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The extracts were diluted accordingly so all samples had the same concentration with 15 μg of proteins resolved by reducing, one dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis (1D SDS-PAGE), to a point of entering the separating gel (maximal path up to 5 mm of 14% SDS-PA gel).  Gels were stained with CBB R-250, and for the shotgun in-gel digestion, gel bands containing all proteins were excised from the gel, reduced by 10 mM dithiothreitol, afterwards alkylated with 55 mM iodoacetamide and finally digested with proteomics-grade trypsin (Sigma-Aldrich, Taufkirchen, Germany) in a 1:30 enzyme to substrate ratio, overnight at 37℃ (Shevchenko, Tomas, Havlis, Olsen, & Mann, 2006). Trypsin digests were cleaned and desalted with HyperSep tips C18 (Thermo Scientific, Rockwood, TN, USA), evaporated and reconstituted in 20 μL of 0.1% aqueous solution of formic acid. Tryptic peptides in 1 µL injection volume and with approximately 375 ng in each sample were chromatographically separated with nLC system UltiMate 3000 (Thermo Scientific, Waltham, Massachusetts, USA) using A) 0.1 % formic acid in water, and B), 0.1 % formic acid in acetonitrile as the mobile phase, using a 5–70% – 95% B gradient at a flow rate of 250 nL/min lasting 88 min. Peptides were analysed using Orbitrap ExplorisTM 240 (Thermo Scientific Inc., Bremen, Germany) in the data-dependent mode with the 20 most intense precursors subjected to fragmentation by collision-induced dissociation (HCD 30%). Scan range in m/z was set to 350-1400, resolution of the full MS1 scan was 60000 and for MS2 15000, isolation window (m/z) was 1.4, normalized automatic gain control targets of MS1 and MS2 were 300% and 200% respectively, while maximum injection time was the same for both scans, e.g. 25 ms. Dynamic exclusion was set to 3 sec after the first repetition ion event."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["BEAS-2B proteins were identified with the PEAKS X Pro platform (Bioinformatics Solution Inc., Ontario, Canada) and its PTM algorithm against a UniProtKB database (http://www.uniprot.org/) of Homo sapiens species (taxon ID 9606, 42379 sequences, and accessed 29/11/2022) and contamination database as common Repository of Adventitious Protein entries (http://www.thegpm.org/, 116 sequences, accessed 18/10/2019). Oxidation (Met) and deamidation (Gln, Asn) were considered as variable modifications, with carbamidomethylation (Cys) set as fixed in the PEAKS DB algorithm. In the PEAKS PTM algorithm, an unrestricted protein modification search was undertaken using an available list of 313 PMs from Unimod database. Up to two missed trypsin cleavages with non-specific cleavages at one end (semi-specific mode of action) of a peptide were allowed. Mass tolerances were set to ± 10 ppm for parent ions and ± 0.02 Da for fragment ions. Protein filters were as follows: protein −10 log P ≥ 20, protein unique peptides ≥ 2, and “A” Score for confident PMs identification of at least 50. Peptide filters were as follows: false discovery rate for peptide-spectrum matches < 0.1%; therefore, the resulting false discovery rate of the peptide sequence was lower than 0.5%, and de novo alignment local confidence score was ≥ 80%. The quantity of identified BEAS-2B proteins was compared by label free quantification (LFQ) using the PEAKS Q algorithm. The term “PTM profiling” means relative extent of the modifications within a single sample. Relative LFQ of proteins and PTMs in five treatment groups with three biological replicates per group was done as described previously [36,65]. Briefly, in LFQ section, cut off filter criteria for defining confident differently regulated proteins were a significance score of 20 (-10logP, p<0.01) and 2-fold change in log2 up/down ratio, comparing any of the treatments in respect to the control group."],"omics_type":["Proteomics"],"labhead":["Tanja Cirkovic Velickovic"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["University of Belgrade - Faculty of Chemistry"],"species":["Homo Sapiens (human)"],"submitter_mail":["katarinas@chem.bg.ac.rs"],"publication":["41892316 Trifunovic S, Kušić-Tišma J, Smiljanić K, Divac Rankov A, Dinić J, Ljujić M. Acute E-Cigarette Aerosol Condensate Exposure Disrupts the Transcriptome and Proteome Profiles of Human Bronchial Epithelial BEAS-2B Cells. Cells. 