{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Singh K"],"funding":["Deutsche Forschungsgemeinschaft","Ministry of Science, Research and the Arts Baden-Württemberg (MWK) and the German Research Foundation (DFG) through"],"pagination":["e04920"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12697871"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(46)"],"pubmed_abstract":["Dysregulation of macrophage populations at the wound site is responsible for the non-healing state of chronic wounds. The underlying mechanisms in diabetic conditions at single cell resolution and therapeutic advances remain, however, largely unexplored. Here, it is reported that acetyl histone-H3 (Lys27), an epigenetic mark regulating the macrophage transcriptome, is lost in the hostile tissue microenvironment of diabetes. Diabetic conditions suppress the acetylation of histone, a critical regulator of trained immunity, by activating histone deacetylase (HDAC)-dependent deacetylation pathways. This, in consequence, suppresses STAT1 signaling in macrophages under diabetic conditions. Interestingly, butyrate, a potent HDAC inhibitor, restores the acetyl histone-H3 (Lys27)-dependent transcri"],"journal":["Advanced science (Weinheim, Baden-Wurttemberg, Germany)"],"pubmed_title":["Restoring Histone Acetylation Accelerates Diabetic Wound Repair by Improving the Spatiotemporal Dynamics of Macrophages."],"pmcid":["PMC12697871"],"funding_grant_id":["35/1503-1 FUGG","450627322","251293561"],"pubmed_authors":["Pandey RK","Scharffetter-Kochanek K","Singh K","Hainzl A","Wlaschek M","Haas P","Wang Y","Krug L","Koroma AK","Aghapour M","Maity P","Cheng J"],"additional_accession":[]},"is_claimable":false,"name":"Restoring Histone Acetylation Accelerates Diabetic Wound Repair by Improving the Spatiotemporal Dynamics of Macrophages.","description":"Dysregulation of macrophage populations at the wound site is responsible for the non-healing state of chronic wounds. The underlying mechanisms in diabetic conditions at single cell resolution and therapeutic advances remain, however, largely unexplored. Here, it is reported that acetyl histone-H3 (Lys27), an epigenetic mark regulating the macrophage transcriptome, is lost in the hostile tissue microenvironment of diabetes. Diabetic conditions suppress the acetylation of histone, a critical regulator of trained immunity, by activating histone deacetylase (HDAC)-dependent deacetylation pathways. This, in consequence, suppresses STAT1 signaling in macrophages under diabetic conditions. Interestingly, butyrate, a potent HDAC inhibitor, restores the acetyl histone-H3 (Lys27)-dependent transcri","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-06-06T02:18:54.316Z","creation":"2026-05-24T03:11:56.995Z"},"accession":"S-EPMC12697871","cross_references":{"pubmed":["41051359"],"doi":["10.1002/advs.202504920"]}}