{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036860/sample_type_all_q_proteins.xlsx"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036860/3_M_K2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036860/9_L_K2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036860/10_L_K3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036860/12_L_AN2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036860/6_M_AN2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036860/4_M_K3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036860/8_L_K1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036860/13_L_AN3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036860/5_M_AN1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036860/2_M_K1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036860/7_M_AN3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036860/11_L_AN1.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["marek.rusin@io.gliwice.pl"],"submitter":["Monika Pietrowska"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"software":[""],"submitter_keywords":["wnt signaling","P53; innate immunity; wnt signaling","innate immunity","Transcriptome","Secretome","P53"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD036860"],"sample_protocol":["A549 cells were grown in 6-cm culture plates. For proteomic analysis the cells were cultured in control conditions or were exposed to 5 nM actinomycin D and 5 µM nutlin-3a for 48 hours. For the first 24 h the cells were kept in complete medium (DMEM+10% FBS) and for the next 24 h they were kept in serum-free DMEM. At the end of the treatment, the culture medium was collected for analysis and the cells were trypsynized, washed with PBS and the cell pellet was frozen at -70oC. Subsequently, the cell lysate was prepared by lysing cells with ice-cold IP buffer (50 mM Tris-HCl, pH 8.0, 120 mM NaCl, 0.5% NP 40) supplemented with protease and phosphatase inhibitors. After incubation on ice for 20 min the lysate was cleared by centrifugation at 14 000 rpm (4oC) for 20 min. The supernatant containing soluble proteins was saved and used for proteomic analysis. The medium (5ml) was harvested, centrifuged to remove cell debris (2 000 rpm/2 min) and 4 ml of the medium was concentrated using Vivaspin Turbo 4 (3,000 MWCO) concentrator. The samples were concentrated to the volume of 400 ul. Proteins in the concentrated culture medium or in cell lysates were precipitated using a solution of 10% trichloroacetic acid in acetone (m/v) with sample to precipitant volume ratio of 1:3. The precipitated pellet of proteins was washed in acetone and dried. Subsequently, the dried protein pellet was boiled in 20 ul of 0.1% of RapiGest in 50 mM NH4HCO3 at 99 oC for 10 min, and cooled to room temperature. For enzymatic in-solution digestion, 10 ug of proteins of each sample was used. Protein reduction and alkylation was performed with dithiothreitol (final conc.: 5 mM) and iodoacetamide (final conc.: 15 mM), respectively. Proteins were digested using Trypsin/LysC-Mix (Promega) with enzyme to protein ratio of 1:100 (m/m), incubation temperature: 37 centigrade, incubation time: 18h. The solution of tryptic peptides was purified on StageTip columns filled with Empore Octadecyl C18 extraction discs. The eluate with tryptic peptides was evaporated to dryness and dissolved in 20 ul of LC-MS grade water. Concentration of peptides was determined using tryptophan fluorescence method. Tryptic peptides, 0.5 ug for each sample, were subjected to nano-LC-MS/MS analysis."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["LC-MS/MS analysis was performed with the use of a Dionex UltiMate 3000 RSLC nanoLC System connected to a Q Exactive Orbitrap mass spectrometer (Thermo Fisher Scientific). Peptides from each sample (0.5 μg) were separated on a reverse phase Acclaim PepMap RSLC nanoViper C18 column (75 μm × 25 cm, 2 μm granulation) using an acetonitrile gradient (from 4 to 60%, in 0.1% formic acid) at 30°C and a flow rate of 300 nL/min (for 180 min). The spectrometer was operated in data-dependent MS/MS mode with survey scans acquired at a resolution of 70,000 at m/z 200 in MS mode, and 17,500 at m/z 200 in MS2 mode. Spectra were recorded in the scanning range of 300–2000 m/z in the positive ion mode. Higher energy collisional dissociation (HCD) ion fragmentation was performed with normalized collision energies set to 25. Protein identification was performed using Swiss-Prot human database with a precision tolerance 10 ppm for peptide masses and 0.02 Da to fragment ion masses. All raw data obtained for each dataset were imported into Proteome Discoverer v.1.4 (Thermo Fisher Scientific) <Thermo raw files>. For protein identification and quantification Mascot and Sequest engines were used for database searches. Protein was considered as positively identified if at least two peptides per protein were found by both search engines, and a peptide score reached the significance threshold FDR = 0.01 (assessed by the Percolator algorithm); a protein was further considered as “present” if detected in at least one sample of a given type. Abundances