{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R3Neg_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/03032025_Alsayegh_RFrac1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R3Neg_3a.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R4Neg_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231124_R1Pos_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/03032025_Alsayegh_RFrac4_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231124_R4Neg_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/03032025_Alsayegh_RFrac9_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R1Neg_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231124_R4Pos_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R1Neg_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/03032025_Alsayegh_RFrac7_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R4Neg_2a.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/03032025_Alsayegh_RFrac2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R4Neg_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/03032025_Alsayegh_RFrac10_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231124_R3Neg_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R3Pos_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R4Neg_3a.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/03032025_Alsayegh_RFrac5_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R1Pos_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R4Pos_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231124_R1Neg_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R3Pos_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/03032025_Alsayegh_RFrac3_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R4Pos_3a.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R1Pos_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/03032025_Alsayegh_RFrac9_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R3Neg_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/03032025_Alsayegh_RFrac8_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R4Pos_2a.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231124_R3Pos_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/03032025_Alsayegh_RFrac6_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R3Neg_2a.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/231127_R4Pos_2.raw"],"Mztab":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078584/03032025_Alsayegh_Quantified_Proteins_Result.mzTab"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"submitter":["Liaqat Ali"],"software":[""],"tissue":["Stem Cell","Cell Culture"],"sample_protocol":["Preparation of protein digests: Proteins, cell lysate and conditioned media, from the mouse embryonic stem cells were reduced (20 mM DTT Sigma, 70 oC, 30 min) and S-alkylated (50 mM IAA Sigma, 1 h, dark). The remaining IAA was quenched (20 mM DTT), proteins were trichloroacetic acid precipitated (30% TCA, 4 oC, overnight) and centrifuged at high speed (16 000 g, 4 oC, 15 min) to pellet the protein. The protein pellet was washed with ice cold acetone, air dried and resuspended in 50 mM ammonium bicarbonate (ABC, Sigma). Protein concentration was determined using the Pierce BCA protein assay kit (Thermo Fisher Scientific). 50 µg proteins were digested with 1:50 (w/w enzyme:protein) MS-grade trypsin/lys-C mix (Thermo Scientific) for 24 h at 37 oC. The enzyme digestion was quenched with 1 µl of formic acid (Fisher), peptide digests was desalted with ZipTip C18 (Merck-Millipore), dried and resuspended in 15 µl of 0.2% formic acid prior liquid chromatography tandem mass spectrometry (LC-MS2). Proteomics Proteomics analysis was conducted using a fully automated EASY-nLC 1200 system (Thermo Scientific) equipped with a PepMap RSLC C18 column (75 µm i.d, 15 cm length) maintained at 40 oC. Mobile phases consisted of 0.1% formic acid (solvent A) and 0.1% formic acid in 95% acetonitrile (solvent B). Samples were loaded in solvent A. A linear gradient was set as follows: 0% B for 3 min and then a gradient up to 35% B in 45 min and to 60% B in 60 min. A 10-min wash at 90% B was used to prevent carryover, and a 15-min equilibration with 0% B completed the gradient. The LC system was coupled to a Q-Exactive high field orbitrap (Thermo Scientific) equipped with an Easy spray ion source and operated in positive ion mode. The spray voltage was set to 1.8 kV, S-lens RF level to 35 and ion transfer tube to 275 °C. The full scans were acquired in the orbitrap mass analyzer that covered an m/z range of 350–1800 at a resolution of 120,000. The AGC target was set to 3E6 and maximum ion time to 50 ms. The MS/MS analysis was performed under data-dependent mode to fragment the top 20 most intense precursors using HCD fragmentation. The MS/MS parameters were set as follows: resolution, 15 000; AGC target, 1E5; minimum AGC target, 8.0E3, intensity threshold, 4.0E5; maximum ion time, 20 ms; isolation width, 1.4 m/z; precursor charge state, 2-5; peptide match, preferred; dynamic exclusion, 30 s, and fixed first mass of 80 m/z. The normalized collision energy for HCD is set to 32%."],"repository":["Pride"],"labhead":["Mohamed Al-Sayegh"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["New York University Abu Dhabi, Division of Biology, Saadiyaat Island, Abu Dhabi, United Arab Emirates New York University Abu Dhabi, Center of Genomics and System Biology, Saadiyaat Island, Abu Dhabi, United Arab Emirates"],"publication":["42228580 Al-Sayegh M, Khalili M, Alzaabi M, Sultana M, Ali L, Ali M, El-Hadidi M. Multi-omics integration reveals convergent extracellular matrix remodelling and lipid metabolic reprogramming as central axes of adipocyte differentiation from mouse embryonic stem cells. Adipocyte. 