{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/summary.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/msms.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/peptides.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/allPeptides.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/parameters.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/matchedFeatures.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/proteinGroups.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/MaxQuant_Sample_Matrix.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/evidence.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/ms3Scans.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/mzRange.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/Oxidation_M_Sites.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/msmsScans.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/modificationSpecificPeptides.txt"],"Pdf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/MQ_Output_Tables.pdf"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/mqpar.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/240821_AP_2426JM_11_S11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/240821_AP_2426JM_10_S07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/240821_AP_2426JM_02_S05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/240821_AP_2426JM_03_S09.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/240821_AP_2426JM_05_S02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/240821_AP_2426JM_07_S10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/240821_AP_2426JM_13_S04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/240821_AP_2426JM_15_S12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/240821_AP_2426JM_14_S08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/240821_AP_2426JM_06_S06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/240821_AP_2426JM_09_S03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/240821_AP_2426JM_01_S01.raw"],"Mztab":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069390/mzTab.mzTab"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["gisa.gerold@i-med.ac.at"],"submitter":["Karsten Cirksena"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Growth plates","Growth","Gene regulation","Body size","Miniaturization","Miniature pigs","Functional genomics","Multi-omics"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069390"],"tissue":["Long Bone"],"sample_protocol":["Flash-frozen samples of growth plates from the left humerus, in triplicate, were immersed in cold lysis buffer (Tris-HCl 50 mM, NaCl 150 mM, 1% NP-40, 0.5% Sodium deoxycholate, 1% SDS, and Protease Inhibitor Mix 1%), homogenised in a pre-cooled SpeedMill, and immediately centrifuged at 4°C. The samples were left on ice for 30 minutes before they were centrifuged at 4°C. An aliquot from the lysate was taken for measuring the protein concentration using a BCA assay. 20 µg of protein were taken from the lysate for precipitation overnight using ice-cold acetone (final concentration of 80 %). Proteins were spun down at 11,000 g for 15 min at 4 °C. Reduction, alkylation and digest of proteins was performed using Trypsin Gold (Promega) following manufacturer’s instructions. Samples were purified using StageTips following the protocol of Rappsilber et al. (PMID: 17703201). Purified peptides were dried in a SpeedVac Vacuum Concentrator and resuspended in MS buffer (0.1 % formic acid, 5 % acetonitrile in water (MS grade)).  Samples were analyzed via liquid chromatography–mass spectrometry using a Vanquish Neo nanoflow UHPLC System coupled to an Orbitrap Eclipse mass spectrometer (Thermo Scientific™). Of each sample, 500 ng peptides were separated on a reversed-phase nanoViper™ PepMap™ separating column (150 mm length, 75 μm inner diameter, and 2 μm C18 particle size (Thermo Scientific™)) using buffer A (0 % ACN, 0.1 % FA) and B (80 % ACN, 0.1 % FA). Peptides were eluted at a flow rate of 250 nL/min at 40 °C by a gradient starting with Buffer B increased from 6 % to 25 % within 60 min and further increased to 90 % within 10 min and hold at 90 % for additional 8 min. Ionization was achieved by a Nano Spray Flex Ion Source and stainless steel emitters (40mm, OD 1/32) at 1,900 V. Precursor scans were performed in the Orbitrap mass analyzer with an m/z range set to 375 1500, at a resolution of 120,000, and stored in profile mode. Twenty most intense precursors with intensities above 2,000 counts were fragmented in the linear ion trap by higher-energy collisional dissociation with collision energy set to 30 % and dynamic exclusion set to 45 s. Fragment ion scans were performed in the Ion Trap mass analyzer with AGC set to Standard, Injection Time Mode set to Auto, mass range set to Normal and spectra stored in centroid mode."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["MS raw data were processed with MaxQuant software (V. 2.4.14.0) for the identification and quantification of proteins using preconfigured settings and, additionally, selecting label-free quantification via LFQ and IBAQ as well as writing mzTab tables. MS spectra were searched against UniProt database of porcine proteins (ID: UP000008227, all entries, downloaded on 21 June 2024)."],"omics_type":["Proteomics"],"labhead":["Gisa Gerold"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Institute of Virology  Medical University of Innsbruck Schöpfstraße 41 6020 Innsbruck, Austria"],"species":["Sus Scrofa (pig)"],"publication":["Not available"],"submitter_mail":["karsten.cirksena.research@posteo.de"],"submitter_affiliation":["Helmholtz Centre for Infection Research"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Integrative multi-omics analysis of growth plate regulation underlying body size in miniature pigs","description":"Body size represents a complex phenotype driven by genetic variation and epigenetic regulation, with the molecular processes underlying this trait remaining a central challenge to disentangle. To elucidate these fundamental mechanisms, we applied a multi-omics approach to investigate the regulatory architecture of growth in the growth plates of the long bones from pigs, a valuable model species for skeletal development. Taking advantage of divergent selection that separates pig breeds into miniature and larger-sized types, we targeted homozygous genomic regions under this intense selection for height, which harbor functional variants with pronounced effects. We sampled two miniature breeds, namely Aachen Minipig (AM) and Mini-LEWE (ML), as well as two larger pig breeds, Angeln Saddleback (AS) and Mangalitza (MA) and assembled an integrated multi-omics dataset comprising the results of WGS, Hi-C, ATAC-seq and RNA-seq, available at ENA Browser with accession number provided in our manuscript, and LC-MS analyses (data available with this submission). Data analyses led to the identification of 23 homozygous mutant variants in Aachen Minipigs and 13 distinct variants in Mini-LEWE predicted to affect cis-regulatory elements and potentially interact with differentially expressed genes that drive body size in breed-dependent ways. Our results pointed to HPX, an lncRNA (ENSSSCG00000048200) located near SDR16C5 and PLAG1, as well as NET-related pathways, as central players in impaired growth in the growth plates. Furthermore, protein-protein interaction networks highlighted 16 proteins that interacted significantly, of which GC vitamin D binding was identified as a regulatory element acting downstream of the key variants for body size across miniature pig breeds. In summary, our study offers a multi-layered characterization of regulatory mechanisms in the growth plates, using miniature pigs as a model to understand the genetic and epigenetic control of long-bone 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