{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD032080/20211218_sample_8_3-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD032080/20211218_sample_7_3-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD032080/20211218_sample_2_1-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD032080/20211218_sample_1_1-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD032080/20211218_sample_6_2-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD032080/20211218_sample_3_1-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD032080/20211218_sample_4_2-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD032080/20211218_sample_9_3-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD032080/20211218_sample_5_2-2.raw"],"Mztab":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD032080/20220110_all_phospho_q_control_.mzTab"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["piotr.widlak@io.gliwice.pl"],"submitter":["Monika Pietrowska"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"disease":["Head And Neck Squamous Cell Carcinoma"],"software":[""],"submitter_keywords":["Phosphoproteomics","Q exactive plus","Bystander effect","Exosomes","Mass spectrometry"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD032080"],"tissue":["Epithelial Cell","Cell Culture"],"sample_protocol":["Lysates in RIPA buffer (300 µg of total protein extract in each) were subjected to protein precipitation with four volumes of ice-cold acetone and kept at -20 °C overnight, then centrifuged (20’000 RCF, 30 min, 4°C).  Thus obtained protein pellets were dissolved in 1 mL 8M urea in 50 mM HN4HCO3 and subjected to in-solution digestion with Trypsin/Lys-C Mix (Promega) with enzyme to protein ratio of 1:50 (m/m). Enzymatic digestion was preceded with reduction of disulfide bridges using dithiothreitol (final concentration of DDT: 5 mM) and alkylation of cysteines with iodoacetamide (final concentration of IAA: 15 mM).  The obtained protein digests were purified using solid-phase extraction on octadecyl bed (Macherey Nagel Chromabond C18, 100mg/1mL cartridges), the collected eluates were mixed with acetonitrile and trifluoroacetic acid to obtain the final concentration of ACN and TFA of 50% and 6%, respectively.  Thus obtained peptide samples were subjected to phosphopeptide enrichment using metal oxide affinity chromatography (MOAC) with titanium dioxide as a sorbent. Two TopTips (Glygen) filled with porous TiO2 (bed volume of 15 µL) were utilized for each sample in order to perform two rounds of enrichment and gain higher recovery of phosphopeptides from each sample.  Phosphopeptide sorption was realized in a batch mode as follows: a portion of TiO2 sorbent contained in one TopTip was  transferred to a 2 mL Eppendorf tube and preconditioned in the Binding Buffer (50% ACN, 6% TFA) upon vigorous mixing using a laboratory vertical rotator, then spun shortly. The activated sorbent was subsequently soaked with a sample solution and incubated at room temperature for 1 hour upon vigorous mixing. Then, the  sample was transferred to the second portion of activated TiO2 beads and incubated for another hour upon mixing.  Both portions of TiO2 were washed twice with the Wash Buffer (50% ACN, 0.1% TFA), the beads and the second portion of the Wash Buffer were transferred back to the emptied TopTips and the retained phosphopeptides were released from each portion of the bed in a two-step elution: first with 0.1 mL of the Elution Buffer 1 (5% NH3 aq), then with 0.1 mL of the Elution Buffer 2 (10% NH3 aq, 25% ACN); each elution step was aided with centrifugation at 400 RCF, 2 min.  Eluates obtained from both portions of TiO2 were subsequently merged and the volatile constituents (i.e. NH3 and ACN) were removed via vacuum evaporation.  All samples were acidified with TFA and desalted using StageTips filled with 8 pieces of octadecyl disk (C18 disks, Empore).  Eluates were dried out in a vacuum centrifuge and peptides were reconstituted in 20 µL of water. Peptide content in each sample was assessed using tryptophan fluorescence method. LC-MS/MS analysis of phosphopeptide samples was carried out using the Dionex UltiMate 3000 RSLC nanoLC System in conjunction with the Q Exactive Plus Orbitrap mass spectrometer (Thermo Fisher Scientific). Peptides from each phosphopeptide-enriched sample (1.0 μg) were separated on a reverse phase Acclaim PepMap RSLC nanoViper C18 column (75 μm × 25 cm, 2 μm granulation) using 0,1% FA in LC-MS grade water as a Mobile Phase A and 80% acetonitrile with 0,1% FA in LC-MS grade water as a Mobile Phase B at 30°C and a flow rate of 300 nL/min (for 120 minutes).  For additional desalting purposes samples were loaded onto a C18 trap column for 3 minutes using 0,1% FA in LC-MS grade water as a Loading Buffer. After desalting the trap column was switched with the analytical column and peptides were eluted with the binary gradients of: 3-8% of the Mobile Phase B for 7 min, 8-28% Mobile Phase B for 50 min, 28-50% Mobile Phase B for 20 min and 50-80% Mobile Phase B in a further 5 min. Finally, rinsing of the column in 80% Mobile Phase B for 15 min and equilibrating in 3% Mobile Phase B for 20 min were performed.  The spectrometer was operated in data dependent MS/MS mode with survey scans acquired at the resolution of 70,000 at m/z 200 in MS mode, and 17,500 at m/z 200 in MS2 mode. Spectra were recorded via positive ion scanning mode in the range of 380-1500 m/z. Using a normalized collision energy of 28, higher energy collisional dissociation (HCD) was used to fragment ions."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Based on the Swiss-Prot human database (release 2021_03 containing 20 325 sequence entries, 11 364 617 residues), peptide and fragment ion masses were measured for protein identification with a precision tolerance of 10 ppm and 0.02 Da, respectively. Cysteine carbamidomethylation was set as a fixed modification, as a variable modification methionine oxidation and phosphorylation of serine, threonine, tyrosine, histidine and aspartic acid were chosen.  