{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069622/pEX2_pp_6596_20250728_Proteins_PD.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069622/pEX2_pp_6596_20250728_PeptideGroups_PD.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069622/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069622/pEX2_pp_6596_20250728_TMT4Plex_BRP_F5_1pt4uL_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069622/pEX2_pp_6596_20250728_TMT4Plex_BRP_F4_1pt5uL_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069622/pEX2_pp_6596_20250728_TMT4Plex_BRP_F8_1uL_8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069622/pEX2_pp_6596_20250728_TMT4Plex_BRP_F7_1pt5uL_7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069622/pEX2_pp_6596_20250728_TMT4Plex_BRP_F3_1pt5uL_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069622/pEX2_pp_6596_20250728_TMT4Plex_BRP_F1_0pt5uL_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069622/pEX2_pp_6596_20250728_TMT4Plex_BRP_F6_1pt5uL_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069622/pEX2_pp_6596_20250728_TMT4Plex_BRP_F2_1pt2uL_2.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["kristie.rose@vanderbilt.edu"],"submitter":["Kristie Lindsey Rose"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"disease":["Gastritis"],"software":[""],"submitter_keywords":["polyamine","Infection","Infection; gastritis; polyamine; quantitative proteomics","gastritis","quantitative proteomics"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069622"],"tissue":["Gastric Epithelial Cell","Epithelial Cell Of Stomach"],"sample_protocol":["For each of the four sample groups, equivalent protein amounts were pooled from two biological replicates. Proteins were digested with trypsin on S-Trap (ProtiFi) micro columns. Peptides were labeled with TMT reagents, combined, and fractionated using high pH reverse phase fractionation. Peptide fractions were analyzed by LC-MS/MS using an Orbitrap Exploris 240 mass spectrometer (Thermo Scientific)."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Data were searched against a mouse database (UniprotKB) using SequestHT in Proteome Discoverer (Thermo Scientific). Percolator validation was performed with a 1% false discovery rate, and reporter-based quantitative analysis was performed using the summed abundance-based approach. Protein results were filtered to include proteins with a minimum of two unique peptides"],"omics_type":["Proteomics"],"labhead":["Kristie Lindsey Rose"],"instrument_platform":[""],"labhead_affiliation":["Vanderbilt University Proteomics Core"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["kristie.rose@vanderbilt.edu"],"publication":["41627564 Gobert AP, McNamara KM, Hawkins CV, Asim M, Barry DP, Delgado AG, Rose KL, Patel P, Tyree RN, Carson KS, Coburn LA, Piazuelo MB, Wilson KT. Epithelial hypusination regulates Helicobacter pylori-induced gastric inflammation. Amino Acids. 2026 58(1):28 10.1007/s00726-026-03496-3"],"submitter_affiliation":["Vanderbilt University"],"submitter_country":["United States"],"pubmed_abstract":["Hypusine is a unique amino acid synthesized on the eukaryotic initiation factor 5 A (EIF5A) from the polyamine spermidine by deoxyhypusine synthase (DHPS). Hypusination of EIF5A plays a key role in translation. Here, we examined the contribution of the epithelial hypusination pathway to gastric inflammation induced by Helicobacter pylori. Immunohistochemical analyses revealed increased expression of DHPS and hypusinated EIF5A (EIF5A<sup>Hyp</sup>) in the gastric mucosa of patients with H. pylori gastritis compared to uninfected individuals, notably within gastric epithelial cells (GECs) and immune infiltrates. Then, we created a mouse model with epithelial-specific deletion of Dhps (Dhps<sup>Δepi</sup>) and confirmed the reduction of DHPS and EIF5A<sup>Hyp</sup> in GECs. H. pylori-infected Dhps<sup>Δepi</sup> mice exhibited an attenuation of gastric histologic inflammation scores compared with infected Dhps<sup>fl/+</sup> controls, without alteration in bacterial colonization levels. Quantitative proteomics of isolated GECs showed that Dhps deletion altered the expression of proteins involved in organismal injury, cancer, and gastrointestinal diseases in naïve mice. Upon H. pylori infection, inflammatory and immune response proteins, including signaling factors and immunoglobulin mediators, were less induced in Dhps<sup>Δepi</sup> GECs, and pathways linked to tissue injury and inflammation were selectively downregulated. Together, these findings demonstrate that epithelial hypusination supports H. pylori-driven gastric inflammation without affecting bacterial persistence. Targeting DHPS-dependent EIF5A hypusination may thus represent a novel therapeutic strategy to limit H. pylori-associated mucosal injury and disease progression."],"pubmed_title":["Epithelial hypusination regulates Helicobacter pylori-induced gastric inflammation."],"pubmed_authors":["Gobert Alain P AP, McNamara Kara M KM, Hawkins Caroline V CV, Asim Mohammad M, Barry Daniel P DP, Delgado Alberto G AG, Rose Kristie L KL, Patel Purvi P, Tyree Regina N RN, Carson Kate S KS, Coburn Lori A LA, Piazuelo M Blanca MB, Wilson Keith T KT"],"additional_accession":[]},"is_claimable":false,"name":"Regulation by hypusination of the proteome of GECs during H. pylori infection","description":"Mice with or without specific deletion of the gene Dhps in intestinal epithelial cells were infected (n = 2 per genotype) or not (n = 2 per genotype) with Helicobacter pylori PMSS1 for 8 weeks. Proteins from isolated gastric epithelial cells (GECs) were extracted and analyzed using a TMT-based proteomics 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