{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Cytosol_liver_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Mytochondria_liver_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Mytochondria_cells_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Nuclear_cells_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Nuclear_liver_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Nuclear_liver_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Cytosol_cells_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Mytochondria_cells_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Nuclear_cells_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Cytosol_liver_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Mytochondria_liver_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Cytosol_cells_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Nuclear_cells_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Mytochondria_liver_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Mytochondria_cells_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Cytosol_liver_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Cytosol_cells_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/Nuclear_liver_2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/PRM_enriquecimiento_mitocondrial-celulas_n3.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067737/PRM_enriquecimiento_mitocondrial-tejido.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["fcorrales@cnb.csic.es"],"submitter":["Alejandra Delgado Sequera"],"technology_type":["SRM/MRM","Mass Spectrometry"],"software":["Not available"],"submitter_keywords":["Subcellular fractionation","Liver","Mitochondrial enrichment","Target proteomic","Prm"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067737"],"tissue":["Primary Cell Line Cell","Liver"],"sample_protocol":["Mitochondria and cytosol were isolated from mouse liver using the Mitochondria Isolation Kit for Tissue (Pierce, 89874 USA) and from PLC/PRF/5 using the Mitochondria Isolation Kit for Cultured Cells (Pierce) according to the manufacturer's instructions. Liver and cell nuclei were obtained using the Nuclei pure prep nuclei isolation kit (Sigma, NUC-201, USA) according to the manufacturer's instructions.Isolated mitochondria and nuclei were lysed in lysis buffer [7 M urea, 2 M thiourea, 4% CHAPS (3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate), 40 mM dithiothreitol (DTT) at pH 7.7] for 30 min at 4 °C, followed by two rounds of sonication for 20 seconds each, with a 20-second pause between cycles. Lysates were centrifuged at 17,000 × g for 20 minutes at 4 °C, and protein concentration was determined in the supernatant using the Pierce 660-nm Protein Assay (Thermo Fisher Scientific). Protein processing (30 μg) was done in micro S-Trap columns (Protifi). Briefly, reduction and alkylation of Cys sulfhydryl groups were performed by incubation with tris (2-carboxyethyl) phosphine (TCEP, 5 mM) and chloroacetamide (CCA, 10 mM), for 1 h at 37 °C. Protein digestion was performed with trypsin (90057, Thermo Fisher Scientific) at a 1:15 ratio (μg trypsin: μg protein) o/n at 37 °C. The resulting peptide mixture was cleaned with stage -Tips (Empore Octadecyl C18 extraction disks, SUPELCO) and the concentration was then determined using a Qubit fluorometric assay (Invitrogen"],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Selection and extraction of the signals corresponding to each selected transition (table 1), was carried out with the Skyline v24.1 software.  All results were manually curated and all interferences excluded. Transition areas were summed and presented at the peptide level. Statistical analyses were performed using GraphPad Prism software (GraphPad Software, USA). Statistical differences were assessed using one-way ANOVA, and results were considered significant at a p-value < 0.05"],"omics_type":["Proteomics"],"labhead":["Fernando Corrales"],"instrument_platform":[""],"labhead_affiliation":["CNB-CSIC"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["alejandra.delgado@gm.uca.es"],"publication":["41740191 Delgado-Sequera A, Paradela A, Corrales FJ. Targeted Quantitative Analysis of Specific Proteins in Cytosolic, Mitochondrial, and Nuclear Fractions Using PRM. J Proteome Res. 2026 25(4):2183-2192 10.1021/acs.jproteome.5c00697"],"submitter_affiliation":["CNB-CSIC"],"submitter_country":["Spain"],"pubmed_abstract":["Mitochondria play a central role in liver physiology by regulating key metabolic processes. Consequently, mitochondrial dysfunction is a hallmark of multiple liver diseases, including steatosis, steatohepatitis, and liver failure following hepatectomy. Subcellular fractionation is widely used to isolate mitochondria from liver cells or tissue; however, the enrichment and purity of isolated fractions are critical to ensure reliable downstream functional and proteomic analyses. Conventional validation methods, such as immunoblotting of organelle-specific markers, are limited by low throughput, restricted sensitivity, and variability. In this study, we present a targeted proteomics strategy based on parallel reaction monitoring (PRM) to quantitatively assess the enrichment of cytosolic, mitochondrial, and nuclear fractions obtained from liver samples using commercial isolation kits. PRM analyses demonstrated robust and compartment-specific enrichment in both PLC/PRF/5 cells and mouse liver tissue. In PLC/PRF/5 cells, high nuclear/cytosolic enrichment was observed for Prelamin A/C, while mitochondrial markers such as ATPase showed strong mitochondrial/cytosolic ratios. Cytosolic markers consistently displayed enrichment in the cytosolic fraction. Similar trends were observed in mouse liver tissue, confirming applicability across biological systems. Overall, these results highlight PRM as a sensitive, reproducible, and cost-effective alternative to immunodetection approaches for evaluating subcellular fraction purity, supporting high-quality mitochondrial preparations for translational hepatology studies."],"pubmed_title":["Targeted Quantitative Analysis of Specific Proteins in Cytosolic, Mitochondrial, and Nuclear Fractions Using PRM."],"pubmed_authors":["Delgado-Sequera Alejandra A, Paradela Alberto A, Corrales Fernando J FJ"],"additional_accession":[]},"is_claimable":false,"name":"Targeted quantitative analysis of specific proteins in cytosolic, mitochondrial, and nuclear fractions using PRM","description":"We present a targeted proteomic approach using parallel reaction monitoring (PRM) to assess the enrichment of cytosolic, mitochondrial, and nuclear fractions obtained from liver samples using commercial isolation kits. For mitochondrial fraction, CPS1 and ATP5F1 were chosen. For the cytosolic fraction, HSP90AB1 and AHCY were selected. For the nuclear fraction, LMNA and NPM1 were used as 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