{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080411/report.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080411/report.tsv.protein_intensities.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080411/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080411/meta.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080411/timsTOF-d-folders.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["rosenberger@biochem.mpg.de"],"submitter":["Mario Oroshi"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":["Heart","Spleen","Mitochondria","Mtdna","Mouse","Liver"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD080411"],"tissue":["Spleen","Heart","Liver"],"sample_protocol":["Approximately 1 mm³ of dissected, frozen tissue was transferred into individual wells of a BeatBox Tissue Kit 96x (PreOmics) and overlaid with 80 µL of LYSE buffer (PreOmics). Samples were homogenized in the BeatBox for 10 min at the standard setting, heated at 95 °C for 10 min with shaking at 1,000 rpm for simultaneous reduction and alkylation, and then subjected to focused ultrasonication on a Covaris instrument at the manufacturer's standard settings. Protein concentration was determined by BCA assay. For each sample, 10 µg of protein was diluted in 50 mM Tris-HCl pH 8.5 and digested with a Trypsin/LysC mix at an enzyme-to-protein ratio of 1:50 (w/w) overnight at 37 °C with mild shaking (500 rpm). Digestion was stopped by acidification to a final concentration of 1% formic acid. Acidified peptides were loaded onto StageTips packed with two SDB-RPS (Empore) disks, washed once with 1% trifluoroacetic acid (TFA) in isopropanol and once with 0.2% TFA/2% acetonitrile in water, and eluted with 60 µL of 1.25% ammonium hydroxide in 80% acetonitrile. Eluates were dried by vacuum centrifugation and reconstituted in 0.1% formic acid (EvoA). Peptide concentrations were measured by Nanodrop. For LC-MS analysis, 500 ng of peptides per sample was loaded onto Evotip Pure tips (Evosep). All loading steps were performed with 50 µL volumes and centrifugation at 700 g. Briefly, Evotips were rinsed with EvoB (0.1% formic acid in acetonitrile), conditioned by soaking in 1-propanol for 3 min until uniformly pale white, and equilibrated with EvoA (0.1% formic acid in MS-grade water). The 500 ng peptide samples were loaded in EvoA, washed once with EvoA, and overlaid with EvoA to keep the tips wet. Loaded Evotips were stored submerged in EvoA at 4 °C until LC-MS/MS analysis.  Samples were analyzed using an Evosep One LC system (EvoSep) coupled to a timsTOF HT mass spectrometer (Bruker Daltonics; TimsControl/acquisition software 5.0.9). Data acquisition was performed with the 30 samples per day method, employing an Evosep Performance column (15 cm × 150 µm ID, EV1137, EvoSep) maintained at 40 °C and interfaced via a nanoelectrospray ion source (Bruker Daltonics) with a 10 µm emitter (ZDV Sprayer 10, Bruker Daltonics). The mobile phases consisted of 0.1% formic acid (FA) in LC–MS-grade water (buffer A) and 99.9% acetonitrile/0.1% FA (buffer B). Mass spectrometry was performed using a dia-PASEF method optimized with py_diaid, comprising 20 dia-PASEF scans, each divided into two ion mobility windows (40 isolation windows in total) with variable isolation widths (11–94 Th), covering an m/z range of 350-1,200 and an ion mobility range of 0.70-1.30 V s cm⁻². The instrument was operated with an accumulation and ramp time of 100 ms, a capillary voltage of 1,750 V, and collision energy ramped linearly from 20 eV at 1/K0 = 0.6 V s cm⁻² to 59 eV at 1/K0 = 1.6 V s cm⁻²."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Data processing was carried out in DIA-NN (v1.9.1) using an in silico–predicted spectral library for the first run, which was then applied to a second instance. A FASTA database without isoforms was used. DIA-NN parameters included MS1/MS2 mass accuracy of 15 ppm, a scan window size of 7, fixed carbamidomethylation, and allowance for one missed cleavage."],"omics_type":["Proteomics"],"labhead":["Florian Rosenberger"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Max Planck Institute of Biochemistry, Dept. Proteomics and Signal Transduction, Martinsried, Germany"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["oroshi@biochem.mpg.de"],"submitter_affiliation":["Proteomics"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Cardiomyocyte-intrinsic somatic mtDNA mutations induce an OXPHOS-dependent immune response and promote progressive heart failure","description":"Mitochondrial DNA (mtDNA) mutations accumulate with age, but their mechanistic contribution to ageing remains unclear. The classical mtDNA mutator mouse expresses a proofreading-deficient mtDNA polymerase (POLGD257A) and accumulates mtDNA mutations across all tissues leading to premature ageing. However, this model cannot resolve whether the ageing phenotype results from systemic dysfunction or cell-intrinsic effects of somatic mtDNA mutations. To overcome this limitation, we generated PolgiMut mice allowing spatial and temporal control of POLGD257A expression. We demonstrate here that mtDNA mutations induced in cardiomyocytes cause progressive contractile dysfunction and respiratory chain deficiency in the heart without accompanying systemic pathology. Proteomic analyses link cardiac mosaic OXPHOS dysfunction to a progressive immune response, characterized by upregulation of antigen-processing proteins and immune cell infiltration. In contrast, longevity-associated pathways are suppressed and uncoupled from mitochondrial and immune alterations, indicating distinct regulatory mechanisms. These findings demonstrate that mtDNA mutations can drive cardiac dysfunction and reveal a mechanistic link between mitochondrial dysfunction, immune responses and 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