2026 15(1):2680625 10.1080/21623945.2026.2680625"],"submitter_affiliation":["New York University Abu Dhabi"],"labhead_mail":["ma3803@nyu.edu"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Type 2 Diabetes Mellitus"],"submitter_keywords":["Adipogenesis; mouse embryonic stem cells; multi-omics integration; extracellular matrix remodeling; lipidomics; mofa+; multi-omics factor analysis","multi-omics factor analysis","multi-omics integration","mofa+","mouse embryonic stem cells","lipidomics","extracellular matrix remodeling","Adipogenesis"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD078584"],"quantification_method":[""],"modification":[""],"data_protocol":["Data Processing Proteins identifications were determined using Thermo proteome discoverer 2.5 (http://thermofischer.com/) software’s with following settings: enzyme, trypsin; instrument, orbitrap; fragmentation, HCD; acquisition, DDA without merging the scans; and precursor and fragment mass tolerance, 10 ppm and 0.2 Da respectively. Correct precursor was detected using mass only. Peptide identifications were performed using UniProtKB_SwissSprot database (release 2025_03, https://www.uniprot.org/uniprot) with mouse taxonomy. The proteome discoverer search tool was used to search for peptides with fixed carbamidomethylation and variable oxidation of methionine (M) and N-terminal acetylation modifications. FDR threshold was set to 1%, fold change set to 2 with 2 unique peptides per proteins were used to filter the identified protein lists."],"omics_type":["Proteomics"],"species":["Mus Musculus (mouse)"],"submitter_mail":["la77@nyu.edu"],"curator_keywords":["Stems cells (b/d-hpp)","Diabetes (b/d-hpp)"],"submitter_country":["United Arab Emirates"],"doi":["10.6019/PXD078584"],"pubmed_abstract":["Adipogenesis from mouse embryonic stem cells (mESCs) offers a tractable model for dissecting early adipocyte commitment, yet the mechanisms coordinating this transition across multiple biological layers remain incompletely understood. Here we present the first simultaneous five-layer multi-omics characterization of mESC-derived adipocyte differentiation, integrating transcriptomics, proteomics, secretomics, lipidomics, and metabolomics from matched adipogenic (Pos) and non-differentiating (Neg) cell populations at day 30. Applying Multi-Omics Factor Analysis (MOFA+), we identified a dominant shared latent axis that perfectly segregated Pos from Neg cells across all five views. Layer-specific functional enrichment converged on two principal biological axes: ECM remodeling - encompassing collagens, laminins, thrombospondins, and lysyl oxidases - and lipid metabolic reprogramming, with phospholipid and glycerolipid metabolic processes dominating the lipidomics/metabolomics layer. Ensemble Machine Learning Feature Ranking (EMFR) identified a secreted factor (Scpep1; importance score 0.90) as the top-ranked discriminatory feature. Network analysis revealed indirect ECM-lipid connectivity mediated by four bridging nodes (Plod1, Thbs2, Plg, Pmp22) through a hub subnetwork of phospholipid-metabolizing enzymes. Targeted qPCR validation of six candidate regulators (Itga5, Igfbp6, Pik3cg, Lpl, Acer3, Sirt1) confirmed RNA-seq concordance. These findings establish convergent ECM remodeling and lipid metabolic reprogramming as central axes of adipocyte identity acquisition from mESCs."],"pubmed_title":["Multi-omics integration reveals convergent extracellular matrix remodelling and lipid metabolic reprogramming as central axes of adipocyte differentiation from mouse embryonic stem cells."],"pubmed_authors":["Al-Sayegh M M, Khalili M M, Alzaabi M M, Sultana M M, Ali L L, Ali M M, El-Hadidi M M"],"additional_accession":[]},"is_claimable":false,"name":"Multi-omics integration reveals convergent extracellular matrix remodeling and lipid metabolic reprogramming as central axes of adipocyte differentiation from mouse embryonic stem cells","description":"Adipose tissue dysfunction is a hallmark of obesity and type 2 diabetes mellitus, yet the full molecular complexity of adipocyte differentiation remains incompletely characterized. Single-omics approaches capture only partial dimensions of this multi-layered biological transition. Here, we applied a comprehensive five-layer multi-omics framework to dissect adipocyte differentiation from mouse embryonic stem cells (mESCs) at day 30 under adipogenic and non-differentiating conditions, integrating transcriptomic, proteomic, secretomic, metabolomic, and lipidomic profiling across matched biological replicates. Principal component analysis demonstrated robust condition-specific separation across all molecular layers, with transcriptomics exhibiting the strongest discriminatory power. MultiOmics Factor Analysis (MOFA+) identified a dominant shared latent factor strongly associated with adipogenic condition (Wilcoxon p = 2.9 × 10⁻⁵), capturing coordinated variance across transcriptomic, proteomic, lipidomic, and metabolomic layers, while secretomic variance was partially independent. Gene Ontology enrichment analyses converged upon extracellular matrix organization and lipid metabolic reprogramming as the principal biological themes driving differentiation across modalities. Interaction network analysis identified lipid metabolic enzymes — including phospholipases, ceramide synthases, and acyltransferases — and extracellular matrix regulators as high-degree network hubs, rather than canonical PPARγdriven transcription factors alone. Targeted qPCR validation of six prioritized candidates confirmed significant upregulation of Lpl and Plg and downregulation of Acer3 in differentiated cells, alongside directionally concordant changes in Itga5, Igfbp6, and Pik3cg. These findings establish that mESC adipogenesis is governed by a systems-level program integrating transcriptional activation, structural ECM remodeling, and lipid enzymatic reprogramming, and nominate novel regulatory hubs with relevance to metabolic disease pathophysiology.","dates":{"publication":"2026-06-08","submission":"2026-05-20"},"accession":"PXD078584","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:460523","NEWT:2423","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:941638","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:280406","NEWT:83906","NEWT:99488","NEWT:99487","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:483179","NEWT:315750","NEWT:99490","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:1479235","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:105812","NEWT:11298","NEWT:4233","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT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