of identified proteins were estimated in Proteome Discoverer using Precursor Ions Area detector node, which calculates the abundance of a given protein based on the average intensity of three most intensive distinct peptides for this protein, with further normalization to the total ion current."],"omics_type":["Proteomics"],"labhead":["Marek Rusin"],"instrument_platform":[""],"labhead_affiliation":["Maria Sklodowska-Curie National Research Institute of Oncology"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["monika.pietrowska@io.gliwice.pl"],"publication":["38460933 Łasut-Szyszka B, Gdowicz-Kłosok A, Małachowska B, Krześniak M, Będzińska A, Gawin M, Pietrowska M, Rusin M. Transcriptomic and proteomic study of cancer cell lines exposed to actinomycin D and nutlin-3a reveals numerous, novel candidates for p53-regulated genes. Chem Biol Interact. 2024 392:110946 10.1016/j.cbi.2024.110946"],"submitter_affiliation":["Maria Sklodowska-Curie National Research Institute of Oncology"],"submitter_country":["Poland"],"pubmed_abstract":["Transcriptomic analyses have revealed hundreds of p53-regulated genes; however, these studies used a limited number of cell lines and p53-activating agents. Therefore, we searched for candidate p53-target genes by employing stress factors and cell lines never before used in a high-throughput search for p53-regulated genes. We performed RNA-Seq on A549 cells exposed to camptothecin, actinomycin D, nutlin-3a, as well as a combination of actinomycin D and nutlin-3a (A + N). The latter two substances synergise upon the activation of selected p53-target genes. A similar analysis was performed on other cell lines (U-2 OS, NCI-H460, A375) exposed to A + N. To identify proteins in cell lysates or those secreted into a medium of A549 cells in control conditions or treated with A + N, we employed mass spectrometry. The expression of selected genes strongly upregulated by A + N or camptothecin was examined by RT-PCR in p53-deficient cells and their controls. We found that p53 participates in the upregulation of: ACP5, APOL3, CDH3, CIBAR2, CRABP2, CTHRC1, CTSH, FAM13C, FBXO2, FRMD8, FRZB, GAST, ICOSLG, KANK3, KCNK6, KLRG2, MAFB, MR1, NDRG4, PTAFR, RETSAT, TMEM52, TNFRSF14, TRANK1, TYSND1, WFDC2, WFDC5, WNT4 genes. Twelve of these proteins were detected in the secretome and/or proteome of treated cells. Our data generated new hypotheses concerning the functioning of p53. Many genes activated by A + N or camptothecin are also activated by interferons, indicating a noticeable overlap between transcriptional programs of p53 and these antiviral cytokines. Moreover, several identified genes code for antagonists of WNT/β-catenin signalling pathways, which suggests new connections between these two cancer-related signalling systems. One of these antagonists is DRAXIN. Previously, we found that its gene is activated by p53. In this study, using mass spectrometry and Western blotting, we detected expression of DRAXIN in a medium of A549 cells exposed to A + N. Thus, this protein functions not only in the development of the nervous system, but it may also have a new cancer-related function."],"pubmed_title":["Transcriptomic and proteomic study of cancer cell lines exposed to actinomycin D and nutlin-3a reveals numerous, novel candidates for p53-regulated genes."],"pubmed_authors":["Łasut-Szyszka Barbara B, Gdowicz-Kłosok Agnieszka A, Małachowska Beata B, Krześniak Małgorzata M, Będzińska Agnieszka A, Gawin Marta M, Pietrowska Monika M, Rusin Marek M"],"additional_accession":[]},"is_claimable":false,"name":"Transcriptomic and proteomic study of cancer cell lines exposed to actinomycin D and nutlin-3a reveals numerous, novel candidates for p53-regulated genes","description":"Transcriptomic analyses revealed hundreds of p53-regulated genes, however these studies used a limited number of cell lines and p53-activating agents. Therefore, we searched for candidate p53-target genes by employing stress factors and cell lines never used in high-throughput search for p53-regulated genes. We performed RNA-Seq on A549 cells exposed either to camptothecin, actinomycin D, nutlin-3a or to a combination of actinomycin D and nutlin-3a (A+N). The latter two substances synergize in activation of selected p53-target genes. Similar analysis was performed on other cell lines (U-2 OS, NCI-H460, A375) exposed to A+N. Mass spectrometry was employed to identify proteins in cell lysates or those secreted to the medium of A549 cells in control conditions or treated with A+N. Expression of selected genes strongly upregulated by A+N or camptothecin was examined by RT-PCR in p53-deficient cells and their controls. We found that p53 participates in upregulation of: ACP5, APOL3, CDH3, CIBAR2, CRABP2, CTHRC1, CTSH, FAM13C, FBXO2, FRMD8, FRZB, GAST, ICOSLG, KANK3, KCNK6, KLRG2, MAFB, MR1, NDRG4, PTAFR, RETSAT, TMEM52, TNFRSF14, TRANK1, TYSND1, WFDC2, WFDC5, WNT4 genes. Twelve of their proteins were detected in the secretome and/or proteome of treated cells. Our data generate new hypotheses concerning functioning of p53 tumor 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