2026 15(6):525 10.3390/cells15060525"],"submitter_affiliation":["Senior Research Associate at University of Belgrade-Faculty of Chemistry, Center of Excellence for Molecular Food Sciences"],"submitter_country":["Serbia"],"doi":["10.6019/PXD072831"],"pubmed_abstract":["The growing popularity of electronic cigarettes (e-cigarettes) necessitates a better understanding of their biological effects. In this study, we aimed to evaluate the effects of e-cigarette aerosol condensates generated from either e-cigarette carrier liquid alone or with e-cigarette liquid with nicotine and flavor on bronchial epithelial cells. BEAS-2B cells were exposed to e-cigarettes for 24 h, and transcriptional and proteomic profiling, including assessment of protein modifications, was performed. Additionally, cell-based assays were used to evaluate mitochondrial function, rate of protein synthesis, lysosomal signal, lipid droplet quantity and actin formation. Our findings reveal that short-term exposure to both types of aerosol condensates altered transcriptome and proteome profiles, disrupting cellular homeostasis in BEAS-2B cells through impaired proteostasis and mitochondrial function in response to both types of condensates. Changes in lipid and lysosome content, as well as a reduction in polymerized actin, were observed with nicotine- and flavor-containing condensate. E-cigarette exposure also induced irreversible protein modifications, including different chemical derivatives (25 out of 49 in nicotine/flavor condensate; 20 out of 48 in nicotine/flavor-free condensate; 4 out of 35 in control), suggesting their particularly harmful effect. Together, these findings point to early-onset cellular stress and impaired lung epithelial fitness caused by acute e-cigarette exposure."],"pubmed_title":["Acute E-Cigarette Aerosol Condensate Exposure Disrupts the Transcriptome and Proteome Profiles of Human Bronchial Epithelial BEAS-2B Cells."],"pubmed_authors":["Trifunovic Sara S, Kušić-Tišma Jelena J, Smiljanić Katarina K, Divac Rankov Aleksandra A, Dinić Jelena J, Ljujić Mila M"],"additional_accession":[]},"is_claimable":false,"name":"Acute e‑cigarette aerosol condensate exposure alters the transcriptome and proteome of human bronchial epithelial BEAS‑2B cells","description":"Electronic cigarettes (e‑cigarettes) generate aerosols by heating e‑liquids composed of propylene glycol, vegetable glycerin, nicotine, and flavoring agents. Although considered safer than conventional cigarettes, thermal decomposition of e‑liquids produces reactive carbonyls such as formaldehyde and acetaldehyde, and device hardware contributes metals and silicates. The health consequences of exposure remain incompletely understood, with evidence pointing to oxidative stress, mitochondrial dysfunction, and altered cellular responses. In this study, we investigated the acute effects of sub‑cytotoxic concentrations of e‑cigarette aerosol condensates on the human bronchial epithelial cell line BEAS‑2B. Condensates were generated from carrier liquids alone and from liquids containing nicotine and flavoring agents. We applied integrated transcriptomic and proteomic profiling, including assessment of protein modifications. Our results show that even short‑term exposure alters RNA and protein expression, disrupts protein translation and mitochondrial function, and is accompanied by irreversible protein modifications.","dates":{"publication":"2026-04-06","submission":"2026-01-09"},"accession":"PXD072831","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:294671","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:3715","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:10891","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:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:31345","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:299467","NEWT:9541","NEWT:51350","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:132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