谷氨酰胺分解
巨噬细胞极化
SIRT3
细胞生物学
化学
巨噬细胞
生物化学
生物
糖酵解
新陈代谢
酶
锡尔图因
NAD+激酶
体外
作者
Wei Zhou,Gaolei Hu,Jianli He,Tianshi Wang,Yong Zuo,Ying Cao,Quan Zheng,Jun Tu,Jiao Ma,Rong Cai,Yalan Chen,Qiuju Fan,Baijun Dong,Hongsheng Tan,Qi Wang,Wei Xue,Jinke Cheng
出处
期刊:Cell Reports
[Elsevier]
日期:2022-04-01
卷期号:39 (2): 110660-110660
被引量:48
标识
DOI:10.1016/j.celrep.2022.110660
摘要
The metabolic program is altered during macrophage activation and influences macrophage polarization. Glutaminolysis promotes accumulation of α-ketoglutarate (αKG), leading to Jumonji domain-containing protein D3 (Jmjd3)-dependent demethylation at H3K27me3 during M2 polarization of macrophages. However, it remains unclear how αKG accumulation is regulated during M2 polarization of macrophages. This study shows that SENP1-Sirt3 signaling controls glutaminolysis, leading to αKG accumulation during IL-4-stimulated M2 polarization. Activation of the SENP1-Sirt3 axis augments M2 macrophage polarization through the accumulation of αKG via glutaminolysis. We also identify glutamate dehydrogenase 1 (GLUD1) as an acetylated protein in mitochondria. The SENP1-Sirt3 axis deacetylates GLUD1 and increases its activity in glutaminolysis to promote αKG production, leading to M2 polarization of macrophages. Therefore, SENP1-Sirt3 signaling plays a critical role in αKG accumulation via glutaminolysis to promote M2 polarization.
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