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In the recovery exposure scheme,  MnO2 was added at the selected concentration for 24 further hours. Afterwards, the medium was changed in order to remove remaining pigments. The medium was then renewed every 24 hours until the end of the 5 day-recovery period. In the repeated exposure scheme, the cells were exposed to MnO2 daily for 4 days. At the end of the exposure, cells were harvested by repeated flushing. They were collected by centrifugation (200g, 5 minutes) and rinsed twice in PBS.  The cell suspensions were then centrifuged (200g, 5 minutes) and lysed in 15 µl of extraction buffer (4M urea, 2.5% cetyltrimethylammonium chloride, 100mM sodium phosphate buffer pH 3, 150µM methylene blue). The extraction was let to proceed at room temperature for 1 hour, after which the lysate was centrifuged (15,000g, 30 minutes) to pellet the nucleic acids. The supernatant were then stored at -20°C until use. For the shotgun proteomic analysis, the samples were included in polyacrylamide plugs. To this purpose, the photopolymerization system using methylene blue, toluene sulfinate and diphenyliodonium chloride was used. As mentioned above, the methylene blue was included in the cell lysis buffer.The other initiator solutions consisted in a 1 M solution of sodium toluene sulfinate in water and in a saturated water solution of diphenyliodonium chloride. The ready-to-use polyacrylamide solution consisted of 1.2 ml of a commercial 40% acrylamide/bis solution (37.5/1) to which 100 µl of diphenyliodonium chloride solution, 100 µl of sodium toluene sulfinate solution and 100 µl of water were added. To the protein samples (15 µl), 5 µl of acrylamide solution were added and mixed by pipetting in a 500µl conical polypropylene microtube. 100 µl of water-saturated butanol were then layered on top of the samples, and polymerization was carried out under a 1500 lumen 2700K LED lamp for 2 hours, during which the initially blue gel solution discolored. At the end of the polymerization period, the butanol was removed, and the gel plugs were fixed for 2x1 hr with 200 µl of 30% ethanol 2 % phosphoric acid, followed by a 30 minutes wash in 30% ethanol. The fixed gel plugs were then stored at -20°C until use. Gel plug processing, digestion, peptide extraction and nanoLC-MS/MS was performed as previously described without the robotic protein handling system and using a nanoACQUITY Ultra-Performance-LC (Waters Corporation, Milford, USA) coupled to a Q-Exactive HF-X mass spectrometer (Thermo Fisher Scientific, Bremen, Germany)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For protein identification, the MS/MS data were interpreted using a local Mascot server with MASCOT 2.6.2 algorithm (Matrix Science, London, UK) against an in-house database containing all Mus musculus and Rattus norvegicus entries from UniProtKB/SwissProt (version 2025_01, 25,574 sequences) and the corresponding 25,574 reverse entries. Spectra were searched with a mass tolerance of 10 ppm for MS and 0.05 Da for MS/MS data, allowing a maximum of one trypsin missed cleavage. Trypsin was specified as enzyme. Acetylation of protein n-termini, carbamidomethylation of cysteine residues and oxidation of methionine residues were specified as variable modifications. Identification results were imported into Proline software version 2.3 (http://proline.profiproteomics.fr/) for validation. Peptide Spectrum Matches (PSM) with pretty rank equal to one were retained. False Discovery Rate was then optimized to be below 1% at PSM level using Mascot Adjusted E-value and below 1% at Protein Level using Mascot Mudpit score."],"omics_type":["Proteomics"],"labhead":["Christine Carapito"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Laboratoire de Spectrometrie de Masse BioOrganique (LSMBO), Universite de Strasbourg, CNRS, IPHC UMR 7178, 67087 Strasbourg, France"],"species":["Mus Musculus (mouse)"],"publication":["10.1016/J.HAZADV.2026.101337"],"submitter_mail":["hdiemer@unistra.fr"],"submitter_affiliation":["LSMBO"],"submitter_country":["France"],"doi":["10.6019/PXD065155"],"additional_accession":[]},"is_claimable":false,"name":"Cellular and molecular effects of manganese dioxide on macrophages under different exposure schemes.","description":"Manganese dioxide (MnO2) is a solid metal oxide widely used in the industry and especially in the batteries industry. This wide use poses in turn the question of its effects on cells. Macrophages, pivotal in taking in charge particulate materials in the body, are also key players in the inflammatory response and tissue homeostasis. Dysregulation in macrophage functionalities can potentially lead to substantial health consequences such as deficient immune response or oppositely chronic inflammation.  Proteomic analyses were conducted to understand the underlying cellular mechanisms under two different exposure schemes. The recovery exposure scenario investigates the delayed effects induced by MnO2 after an acute exposure, while the repeated exposure scenario investigates the effects of a chronic 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