All raw data derived from each dataset were imported into Protein Discoverer v. 2.3.0 (Thermo Fisher Scientific) < Thermo raw files > to identify and quantify proteins (Sequest engine was used to search the database). Using the search engine, proteins were considered as positively identified if one peptide per protein were detected by the search engine, and the peptide score met the significance threshold FDR = 0.01 (based on the Percolator algorithm); a protein was also considered as “present” if detected in at least one sample of a given type.  Protein abundances were determined in Proteome Discoverer by using the Precursor Ions Area detector mode, which uses an average intensity of three most intensive peptides for a given protein, normalized to the total ion current (TIC)."],"omics_type":["Proteomics"],"labhead":["Piotr Widlak"],"instrument_platform":[""],"labhead_affiliation":["Maria Sklodowska-Curie National Research Institute of Oncology, Gliwice Branch"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["monika.pietrowska@io.gliwice.pl"],"publication":["35456987 Smolarz M, Skoczylas Ł, Gawin M, Krzyżowska M, Pietrowska M, Widłak P. Radiation-Induced Bystander Effect Mediated by Exosomes Involves the Replication Stress in Recipient Cells. Int J Mol Sci. 2022 23(8):4169 10.3390/ijms23084169"],"submitter_affiliation":["Maria Sklodowska-Curie National Research Institute of Oncology"],"submitter_country":["Poland"],"pubmed_abstract":["Exosomes released by irradiated cells mediate the radiation-induced bystander effect, which is manifested by DNA breaks detected in recipient cells; yet, the specific mechanism responsible for the generation of chromosome lesions remains unclear. In this study, naive FaDu head and neck cancer cells were stimulated with exosomes released by irradiated (a single 2 Gy dose) or mock-irradiated cells. Maximum accumulation of gamma H2A.X foci, a marker of DNA breaks, was detected after one hour of stimulation with exosomes from irradiated donors, the level of which was comparable to the one observed in directly irradiated cells (a weaker wave of the gamma H2A.X foci accumulation was also noted after 23 h of stimulation). Exosomes from irradiated cells, but not from control ones, activated two stress-induced protein kinases: ATM and ATR. Noteworthy is that while direct irradiation activated only ATM, both ATM and ATR were activated by two factors known to induce the replication stress: hydroxyurea and camptothecin (with subsequent phosphorylation of gamma H2A.X). One hour of stimulation with exosomes from irradiated cells suppressed DNA synthesis in recipient cells and resulted in the subsequent nuclear accumulation of RNA:DNA hybrids, which is an indicator of impaired replication. Interestingly, the abovementioned effects were observed before a substantial internalization of exosomes, which may suggest a receptor-mediated mechanism. It was observed that after one hour of stimulation with exosomes from irradiated donors, phosphorylation of several nuclear proteins, including replication factors and regulators of heterochromatin remodeling as well as components of multiple intracellular signaling pathways increased. Hence, we concluded that the bystander effect mediated by exosomes released from irradiated cells involves the replication stress in recipient cells."],"pubmed_title":["Radiation-Induced Bystander Effect Mediated by Exosomes Involves the Replication Stress in Recipient Cells."],"pubmed_authors":["Smolarz Mateusz M, Skoczylas Łukasz Ł, Gawin Marta M, Krzyżowska Monika M, Pietrowska Monika M, Widłak Piotr P"],"additional_accession":[]},"is_claimable":false,"name":"Radiation-induced bystander effect mediated by exosomes involves the replication stress in recipient cells","description":"Exosomes secreted by irradiated cells mediate radiation-induced bystander effect, which is manifested by DNA breaks detected in recipient cells, yet the specific mechanism responsible for the generation of chromosome lesions remains unclear. In this study, naïve FaDu head and neck cancer cells were stimulated with exosomes released by irradiated (a single 2Gy dose) or mock-irradiated cells. Maximum accumulation of gamma H2A.X foci, a marker of DNA breaks, was detected after one hour of stimulation with exosomes from irradiated donors, which level was comparable to the one observed in directly irradiated cells. Exosomes from irradiated cells, but not from control ones, activated two stress-induced protein kinases ATM and ATR. Noteworthy, while direct irradiation activated only ATM, both ATM and ATR were activated by two factors known to induce the replication stress: hydroxyurea and camptothecin (with subsequent phosphorylation of gamma H2A.X). One hour of stimulation with exosomes from irradiated cells suppressed DNA synthesis in recipient cells and resulted in the subsequent nuclear accumulation of RNA:DNA hybrids, which is an indicator of impaired replication. Interestingly, the abovementioned effects were observed before a substantial internalization of exosomes, which may suggest a receptor-mediated mechanism. After one hour of stimulation with exosomes from irradiated donors increased phosphorylation of several nuclear proteins was observed, including replication factors and regulators of heterochromatin remodeling, as well as components of multiple intracellular signaling pathways. Moreover, analysis of gene and protein profiles of recipient cells performed after 24 hours of stimulation with exosomes from irradiated donors revealed that upregulated transcripts and proteins were associated with GO terms related to the regulation of DNA replication and cell division. Hence, we concluded that the bystander effect mediated by exosomes released from irradiated cells involves the replication stress in recipient cells. We hypothesize that this type of stress, depending on the specific cellular context, may have either cytotoxic or cytoprotective consequences for target 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