was operated in PASEF mode using Compass Hystar 5.0.36.0. The TIMS setting was as follows: Mass Range 100 to 1700 m/z, 1/K0 Start 1.6 Vs/cm2 End 1.6 Vs/cm2, Ramp time 100 ms, Lock Duty Cycle to 100 %, Capillary Voltage 1500V, Dry Gas 3 l/min, Dry Temp 180°C. PASEF settings: 10 MS/MS scans, charge range 0-5, active exclusion for 0.4 min, Scheduling Target intensity 20000, Intensity threshold 2500, CID collision energy 49 eV."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Sulfenylation enrichment Data analysis Data were evaluated with PEAKS ONLINE software using 15 ppm for precursor mass tolerance, 0.5 Da for fragment mass tolerance, specific tryptic digest, and a maximum of 3 missed cleavages. BTD –UV-cleavable probe (cleaved, +418.1311 Da), and carbamidomethylation (+57.021464 Da) on C, N-term Acetylation (+42.010565 Da), and methionine oxidation (+15.994915 Da) were added as variable modifications, PSM and proteins were filtered at FDR 1 %. Samples were then normalized using eigenMS(3) on R studio.    Total proteome data analysis Data were evaluated with PEAKS ONLINE software using 15 ppm for precursor mass tolerance, 0.05 Da for fragment mass tolerance, specific tryptic digest, and a maximum of 3 missed cleavages. Carbamidomethylation (+57.021464 Da) on C, N-term acetylation (+42.010565 Da), and methionine oxidation (+15.994915 Da) were added as variable modifications, PSM and proteins were filtered at FDR 1 %. Data was normalized based on the total ion count (TIC)."],"omics_type":["Proteomics"],"labhead":["Milos Filipovic"],"instrument_platform":[""],"labhead_affiliation":["SULFAGING lab, Leibniz institut für analytische wissenschaften, isas .ev, Germany"],"submission_type":["COMPLETE"],"species":["Mus Musculus (mouse)"],"submitter_mail":["thibaut.vignane@outlook.com"],"publication":["Not available"],"submitter_affiliation":["Leibniz-Institut für Analytische Wissenschaften - ISAS,e.V, Dortmund, Germany"],"submitter_country":["Germany"],"doi":["10.6019/PXD045785"],"additional_accession":[]},"is_claimable":false,"name":"Sulfenylation and total proteome changes analysis aging Brain of WT, CSE-/- and MPST-/- mice","description":"Cellular homeostasis relies on precise regulation through chemical processes, such as protein posttranslational modifications and physical processes, such as biomolecular condensation. Aging disrupts this balance, increasing susceptibility to diseases and death. However, the mechanisms behind age-related pathogenesis remain unclear. Using chemoproteomic methods to dissect different cysteine posttranslational modifications, we found that age-related changes in cysteine redox homeostasis impact proteins ability to form biomolecular condensates. Age-related increase in sulfenylation and sulfonylation promotes phase separation and through conformational change increases proteins propensity to aggregate. Causing condensates dissolution, protein persulfidation, a protective thiol modification, prevents this. Reduced persulfidation and increased sulfonylation in aging drive abnormal phase separation, leading to shorter life and spontaneous protein aggregation in CSE-/- mice.  In this study, we assessed the changes in protein sulfenylation levels in brain aging. For this, we used the frontal cortex of 10 weeks, 10 months and 18 months-old WT mice . To unravel the protective role of H2S against ROS, we used two other knockouts mice: Cystathionine-gamme-lyase (CSE) knockout and 3-mercaptosulfure transferase (MPST) knockout, both proteins being responsible for H2S production.","dates":{"publication":"2026-05-23","submission":"2023-09-28"},"accession":"PXD045785","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:1073882","NEWT:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","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:110368","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:419481","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:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","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:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","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:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","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:51338","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:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:48106","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300273","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255"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