{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067007/BHG_TMT_Proteomics_Master_File.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067007/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067007/B_TMT_F8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067007/B_TMT_F6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067007/B_TMT_F3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067007/B_TMT_F5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067007/B_TMT_F4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067007/B_TMT_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067007/B_TMT_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067007/B_TMT_F7.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067007/B_TMT_F_noSet1_no50k_2.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067007/Braeden_noSet1_no50k_2.pdStudy"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["koren.mann@mcgill.ca"],"submitter":["Koren Mann"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Lipid droplets","Cholesterol biosynthesis","Proteomics","Flame retardants","Organophosphate esters","Mixture","Macrophage"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067007"],"tissue":["Leukocyte","Macrophage"],"sample_protocol":["THP-1 macrophages (6 x 106 per plate) were washed three times with cold PBS to remove bovine proteins found in the FBS. Control and OPE (1:100,000; 1:20,000) treated macrophages were lysed in 400 \uD835\uDF07L of a filter-sterilized alkaline-urea lysis buffer (8M urea, 0.15% SDS, 25mM HEPES, sterile water, pH = 8) and transferred to a 2 mL Eppendorf tube on ice. Each sample was treated with 25 U/mL benzonase nuclease (SigmaAldrich, #70664) for 30 min on ice to degrade nucleic acids within the lysate and free bound nucleoproteins. Samples were then sonicated for 5 min on ice in 10-second pulses to aid in membrane degradation and protein solubilization. Lysates were then centrifuged at 13,000 x g for 15 min at 4 °C, and the supernatant was transferred to a new tube and frozen at -80 °C until all samples were ready for downstream processing.  Each sample was treated with TMT-16 plex reagents (ThermoFisher Scientific, Waltham, MA, #A44521) according to the manufacturer’s instructions. Labelled peptides were fractionated using Pierce™ High pH Reversed-Phase Peptide Fractionation Kit (ThermoFisher Scientific, #84868) into 8 fractions. Each fraction was re-solubilized in 0.1% aqueous formic acid and 2 \uD835\uDF07g of each was loaded onto a Thermo Acclaim Pepmap (Thermo, 75 µM ID X 2 cm C18 3 µM beads) precolumn and then onto an Acclaim Pepmap Easyspray (Thermo, 75 µM X 15 cm with 2 µM C18 beads) analytical column separation using a Dionex Ultimate 3000 uHPLC at 250 nL/min with a gradient of 2-35% organic (0.1% formic acid in acetonitrile) over three hours running the default settings for MS3-level SPS TMT quantitation (McAlister et al. 2014) on an Orbitrap Fusion instrument (ThermoFisher Scientific) operated in DDA-MS3 mode.  Briefly, MS1 scans were collected at 120,000 resolution, scanning from 375-1500 m/z, collecting ions for 50ms or until the AGC target of 4e5 was reached. Precursors with a charge state of 2-5 were included for MS2 analysis, which were isolated with an isolation window of 0.7 m/z. Ions were collected for up to 50ms or until an AGC target value of 1e4 was reached and fragmented using CID at 35% energy; these were then read out on the linear ion trap in rapid mode. Subsequently, the top 10 (height) sequential precursor notches were selected from MS2 spectra for MS3 quantitative TMT reporter ion analysis, isolated with an m/z window of 2 m/z, and fragmented with HCD at 65% energy. Resulting fragments were read out in the Orbitrap at 60,000 resolution, with a maximum injection time of 105ms or until the AGC target value of 1e5 was reached."