{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bai YP"],"funding":["Anhui Provincial Key Research and Development Plan","National Natural Science Foundation of China"],"pagination":["103949"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12704266"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["88"],"pubmed_abstract":["Septic liver injury is a major complication of sepsis, driven in part by oxidative stress-induced macrophage inflammasome activation and hepatocyte apoptosis. β-Hydroxybutyrate (β-OHB), a key ketone body, induces lysine β-hydroxybutyrylation (Kbhb), a novel post-translational modification, yet its role in septic liver injury remains unclear. In this study, we demonstrated that β-OHB markedly increased Kbhb modification of superoxide dismutase 2 (SOD2), a mitochondrial antioxidant enzyme, in both macrophages and hepatocytes. Mechanistically, β-OHB promoted Kbhb at lysine 68 of SOD2, thereby preventing ubiquitin-proteasome-mediated degradation, and then stabilizing the protein, which enhanced its enzymatic activity, and reduced mitochondrial reactive oxygen species accumulation. Consequently"],"journal":["Redox biology"],"pubmed_title":["β-Hydroxybutyrate ameliorates lipopolysaccharide-induced liver injury through β-hydroxybutyrylation of the SOD2 protein in mice."],"pmcid":["PMC12704266"],"funding_grant_id":["81970699","AHWJ2024Aa10024"],"pubmed_authors":["Wang DG","Lv K","Li ZC","Zhang Y","Chen ZY","Bai YP","Zha L","Li K","Wan SJ","Zhang CW","Sun Y","Kong X"],"additional_accession":[]},"is_claimable":false,"name":"β-Hydroxybutyrate ameliorates lipopolysaccharide-induced liver injury through β-hydroxybutyrylation of the SOD2 protein in mice.","description":"Septic liver injury is a major complication of sepsis, driven in part by oxidative stress-induced macrophage inflammasome activation and hepatocyte apoptosis. β-Hydroxybutyrate (β-OHB), a key ketone body, induces lysine β-hydroxybutyrylation (Kbhb), a novel post-translational modification, yet its role in septic liver injury remains unclear. In this study, we demonstrated that β-OHB markedly increased Kbhb modification of superoxide dismutase 2 (SOD2), a mitochondrial antioxidant enzyme, in both macrophages and hepatocytes. Mechanistically, β-OHB promoted Kbhb at lysine 68 of SOD2, thereby preventing ubiquitin-proteasome-mediated degradation, and then stabilizing the protein, which enhanced its enzymatic activity, and reduced mitochondrial reactive oxygen species accumulation. Consequently","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-06-07T05:20:12.052Z","creation":"2026-06-07T03:07:01.458Z"},"accession":"S-EPMC12704266","cross_references":{"pubmed":["41319591"],"doi":["10.1016/j.redox.2025.103949"]}}