Prmt2, a member of the protein arginine methyltransferase (PRMT) family, acts as a type I enzyme that catalyzes the arginine methylation of target proteins, producing asymmetric dimethyl arginine [2]. It contains a canonical PRMT methylation core and a unique Src homology 3 domain, and is involved in multiple cellular processes such as histone methylation and transcriptional regulation [2].

In cancer research, Prmt2 has been shown to play significant roles. In renal cell cancer (RCC), its overexpression promotes cell proliferation and motility both in vitro and in vivo by enhancing WNT5A transcriptional expression, suggesting it as a novel therapeutic target [1]. In hepatocellular carcinoma (HCC), Prmt2 is overexpressed and is an independent predictor of poor prognosis. Depletion of Prmt2 in HCC cell lines inhibits cell growth and induces apoptosis, as it activates Bcl2 via histone H3R8 methylation [4]. In glioblastomas, Prmt2 is activated by HIF1α under hypoxic conditions, and its inactivation suppresses hypoxia-induced cell migration, attenuates tumor progression, and enhances chemotherapeutic sensitivity [3]. In acute myeloid leukemia (AML), low Prmt2 expressors show inferior survival and increased pro-inflammatory cytokine signaling, indicating Prmt2 as a key regulator of inflammation in AML [5].

Overall, Prmt2 is crucial in various cellular processes and significantly impacts multiple disease conditions, especially in cancer development. Studies using gene knockout models in these diseases have revealed its role in promoting tumorigenesis, metastasis, and regulating inflammation, providing potential therapeutic targets for treatment.