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["To translate .raw files into protein identifications and TMT reporter ion intensities, Proteome Discoverer 2.2 (ThermoFisher Scientific) was used with the built-in TMT Reporter ion quantification workflows. Default settings were applied, with trypsin as the enzyme specificity. Spectra were matched against the human protein FASTA database obtained from Uniprot. Dynamic modifications were set as Oxidation (M) and Acetylation on protein N-termini. Cysteine carbamidomethyl was set as a static modification, together with the TMT tag on both peptide N-termini and K residues. All results were filtered to a 1% FDR (false discovery rate)."],"omics_type":["Proteomics"],"labhead":["Koren Mann"],"instrument_platform":[""],"labhead_affiliation":["McGill University"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["koren.mann@mcgill.ca"],"publication":["42015365 Giles BH, Robaire B, Mann KK. An environmentally relevant mixture of organophosphate esters induces cholesterol biosynthesis in THP-1 macrophages. Toxicol Sci. 2026 209(5):kfag048 10.1093/toxsci/kfag048"],"submitter_affiliation":["McGill University"],"submitter_country":["Canada"],"pubmed_abstract":["Organophosphate esters (OPEs), widely used as flame retardants and plasticizers, are environmental toxicants known to disrupt lipid metabolism. Although most studies have focused on individual OPEs, environmental exposures typically involve complex mixtures. Our previous studies demonstrated that a representative OPE mixture from Canadian household dust promotes cholesterol and lipid droplet accumulation in THP-1 macrophages. However, the molecular mechanisms underlying this lipid dysregulation remain unclear. Here, we employed tandem mass tag (TMT)-based quantitative proteomics to investigate how OPE mixtures alter protein expression and lipid regulation in macrophages. THP-1 macrophages were exposed to vehicle or environmentally relevant dilutions of the OPE mixture for 48 h. Lysates were subjected to TMT labeling and mass spectrometry. Bioinformatic analyses using STRING and Ingenuity Pathway Analysis identified 162 differentially expressed proteins, with unsupervised clustering highlighting cholesterol biosynthesis as a key pathway. Further validation via qPCR and upstream analysis implicated the sterol regulatory element-binding protein 2 (SREBP2) signaling axis in OPE-induced cholesterol biosynthesis. Functional assays revealed that atorvastatin-mediated HMG-CoA reductase inhibition, the rate limiting enzyme in cholesterol biosynthesis, prevents cholesterol buildup and lipid droplet formation in macrophages. These findings provide the first evidence that an environmentally relevant OPE mixture can induce cholesterol biosynthesis in human macrophages. These studies provide mechanistic evidence that an environmentally relevant mixture of organophosphate esters induces cholesterol biosynthesis in macrophages. These findings link real-world exposure to lipid pathways implicated in metabolic disease and support the need for updated regulatory standards that protect human health."],"pubmed_title":["An environmentally relevant mixture of organophosphate esters induces cholesterol biosynthesis in THP-1 macrophages."],"pubmed_authors":["Giles Braeden H BH, Robaire Bernard B, Mann Koren K KK"],"additional_accession":[]},"is_claimable":false,"name":"An environmentally relevant mixture of organophosphate esters induces cholesterol biosynthesis in THP-1 macrophages","description":"Organophosphate esters (OPEs), widely used as flame retardants and plasticizers, are environmental toxicants known to disrupt lipid metabolism. Although most studies have focused on individual OPEs, environmental exposures typically involve complex mixtures. Our previous studies demonstrated that a representative OPE mixture from Canadian household dust promotes cholesterol and lipid droplet accumulation in THP-1 macrophages. However, the molecular mechanisms underlying this lipid dysregulation remain unclear. Here, we employed tandem mass tag (TMT)-based quantitative proteomics to investigate how OPE mixtures alter protein expression and lipid regulation in macrophages. THP-1 macrophages were exposed to vehicle or environmentally relevant dilutions (1:100,000 and 1:20,000) of the OPE mixture for 48 hours. Lysates were subjected to TMT labeling and mass spectrometry. Bioinformatic analyses using STRING and Ingenuity Pathway Analysis identified 162 differentially expressed proteins, with unsupervised clustering highlighting cholesterol biosynthesis as a key pathway. Further validation via qPCR and upstream analysis implicated the sterol regulatory element-binding protein 2 (SREBP2) signaling axis in OPE-induced cholesterol biosynthesis. Functional assays revealed that co-treatment with atorvastatin, an HMG-CoA reductase inhibitor, prevented cholesterol accumulation and mitigated lipid droplet formation. These findings provide the first evidence that an environmentally relevant OPE mixture can induce cholesterol biosynthesis in human 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