Macrophage PRMT9 Ameliorates Acute Myocardial Infarction by Promoting Symmetric Dimethylation and Degradation of STAT1
Authors' conclusion
This study discovered a novel PRMT9-driven symmetric dimethylation of STAT1, resulting in its ubiquitination and lysosomal degradation, which suppresses the proinflammatory polarization of macrophages and mitigates myocardial damage following MI.
Study context
- Population
- Murine models of myocardial infarction (MI); human PBMCs from healthy individuals and patients with MI
- Comparison
- PRMT9 deficiency or overexpression in macrophages in murine MI models
Methodological detailsmacrophage-specific Prmt9 knockout mice, macrophage-specific overexpression AAV vectors
- Macrophage-specific Prmt9 knockout mice
- Macrophage-specific overexpression AAV vectors
Main finding
As reported in the abstract
- PRMT9 highly expressed in murine and human PBMCs in early stages of MI
- PRMT9 deficiency enhanced M1-like polarization and exacerbated cardiac damage in murine MI
- Macrophage PRMT9 overexpression reduced infarct size, accelerated inflammation resolution and improved cardiac function after MI
- PRMT9 binds STAT1 and facilitates its symmetric dimethylation at R588 and R736, promoting STAT1 ubiquitination and selective autophagic degradation (via SQSTM1/p62 and NDP52/CALCOCO2), suppressing excessive M1-like responses
- STAT1 inhibitor fludarabine mitigated the exacerbation of post-MI myocardial injury induced by macrophage PRMT9 deletion
Original publication
Macrophage PRMT9 Ameliorates Acute Myocardial Infarction by Promoting Symmetric Dimethylation and Degradation of STAT1. Circulation. Published 11 February 2026. doi:10.
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