PRMT1 promotes H2O2 induced cardiomyocytes cell via mediating arginine methylation of P53.

BACKGROUND

Abnormal methylation of protein arginine can cause dysfunction of cardiomyocytes, it is important to further elucidate the molecular mechanism.

METHOD: Candidate protein arginine methyltransferases (PRMTs) were selected using blood samples of myocardial infarction (MI) and control group. The isolated primary cardiomyocyte (PC) and H9C2 cells were treated with H2O2 to mimic MI in vitro and rats with myocardial ischemia-reperfusion (I/R) were established to mimic MI in vivo. The protein content of PRMT1 methylation product P53 was detected to reflect the PRMT1 activity.

RESULT: PRMT1 was aberrant upregulated in MI models. PRMT1 ablation suppressed cell apoptosis and inflammatory cytokine secretion to reverse the H2O2 function. The upregulation of PRMT1 accelerated the degradation of P53 protein through the arginine methylation. Inhibition of PRMT1 alleviated cardiac damage after I/R in rats.

CONCLUSION

PRMT1 promoted MI by mediating arginine methylation of P53. PRMT1 may be a promising therapeutic target for MI.