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pm-mito; ibm-sd; mitochondria","mitochondria","Polymyositis with mitochondrial pathology","ibm-sd"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD053742"],"tissue":["Skeletal Muscle"],"sample_protocol":["Muscle tissue of patients lysed in 200 μl of 50 mM Tris-HCl (pH 7.8) buffer, 5% SDS and cOmplete ULTRA protease inhibitor (Roche) using a Bioruptor® sonication device (Diagenode) for 10 min (30 s on, 30 s off, 10 cycles) at 4 °C. To ensure complete lysis, an additional sonication step was performed by ultrasound (30 s, 1 s/1 s, amplitude 40%), followed by centrifugation at 4 °C and 20,000 g for 15 min. Protein concentration of the supernatant was determined by BCA assay (Pierce) according to the manufacturer's protocol. Disulfide bonds were reduced by addition of 10 mM Tris(2-carboxyethyl)phosphine hydrochloride (TCEP) at 37 °C for 30 min, and free sulfhydryl bonds were alkylated with 15 mM IAA at room temperature (RT) in the dark for 30 min. From each sample 100 μg of protein was used for proteolysis utilizing the S-trap protocol (Protifi) and a protein-to-trypsin ratio of 20:1. The samples were incubate for 2 h at 37 °C. Proteolysis was stopped by acidification of the sample (pH < 3.0) with formic acid to acidify the sample."],"repository":["pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["For analysis of samples acquired by nano-LC-MS/MS in DIA mode, data were submitted to Spectronaut software (Biognosys) and analyzed using a library-based search. A spectral library created in-house was used as the library. Search and extraction settings were kept as default (BGS Factory settings). Human proteome data from UniProt (www.uniprot.org) with 20,374 entries were selected as the proteome background.  For reliable label-free quantification, only proteins with ≥ 2 unique peptides were considered for further analysis. Subsequently, average normalized abundances (determined using Spectronaut) were calculated for each protein and used to determine the ratio between patient samples and corresponding controls. Finally, a Student's t-test p-values were calculated for each protein using MS Excel."],"omics_type":["Proteomics"],"labhead":["Albert Sickmann"],"instrument_platform":[""],"labhead_affiliation":["Proteomics,Leibniz-Institut für analytische Wissenschaften -ISAS - e.V., Germany"],"species":["Homo Sapiens (human)"],"submission_type":["PARTIAL"],"publication":["40193586 Kleefeld F, Cross E, Lagos D, Walli S, Schoser B, Hentschel A, Ruck T, Nelke C, Hahn K, Hathazi D, Mammen AL, Casal-Dominguez M, Gut M, Gut IG, Heath S, Schänzer A, Goebel HH, Pinal-Fernandez I, Roos A, Preuße C, Stenzel W, Horvath R. Mitochondrial damage is associated with an early immune response in inclusion body myositis. Brain. 2025 148(9):3199-3214 10.1093/brain/awaf118"],"submitter_mail":["andreas.hentschel@isas.de"],"submitter_affiliation":["Leibniz Institut für Analytische Wissenschaften"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Mitochondrial leakage and mtDNA damage triggering early immune response in Inclusion Body Myositis.","description":"Polymyositis with mitochondrial pathology (PM-Mito) was first identified in 1997 as a subtype of idiopathic inflammatory myopathy (IIM). Significant molecular similarities have been recently detected between PM-Mito and Inclusion Body Myositis (IBM), suggesting a trajectory from early to full-blown IBM, and prompting the inclusion of PM-Mito as an early form of IBM (eIBM) within the IBM spectrum. Both early and late stages of IBM show mitochondrial abnormalities, suggesting mitochondrial dysfunction is an early feature of IBM.  The primary objective of this study was to characterize the mitochondrial phenotype in eIBM/PM-Mito at histological, ultrastructural, and molecular levels and to study the possible interplay between mitochondrial dysfunction and inflammation. Skeletal muscle biopsies of 27 patients with eIBM/PM-Mito and 27 full-blown IBM were included for morphological and ultrastructural analysis. Mitochondrial DNA (mtDNA) copy number and deletions were assessed by qPCR and long-range PCR, respectively. In addition, full-length single-molecule sequencing of the mtDNA enabled precise mapping of deletions. Protein and RNA levels were studied using unbiased proteomic profiling, immunoblotting, and bulk RNA sequencing. Cell-free mtDNA (cfmtDNA) was measured in the serum of full-blown IBM 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