Ask about this productRelated genes to: PRMT3 antibody
- Gene:
- PRMT3 NIH gene
- Name:
- protein arginine methyltransferase 3
- Previous symbol:
- HRMT1L3
- Synonyms:
- -
- Chromosome:
- 11p15.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-06-18
- Date modifiied:
- 2014-11-19
Related products to: PRMT3 antibody
Related articles to: PRMT3 antibody
- Protein arginine methyltransferase 3 (PRMT3) is a type I arginine methyltransferase that catalyzes asymmetric dimethylation of arginine residues on diverse substrate proteins. Initially characterized as a regulator of ribosomal protein methylation, PRMT3 has more recently been implicated in several cancer-related processes. Accumulating evidence suggests that PRMT3 is dysregulated in a variety of malignancies, including hepatocellular carcinoma, colorectal cancer, glioblastoma, breast cancer, pancreatic cancer, and non-small cell lung cancer. Through arginine methylation of selected regulatory proteins, PRMT3 has been linked to signaling pathways associated with tumor progression, metabolic adaptation, immune modulation, and therapeutic resistance. Mechanistically, available studies indicate that PRMT3 can regulate RNA-associated networks by methylating RNA-binding proteins and epitranscriptomic regulators such as IGF2BP1 and METTL14, thereby influencing mRNA stability and gene expression programs. In addition, PRMT3 has been reported to contribute to tumor metabolic reprogramming by promoting glycolytic activity and modulating amino acid metabolism through factors including HIF1A, PDHK1, and IDO1. These alterations may support tumor growth and, in some contexts, influence the tumor immune microenvironment. PRMT3 has also been associated with immune evasion, for example through effects on PD-L1 expression and innate immune signaling pathways such as cGAS-STING. Moreover, emerging evidence links PRMT3 to therapeutic resistance through mechanisms involving oncogenic transcript stabilization, immunometabolic remodeling, and drug efflux regulation. In this review, we summarize the current understanding of PRMT3 structure, catalytic mechanisms, and biological functions in cancer. We further discuss its emerging roles in metabolic regulation, immune suppression, and therapy resistance, while distinguishing mechanisms directly supported within specific cancer contexts from broader conceptual models inferred across studies. Overall, current evidence supports PRMT3 as an emerging and context-dependent regulator of tumor biology and a potential target for anticancer therapy. - Source: PubMed
Publication date: 2026/05/01
Jin HuiHuang HuaPan Xin - Protein arginine methyltransferase 3 (PRMT3) is a key member of the PRMT family that catalyzes the arginine methylation of proteins, thereby modulating their structure, localization, or interactions and influencing essential physiological processes, such as cell growth and signal transduction. Its dysregulation is closely associated with tumorigenesis and neurological disorders. PRMT3 is critically involved in cellular processes, such as cell growth, invasion, and apoptosis, making it a promising target for drug discovery. In this review, we summarized the structure and biological functions of PRMT3, particularly the mechanism of action in human diseases. We also evaluated the co-crystal structure of PRMT3 inhibitors. Furthermore, we examined the recent advancements in the development of PRMT3 modulators, including isoform-selective and partially isoform-selective PRMT3 inhibitors as well as PRMT3-targeting PROTACs, from a rational design perspective. Finally, we discussed the existing challenges and future directions in PRMT3-targeted drug discovery. - Source: PubMed
Publication date: 2026/02/04
Yu DongminHe KangMai CunjunLi Meifang - Protein arginine methyltransferases are key epigenetic regulators and promising targets for cancer therapy. PRMT4 plays an important role in transcriptional regulation and tumor progression, yet selective inhibition remains challenging because type I PRMTs share highly conserved catalytic sites. The success of allosteric inhibitors targeting PRMT3 and PRMT6 suggests that selective modulation through regulatory sites outside the catalytic pocket may also be feasible for PRMT4. Motivated by this rationale, we investigated whether PRMT4 undergoes conformational transitions between active and inactive states and whether it contains allosterically targetable pockets capable of regulating its enzymatic activity. Using an integrated computational strategy, we characterized the conformational dynamics and allosteric regulation mechanisms of PRMT4. Structural analysis identified a molecular switch involving order and disorder transitions of the N terminal helices that governs the active inactive transition. Free energy landscape analysis supported that this transition is thermodynamically accessible. We identified a PRMT3 like allosteric pocket, Cavity 1, whose targeting is predicted to disrupt inter chain communication and impair cofactor binding and active site organization. Dynamic residue network analysis further supported Cavity 1 as a functional allosteric site. We also identified a PRMT4 specific pocket, Cavity 2, with a distinct selectivity profile. These findings validate the active inactive switch and identify two druggable allosteric sites. Although experimental validation is required, this work provides a computational framework for the rational design of PRMT4 selective allosteric inhibitors. - Source: PubMed
Publication date: 2026/03/26
Abbas AmrMiao ZhanpengJin JiaYe Fei - Aortic valve calcification increases leaflet stiffness and contributes to the development of calcific aortic valve disease. The molecular and cellular mechanisms underlying calcification remain unclear. Here, we aimed to investigate the role of PRMT3 (protein arginine methyltransferase 3) in valvular calcification and calcific aortic valve disease progression. - Source: PubMed
Publication date: 2026/03/09
Zhang XiHao YanglinHan DongJin XinShang XiaokeZhang LiGan ZhengYe WeicongWang SongLi XiaohanLi RanZheng KexiaoLiu YinghuanZou ZifengTao ZetongLi YilongWang YongjunXia JiahongWu Jie - Age-related macular degeneration (AMD) is a leading cause of blindness in developed countries and a growing global health concern. The multifactorial nature of AMD calls for integrative multi-omics approaches. We summarize studies employing multi-omics in AMD. A comprehensive search in PubMed and Scopus databases identified 561 records with multi-omics criteria, of which duplicates, unrelated and unavailable articles were excluded, resulting in 33 reports. Quality was assessed following the Office of Health Assessment and Translation (OHAT) method, and data was synthesized through standardized evidence tables. Across the reviewed reports, multi-omics approaches were applied to non-clinical and clinical samples, including ocular and systemic fluids. Methodological trends included the widespread use of causal inference approaches (e.g., Mendelian randomization and Bayesian colocalization) and increasing adoption of spatial and single-cell resolution techniques. Converging molecular patterns consistently suggested inflammation, complement activation, angiogenesis, lipid dysregulation, and mitochondrial dysfunction as key processes underlying AMD. Integration of genetic risk with proteomic and metabolomic alterations, enabled the identification of candidate diagnostic and prognostic biomarkers such as carboxyethylpyrrole and PRMT3. Additionally, this review revealed opportunities for personalized medicine in AMD patient stratification, improvement of prediction models, and therapeutic personalization; however, heterogeneity was noted across studies, particularly regarding sample source (systemic vs. ocular), analytical platforms, integration strategies, and ancestry representation. Despite this variability, this review illustrates how integrating multiple omics layers provides a comprehensive and multidimensional understanding of AMD pathology, advancing research towards better diagnosis, prognosis, and therapeutics for these patients. - Source: PubMed
Publication date: 2026/02/03
Castro-Fernández Diana CarolinaCañizo-Outeriño AntonioCuartero-Martínez AndreaGil-Martinez MariaMondelo-Garcia CristinaGonzález-Barcia MiguelÁlvarez-Barrios AnaFernández-Ferreiro Anxo