{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Li T"],"funding":["Doctoral Fund of Jining No.1 People's Hospital","Projects of medical and health technology development program in Shandong province","Natural Science Research Project of Universities in Jiangsu Province","Key Research and Development Program of Jining Science and Technology","General Program of China Postdoctoral Science Foundation","Suzhou Science and Technology Council","Natural Science Foundation of Jiangsu Province"],"pagination":["e2307648"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10870076"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(7)"],"pubmed_abstract":["T-2 toxin causes renal dysfunction with proteinuria and glomerular podocyte damage. This work explores the role of metabolic disorder/reprogramming-mediated epigenetic modification in the progression of T-2 toxin-stimulated podocyte injury. A metabolomics experiment is performed to assess metabolic responses to T-2 toxin infection in human podocytes. Roles of protein O-linked-N-acetylglucosaminylation (O-GlcNAcylation) in regulating T-2 toxin-stimulated podocyte injury in mouse and podocyte models are assessed. O-GlcNAc target proteins are recognized by mass spectrometry and co-immunoprecipitation experiments. Moreover, histone acetylation and autophagy levels are measured. T-2 toxin infection upregulates glucose transporter type 1 (GLUT1) expression and enhances hexosamine biosynthetic pa"],"journal":["Advanced science (Weinheim, Baden-Wurttemberg, Germany)"],"pubmed_title":["T-2 Toxin-Mediated β-Arrestin-1 O-GlcNAcylation Exacerbates Glomerular Podocyte Injury via Regulating Histone Acetylation."],"pmcid":["PMC10870076"],"funding_grant_id":["2022M711369","BK20221091","2022YXNS118","2021-BS-008","SNG201907","20KJB330002","202113050502"],"pubmed_authors":["He C","Li T","Zhang J","Chang T","Chen Y","Sun W","Zhu S"],"additional_accession":[]},"is_claimable":false,"name":"T-2 Toxin-Mediated β-Arrestin-1 O-GlcNAcylation Exacerbates Glomerular Podocyte Injury via Regulating Histone Acetylation.","description":"T-2 toxin causes renal dysfunction with proteinuria and glomerular podocyte damage. This work explores the role of metabolic disorder/reprogramming-mediated epigenetic modification in the progression of T-2 toxin-stimulated podocyte injury. A metabolomics experiment is performed to assess metabolic responses to T-2 toxin infection in human podocytes. Roles of protein O-linked-N-acetylglucosaminylation (O-GlcNAcylation) in regulating T-2 toxin-stimulated podocyte injury in mouse and podocyte models are assessed. O-GlcNAc target proteins are recognized by mass spectrometry and co-immunoprecipitation experiments. Moreover, histone acetylation and autophagy levels are measured. T-2 toxin infection upregulates glucose transporter type 1 (GLUT1) expression and enhances hexosamine biosynthetic pa","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Feb","modification":"2026-06-12T05:50:40.007Z","creation":"2025-04-05T09:07:16.008Z"},"accession":"S-EPMC10870076","cross_references":{"pubmed":["38083975"],"doi":["10.1002/advs.202307648"]}}