{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250831_173905_20250830-1235_Report.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/sample_metadata_labels.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250831-0630_AS1_003962_16.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250831-0742_AS1_003963_17.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250830-1346_AS1_003949_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250831-1228_AS1_003967_21.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250830-1610_AS1_003951_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250831-1116_AS1_003966_20.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250831-0407_AS1_003960_14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250830-2321_AS1_003956_10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250830-1723_AS1_003952_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250831-0256_AS1_003959_13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250831-0519_AS1_003961_15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250831-0144_AS1_003958_12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250830-1946_AS1_003954_7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250831-1005_AS1_003965_19.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250830-1834_AS1_003953_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250831-0033_AS1_003957_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250831-0853_AS1_003964_18.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250830-1458_AS1_003950_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250830-1235_AS1_003948_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250830-2210_AS1_003955_9.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077710/20250831_173905_20250830-1235.sne"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["grevengoed@sund.ku.dk"],"submitter":["Ivan Bradić"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"disease":["Barth Syndrome"],"software":[""],"submitter_keywords":["Tafazzin","Barth syndrome","Fish oil diet"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077710"],"tissue":["Muscle"],"sample_protocol":["Approximately 10 µg of gastrocnemius were lysed in 50mM HEPES, pH 8.5, containing 5 % sodium deoxycholate (SDC), supplemented with Complete protease inhibitor (EDTA-free 118735800001, Roche). Samples were sonicated on ice for 30 s, and proteins were denatured at 98 °C for 5 min. Samples were then centrifuged at 20,000 xg for 20 min at 4 °C, and the supernatant was transferred to a new tube. Protein concentrations were determined by BCA.  Reduction was performed with 10 mM dithiothreitol for 20 min and alkylation with 20 mM iodoacetamide for 20 min. An aliquot of 20 µg of protein was used for digestion at 37* and preincubated with LysC = 0.04 activity units per mg proteins before adding 5% trypsin. SDC was precipitated by adding TFA to a final concentration of 1% and centrifuging at 20,000 xg for 10 min. The supernatant was collected, and peptides were purified using a C18 stage tip. Purified peptides were vacuum-dried and resuspended in 0.1% formic acid.  Approximately 1000 ng of peptides, dissolved in solvent A (0.1% formic acid), were loaded onto a 20-cm analytical column (100-µm inner diameter) packed with ReproSil-Pur C18 AQ 1.9-µm RP material using a Thermo Scientific™ Vanquish™ Neo UHPLC system coupled to an Orbitrap Astral mass spectrometer. Elution of peptides was performed steadily with a flow of 300 ul/min by increasing the amount of solvent B (95% acetonitrile and 0.1% formic acid) from 0.3% to 38% over 40 minutes and then increasing to 90% B over 2 minutes and keeping that % for 5 more minutes. During the 30 min gradient, the mass spectrometer operated in positive mode with Orbitrap resolution set at 240,000, a scan range of 400-1000 m/z, and a maximum injection time of 5 ms. Data-independent acquisition (DIA) was performed with higher-energy collision-induced dissociation set to 25%, a scan range from 150 to 2000 m/z, a maximum injection time of 3.5 ms, and a cycle time of 0.6 s. Fragment ions were detected using the Astral detector."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw data files were searched with Spectronaut 20.0, using the Mus musculus reference proteome FASTA file, ID UP000000589, containing 21,757 genes (downloaded on 27.01.2025). BGS Factory Settings were used for the search with minor modifications. Most search settings were kept at their defaults. In brief, search settings included Trypsin/P-digested peptides with a maximum of 2 missed cleavages, carbamidomethyl (C) as a fixed modification, and a maximum of 5 variable modifications, including acetyl (protein N-term) and oxidation (M). The Deep directDIA+ workflow was used for identification. For quantification, precursor filtering was set to “Identified (Qvalue)”, and no imputation was performed. The proteotypicity filter was set to “Only protein group specific”, and cross-run normalization was used."],"omics_type":["Proteomics"],"labhead":["Trisha J. Grevengoed"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Biomedical Sciences, University of Copenhagen, Denmark"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["ibradic95@gmail.com"],"submitter_affiliation":["University of Southern Denmark"],"submitter_country":["Denmark"],"additional_accession":[]},"is_claimable":false,"name":"Omega-3 fatty acid supplementation improves skeletal muscle mitochondrial function in a model of Barth syndrome","description":"The composition of mitochondrial membrane lipids is crucial to cellular respiration, as seen in Barth syndrome (BTHS), a rare disease affecting skeletal muscle, heart, and neutrophils. In BTHS, mutations in the tafazzin (TAZ) gene reduce remodeling of the mitochondrial phospholipid, cardiolipin, resulting in mitochondrial dysfunction in skeletal muscle and heart. Here, we investigate the effects of altering polyunsaturated fatty acid content in cardiolipin using preclinical models of BTHS. In vitro, the lack of TAZ did not impair omega-3 fatty acid incorporation into cardiolipin and led to higher turnover of these acyl chains. To examine this in a functional model, we generated a muscle-specific knockout mouse of TAZ (TAZ MKO), which recapitulated the human phenotype in skeletal muscle. Supplementing the diet of TAZ MKO with fish-oil derived omega-3 fatty acids prevented lean mass loss, improved mitochondrial respiration, altered mitochondrial structure and revealed moderate improvements in the stress response. Surprisingly, no diet-induced changes to cardiolipin species were observed in the TAZ MKO, but other phospholipids were altered by both genotype and diet, revealing complex regulation and potential compensation. Overall, this work provides evidence that omega-3 fatty acid supplementation is beneficial in muscle lacking TAZ to improve quality of life when added to current treatments in 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