{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD055812/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD055812/20220201_MK_Evo_FAIMS_VC_3CV_DIA_global_WT_2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD055812/20220201_MK_Evo_FAIMS_VC_3CV_DIA_global_B11_2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD055812/20220201_MK_Evo_FAIMS_VC_3CV_DIA_global_D2_3_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD055812/20220201_MK_Evo_FAIMS_VC_3CV_DIA_global_D2_1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD055812/20220201_MK_Evo_FAIMS_VC_3CV_DIA_global_WT_1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD055812/20220201_MK_Evo_FAIMS_VC_3CV_DIA_global_WT_3_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD055812/20220201_MK_Evo_FAIMS_VC_3CV_DIA_global_D2_2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD055812/20220201_MK_Evo_FAIMS_VC_3CV_DIA_global_B11_1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD055812/20220201_MK_Evo_FAIMS_VC_3CV_DIA_global_B11_3_1.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD055812/20220201_VC_3D_PROTEOME_BG_AB_WT_v2.sne"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["chiafra@dtu.dk"],"submitter":["Vahap Canbay"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"disease":["Wounds And Injuries"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD055812"],"tissue":["Primary Cell","Epithelial Cell","Keratinocyte","Epidermal Keratinocyte","Skin","Skin Fibroblast"],"sample_protocol":["Lysis buffer (4M guanidine hydrochloride (GuHCl) and 250 mM N-2-hydroxyethylpiperazine-N-2-ethane sulfonic acid (HEPES) (pH 7.8)) was mixed with 3D organotypic skin cultures, homogenized using the steel beads (QIAGEN) and TissueLyser II (QIAGEN). The lysate was processed twice for 1 min each at varying frequencies (3 Hz to 30 Hz), beads were removed using a magnetic rack and the suspension was heated for 5 min at 95 °C. Following this, the samples underwent five cycles of sonication and cooling using the TissueLyser ii (QIAGEN). After centrifugation, the protein content was determined using Nanodrop (Thermo Fisher Scientific) and Bradford assays (Bio-Rad). The samples were reduced and alkylated on aliquots of 50 µg protein using 5 mM tris(2-carboxyethyl)phosphin (TCEP) and 20 mM 2-chloroacetamide (CAA). The samples were diluted with 50 mM HEPES buffer (pH 7.8) and incubated with Lys-C (FUJIFILM) for 4 h, 37 °C followed by trypsin (Promega) for 16 h at 37 °C. The enzyme activity was blocked by 1% tri-fluoroacetic acid (TFA) and samples were desalted using Solaµ plates (Thermo Fisher Scientific), according to manufacturer’s instructions. For each resuspended proteome, peptides were analysed using the pre-set ’30 samples per day’ method on the EvoSep One instrument. Peptides were eluted over an EvoSep One defined 44-min gradient and analysed by mass spectrometry, Orbitrap Exploris 480 (Thermo Fisher Scientific), with the following settings: Spray voltage was set to 2.3 kV, funnel RF level at 40, and heated capillary at 240 °C. Full MS spectra were collected at a resolution of 120000, with an AGC target of 300% or maximum injection time set to ‘custom’ and a scan range of 350–1650 m/z. The MS2 spectra were obtained in DIA mode in the Orbitrap operating at a resolution of 15000, equipped with FAIMS Pro™ Interface (Thermo Fisher Scientific) with a CV of -35, -55 and -75 V, with an AGC target 1000% or maximum injection time set to ‘auto’, a normalised HCD collision energy of 30. The isolation window was set to 38 m/z with a 1 m/z overlap and window placement off. MS performance was verified for consistency by running complex cell lysate quality control standards, and chromatography was monitored to check for reproducibility."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Raw files were analysed using Spectronaut™ (Biognosys) directDIA+ (deep) default settings, spectra were matched against the homo sapiens reference FASTA database (UP000005640; downloaded from Uniprot on 27th of December 2022). Default settings were used without imputation. Dynamic modifications were set as Oxidation (M), Glutamine  to pyro-Glutamine and Acetyl on protein N-termini. Cysteine carbamidomethyl was set as a static modification. Protein quantitation was done on the MS2 level, data filtering set to default Q-values (1 % FDR). Data were processed using R (version 4.1.1) and functions implemented in the pipeline of limma (version 1.30.7). The volcano plots were visualized using ggplot2 and the Gene Ontology analysis was performed using Metascape."],"omics_type":["Proteomics"],"labhead":["Chiara Francavilla"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Section for Protein Science and Biotherapeutics, Department of Biotechnology and Biomedicine, Technical University of Denmark, Søltofts Plads, 2800, Kongens Lyngby, Denmark"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["vahcan@dtu.dk"],"submitter_affiliation":["Technical University of Denmark"],"submitter_country":["Denmark"],"additional_accession":[]},"is_claimable":false,"name":"Mulit-omics analysis of keratinocytes reveals dermokine as regulator keratinocyte differentiation and adhesion  - 3D Proteome","description":"Impaired adhesion and differentiation of keratinocytes is a hallmark of several skin diseases, but only some of the factors that regulate these processes have been identified. Here, we studied the role of isoform-rich dermokine – a wound- and tumor-regulated protein – in keratinocytes using a combination of multi-omics and functional approaches. CRISPR/Cas9-induced knockout of dermokine isoforms in human keratinocytes inhibited differentiation of these cells in three-dimensional organotypic skin cultures, which was confirmed by quantitative proteomics. In two-dimensional monocultures, dermokine deficiency affected the proteome and phosphoproteome as revealed by mass spectrometry. We found reduced abundance of differentiation-specific proteins and increased phosphorylation of cell adhesion protein p120 (catenin-δ1). The adhesive strength of dermokine knockout keratinocytes was impaired, which was rescued by p120 knock-down or ROCK inhibition. Finally, we verified the correlation between decreased dermokine expression and increased p120 phosphorylation in human non-healing wounds. These results identify dermokine as regulator of keratinocyte adhesion and differentiation, involving at least in part its effect on p120 phosphorylation and ROCK. Our data point to a function of dermokine in the pathogenesis of chronic 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