{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T11:18:58Z","timestamp":1788261538856,"version":"build-2803163510"},"reference-count":80,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Physiol."],"abstract":"<jats:p>Protein arginine methyltransferases (PRMTs) constitute a family of nine enzymes that catalyze the post-translational methylation of arginine residues on histone and non-histone proteins. This epigenetic modification regulates diverse cellular processes including gene transcription, RNA splicing, signal transduction, and protein-protein interactions. Emerging evidence indicates that dysregulated PRMT activity contributes significantly to the pathogenesis of cardiovascular diseases (CVDs), including atherosclerosis, hypertension, heart failure, and myocardial infarction. This review synthesizes current literature on PRMT-mediated mechanisms in cardiovascular pathology, examining the roles of individual PRMT isoforms, their downstream substrates, and the therapeutic implications of PRMT modulation. PRMT1, PRMT5, and PRMT7 demonstrate cardioprotective functions under physiological conditions but contribute to pathological remodeling when dysregulated. The PRMT-DDAH-ADMA axis emerges as a critical regulator of endothelial nitric oxide pro-duction and vascular homeostasis. Type I PRMTs generate asymmetric dimethylarginine (ADMA), an endogenous nitric oxide synthase inhibitor that promotes endothelial dysfunction and atherosclerosis. Type II PRMTs, particularly PRMT5, regulate cardiac fibroblast activation, hypertrophic signaling, and vascular smooth muscle cell phenotypic switching. PRMTs represent promising therapeutic targets for cardiovascular disease intervention. Selective PRMT inhibitors have demonstrated efficacy in preclinical models of cardiac hypertrophy, fibrosis, and ischemic injury. Future research should focus on developing isoform-specific inhibitors with favorable safety profiles and establishing biomarker-guided patient selection strategies for PRMT-targeted therapies.<\/jats:p>","DOI":"10.3389\/fphys.2026.1904070","type":"journal-article","created":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T09:15:15Z","timestamp":1788254115000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["Protein arginine methyltransferases in cardiovascular disease: mechanisms, therapeutic potential, and future directions"],"prefix":"10.3389","volume":"17","author":[{"given":"Ting","family":"Zhang","sequence":"first","affiliation":[{"name":"Department of Cardiovascular Medicine, Karamay Central Hospital","place":["Karamay, Xinjiang, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hong","family":"Lei","sequence":"additional","affiliation":[{"name":"Department of Cardiovascular Medicine, Karamay Central Hospital","place":["Karamay, Xinjiang, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chunmei","family":"Zhang","sequence":"additional","affiliation":[{"name":"Department of Cardiovascular Medicine, Karamay Central Hospital","place":["Karamay, Xinjiang, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2026,9,1]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1007\/s00018-021-04097-x","article-title":"PRMT7 ablation in cardiomyocytes causes cardiac hypertrophy and fibrosis through \u03b2-catenin dysregulation","volume":"79","author":"Ahn","year":"2022","journal-title":"Cell. 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