S-Adenosylmethionine-Dependent Methylation, Protein Arginine Methyltransferases and Cardiovascular Diseases

Methylation, catalyzed by a diverse family of S-adenosylmethionine (SAM)-dependent methyltransferases, is a fundamental biochemical process that regulates the function of proteins, DNA, and RNA. Among these modifications, protein arginine methylation, catalyzed by protein arginine methyltransferases (PRMTs), represents a critical post-translational mechanism regulating transcription, DNA repair, RNA splicing, and signal transduction. Emerging evidence highlights important roles of PRMTs in cardiovascular diseases (CVDs); however, current research is limited by several challenges, including the paradoxical and context-dependent functions of individual PRMTs and the lack of highly specific inhibitors or activators, leaving their therapeutic potential incompletely defined. This review summarizes the classification, structure, and functional characteristics of methyltransferases, with a particular focus on PRMTs and their roles in normal physiology and diverse CVDs. We integrate current knowledge to provide a comprehensive understanding of how PRMTs contribute to cardiovascular pathophysiology by methylating histones, transcription factors, and other functional proteins. Collectively, PRMTs emerge as pivotal regulators in CVD development and progression. Future studies should prioritize resolving the functional duality of specific PRMTs, developing targeted precision therapeutics, and elucidating the roles of less-characterized family members in CVDs.