Restoring Histone Acetylation Accelerates Diabetic Wound Repair by Improving the Spatiotemporal Dynamics of Macrophages.

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

SUBMITTER: Singh K 

PROVIDER: S-EPMC12697871 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature