{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077246/20260113_103214_KAK424_FFPE_SPEED_TCA_Prec_BSG_PGspec_X9excluded_ProteinReport.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077246/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077246/KAK424_X012_CK9_12_1_2946.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077246/KAK424_X008_CK6_8_1_2942.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077246/KAK424_X004_CK3_4_1_2938.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077246/KAK424_X014_CK11_14_1_2948.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077246/KAK424_X002_CK1_2_1_2936.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077246/KAK424_X010_CK8_10_1_2944.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077246/KAK424_X013_CK10_13_1_2947.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077246/KAK424_X005_CK4_5_1_2939.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077246/KAK424_X007_CK5_7_1_2941.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077246/KAK424_X003_CK2_3_1_2937.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["heiko.lickert@helmholtz-munich.de"],"submitter":["Christine von Toerne"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Lc-ms","Porcine","Slc20a2","Zcchc7","Pancreas"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077246"],"tissue":["Pancreas"],"sample_protocol":["Pig colony management Pigs from different  transgenic backgrounds (German landrace) were used for this study with a sampling method of convenience, meaning than pancreata were sampled following pig euthanization for other planned experiments. Pigs were maintained at the pathogen-free pig facility of LMU Munich (Center for Innovative Medical Models; www.lmu.de/cimm/). Health assessment was routinely carried out according to FELASA guidelines. Work described in this paper was performed under the Permission No. 55.2-2532.Vet_02-17-136 and 55.2-2532.Vet_02-19-195 approved by the licensing committee from the responsible authority (Government of Upper Bavaria). All experiments were conducted according to the German Animal Welfare Act and Directive 2010/63/EU on the protection of animals used for scientific purposes.  Porcine pancreas processing and staining Isolated whole pancreata was cleaned from larger vessels and connective tissue, smaller pieces were cut (2-5 cm) and fixed with 4% paraformaldehyde overnight. After washing three times with PBS 1X, half of the pieces were allocated for cryo-embedding and half were used for paraffin embedding, when sample number was permitting. For cryo-embedding, pancreas was incubated consecutively with 15% and 30% of sucrose solution in PBS 1X overnight and embedded in tissue freezing medium before storing at -80oC, until use. For paraffin embedding, pancreas was dehydrated with a gradient of alcohol before embedding into melted paraffin. Samples were stored at 4oC degrees until further processing. Proteomics data acquisition and analysis For proteomics sample preparation, we de-paraffinized 20 µm thick paraffin-embedded sections from four non-pregnant, three early pregnancy and three late pregnancy samples. Deparaffinization was performed according to the recently described protocol for human pancreas paraffin tissue[22]. Following deparaffinization, the tissue was scraped into a low-protein bind Eppendorf tube and stored at -80oC until further processing. De-parafinized material was subjected to the SPEED protocol [38]. After protein quantification using BCA (ThermoFischer Scientific), ten µg per sample were reduced, alkylated and digested in-solution using trypsin and Lys-C, overnight. Peptides were purified as described previously[39] and stored at -20°C until measurement.  The MS data were acquired in DIA-PASEF mode on a timsTOF HT mass spectrometer (Bruker, Bremen, DE). Equal amounts of peptides were automatically loaded to the online coupled VanquishNeo (Thermo Fisher Scientific, Dreieich, DE) HPLC system. A Nano-Trap column was used (300-µm inner diameter (ID) × 5 mm), packed with Acclaim PepMap100 C18, 5µm, 100 Å from LC Packings, Sunnyvale, CA, USA, before separation by reversed-phase chromatography (AuroraUltimate 75µm ID × 250 mm, 1.7µm from IonOptics) at 40°C. Peptides were eluted from the column at 250 nl/min using increasing ACN concentration in 0.1% formic acid from 3 to 40% over a 45-min gradient. The DIA-PASEF method covered a mass range from 300 to 1,250 m/z and a mobility range from 0.65 to 1.35 1/ko. Precursor peptides were isolated with 34 equal windows. Collision energy for 0.6 1/ko was set to 20 and for 1.6 1/ko to 59. Estimated cycle time was 1.91 seconds."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["DIA files were processed with Spectronaut (Version 20, Biognosys) as direct DIA analysis against a custom-built pig protein database comprised of SwissProt pig proteins combined with non-redundant Trembl sequences, selected for longest sequences per protein entry based on human gene names (16534 sequences; version 1 generated February 2024) using BSG factory settings for Pulsar search. For DIA analysis, default settings were applied. For quantification, precursor filtering was set on Qvalue, with cross run normalization. Quantity MS level was set to MS2; Quantity type was area, and protein quantification is based on the summed-up peptide intensities. PCA plot was calculated on the top 500 most variable proteins. Differential protein analysis was performed with the DEP2 pipeline for comprehensive proteomics data analysis[40]. We imputed the data with the QRILC method and corrected for FDR using Storey’s value, padj<0.1 was considered significant.Statistical analysis was performed using the GraphPad Prism (version 10.6.1). First samples were tested for normality before employing the statistical tests fit in each analysis and which are mentioned in the figure legends of the work."],"omics_type":["Proteomics"],"labhead":["Heiko Lickert"],"instrument_platform":[""],"labhead_affiliation":["Institute of Diabetes and Regeneration Research, Helmholtz Munich, Neuherberg, Germany"],"submission_type":["PARTIAL"],"species":["Sus Scrofa Domesticus (domestic Pig)"],"publication":["Not available"],"submitter_mail":["vontoerne@helmholtz-muenchen.de"],"submitter_affiliation":["Helmholtz Zentrum München"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"LC-MS on porcine pancreatic remodeling","description":"The pancreatic endocrine cells, particularly the insulin secreting β-cells, adapt to pregnancy by increasing cell mass, size and altering secretory patterns. Since most studies utilize rodent models, translating findings to human pregnancy remains challenging. In this work, we performed an extensive characterization of pancreatic adaptations throughout pig pregnancy. Pigs have long gestational cycles (114 days) as well as similar size and metabolism to humans. By analyzing pancreatic samples from early and late gestation ages, we captured the full trajectory of endocrine remodeling. We observed that pregnancy induces selective endocrine cell-type remodeling, marked by preferential expansion of pancreatic polypeptide cells. Proteomic characterization of pancreata from early and late gestation showed a downregulation of SLC20A2 and ZCCHC7, identifying new targetable proteins for physiological endocrine cell adaptation. Overall, our comprehensive characterization of pancreatic adaptations in the pig model bridges the translational gap between rodents and humans and highlights new proteins with therapeutic potential in gestational 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