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Immunol."],"abstract":"<jats:p>Protein arginine methyltransferase 3, a type I PRMT family member, plays pleiotropic roles in chronic inflammatory diseases through its catalysis of asymmetric dimethylarginine modifications. Chronic inflammation, marked by metabolic dysregulation, immune dysfunction, and tissue fibrosis, drives diverse pathologies including non-alcoholic fatty liver disease, chronic kidney disease, and atherosclerosis. In this review, we comprehensively dissect the multifaceted contributions and molecular mechanisms of PRMT3 in inflammation-associated disorders. Mechanistically, PRMT3 aggravates inflammatory-metabolic dyshomeostasis in chronic inflammation via LXR\u03b1\/HIF-1\u03b1 methylation, thereby accelerating vascular calcification and fibrosis. Paradoxically, it simultaneously suppresses antiviral immunity and facilitates tumor immune evasion, underscoring its dual role as a molecular \u201cdouble-edged sword\u201d. Notably, PRMT3 inhibitors such as SGC707 demonstrate preclinical promise in modulating lipid metabolism and curtailing tumor progression. However, challenges persist regarding tissue specificity and off-target toxicity, necessitating further refinement. Collectively, these results provide a new molecular basis for therapeutic approaches targeting PRMT3.<\/jats:p>","DOI":"10.3389\/fimmu.2025.1663258","type":"journal-article","created":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T06:38:20Z","timestamp":1767940700000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":7,"title":["PRMT3 at the crossroads of inflammation: dual roles in metabolic reprogramming and immune dysregulation in chronic diseases"],"prefix":"10.3389","volume":"16","author":[{"given":"Huining","family":"Hou","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiaojiao","family":"Meng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yingqing","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xili","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhuqing","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qianqian","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Min","family":"Zheng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zebo","family":"Jiang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2026,1,9]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","DOI":"10.3892\/mmr.2019.10111","article-title":"Regulation of histone arginine methylation\/demethylation by methylase and demethylase (Review)","volume":"19","author":"Zhang","year":"2019","journal-title":"Mol Med Rep"},{"key":"B2","doi-asserted-by":"publisher","DOI":"10.3389\/fphar.2018.00173","article-title":"Identification of a novel protein arginine methyltransferase 5 inhibitor in non-small cell lung cancer by structure-based virtual screening","volume":"9","author":"Wang","year":"2018","journal-title":"Front Pharmacol"},{"key":"B3","doi-asserted-by":"publisher","first-page":"7436","DOI":"10.3390\/molecules27217436","article-title":"Structure-based discovery and biological assays of a novel PRMT5 inhibitor for non-small cell lung cancer","volume":"27","author":"Chen","year":"2022","journal-title":"Molecules"},{"key":"B4","doi-asserted-by":"publisher","DOI":"10.1007\/s00018-019-03145-x","article-title":"Protein arginine methyltransferases: insights into the enzyme structure and mechanism at the atomic level","volume":"76","author":"Tewary","year":"2019","journal-title":"Cell Mol Life Sci"},{"key":"B5","doi-asserted-by":"publisher","DOI":"10.1016\/j.str.2012.06.001","article-title":"An allosteric inhibitor of protein arginine methyltransferase 3","volume":"20","author":"Siarheyeva","year":"2012","journal-title":"Structure"},{"key":"B6","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1177\/1087057111422256","article-title":"Fluorescence-based methods for screening writers and readers of histone methyl marks","volume":"17","author":"Allali-Hassani","year":"2012","journal-title":"J Biomol Screen"},{"key":"B7","doi-asserted-by":"publisher","first-page":"60","DOI":"10.2337\/db13-1394","article-title":"PRMT3 regulates hepatic lipogenesis through direct interaction with LXR\u03b1","volume":"64","author":"Kim","year":"2015","journal-title":"Diabetes"},{"key":"B8","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1186\/s10020-023-00759-7","article-title":"PRMT3 methylates HIF-1\u03b1 to enhance the vascular calcification induced by chronic kidney disease","volume":"30","author":"Zhou","year":"2024","journal-title":"Mol Med"},{"key":"B9","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M006445200","article-title":"PRMT3 is a distinct member of the protein arginine N-methyltransferase family. 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