Protein Arginine Methyltransferase 1: A Multi-Purpose Player in the Development of Cancer and Metabolic Disease

Protein arginine methyltransferase 1 (PRMT1) is the primary enzyme within the PRMT family responsible for generating monomethylarginine and asymmetric dimethylarginine on its protein substrates. Many of these substrates play critical roles in cell proliferation and oncogenesis, making PRMT1 a focal point in cancer research. However, emerging in vitro and in vivo studies suggest that PRMT1 also contributes to metabolic disorders, expanding its relevance beyond cancer biology.

This review provides a comprehensive analysis of PRMT1’s role in epigenetic modulation, transcriptional regulation, DNA damage repair, and signal transduction, particularly in the context of cancer. Additionally, it explores PRMT1’s involvement in metabolic reprogramming, lipid metabolism, and glucose metabolism, linking its activity to metabolic pathologies such as obesity, liver disease, and type 2 diabetes. These findings underscore the multifaceted nature of PRMT1 in both oncogenic and metabolic processes.

Inhibition of PRMT1 has emerged as a promising therapeutic strategy, as preclinical studies have demonstrated the potential of PRMT1 inhibitors to mitigate both cancer progression and metabolic diseases. However, despite these encouraging preclinical results, pharmacological inhibition of PRMT1 has not yet proven effective in clinical trials. Further research is needed to translate these findings into clinically viable treatments, highlighting the importance of continued investigation into PRMT1’s mechanisms and therapeutic potential. JNJ-64619178