Methyl-CpG-binding 2 K271 lactylation-mediated M2 macrophage polarization inhibits atherosclerosis

Methyl-CpG-binding 2 K271 lactylation-mediated M2 macrophage polarization inhibits atherosclerosis

2024.07.08 | Liangqi Chen, MeiJu Zhang, Xueyan Yang, Yanan Wang, Tuo Huang, Xin Li, Yunting Ban, Qifeng Li, Qingyuan Yang, Yongxiang Zhang, Yang Zheng, Di Wang, Xiaojie Wang, Xiujie Shi, Maomao Zhang, Yong Sun, Jian Wu
Exercise-induced lactylation of MeCP2 K271 promotes atherosclerosis regression by enhancing M2 macrophage polarization. This study reveals that exercise reduces atherosclerosis in ApoE $ ^{-/-} $ mice through the lactylation of MeCP2 K271, which promotes pro-repair M2 macrophage polarization, reduces plaque area, shrinks necrotic cores, decreases lipid deposition, and increases collagen content. Lactylation of MeCP2 K271 is mediated by P300 and regulated by HDAC3. The interaction between MeCP2 K271 lactylation and H3K36me3 leads to increased chromatin accessibility and transcriptional repression of RUNX1, promoting M2 macrophage polarization and plaque stability. Pharmacological inhibition of RUNX1 enhances atheroprotective effects by promoting M2 macrophage polarization. These findings suggest that interventions enhancing MeCP2 K271 lactylation can promote plaque stabilization and reduce the risk of atherosclerotic cardiovascular disease. The study also identifies RUNX1 as a potential drug target for exercise therapy.Exercise-induced lactylation of MeCP2 K271 promotes atherosclerosis regression by enhancing M2 macrophage polarization. This study reveals that exercise reduces atherosclerosis in ApoE $ ^{-/-} $ mice through the lactylation of MeCP2 K271, which promotes pro-repair M2 macrophage polarization, reduces plaque area, shrinks necrotic cores, decreases lipid deposition, and increases collagen content. Lactylation of MeCP2 K271 is mediated by P300 and regulated by HDAC3. The interaction between MeCP2 K271 lactylation and H3K36me3 leads to increased chromatin accessibility and transcriptional repression of RUNX1, promoting M2 macrophage polarization and plaque stability. Pharmacological inhibition of RUNX1 enhances atheroprotective effects by promoting M2 macrophage polarization. These findings suggest that interventions enhancing MeCP2 K271 lactylation can promote plaque stabilization and reduce the risk of atherosclerotic cardiovascular disease. The study also identifies RUNX1 as a potential drug target for exercise therapy.
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