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Identification of arginine methylation in colorectal cancer across the proteome

Hanjie Chen

Protein arginine methyltransferase (PRMT) catalyses the protein arginine methylation process, which is linked to several illnesses, including cancer. Currently, proteomics technique based on high-resolution mass spectrometry has been used to identify thousands of arginine methylation sites. It has not yet been documented how to identify arginine methylation using clinical samples at the proteome level. Finding monomethyl-arginine (MMA) and asymmetric dimethyl-arginine (ADMA) sites in colorectal cancer (CRC) tissues at the proteome level was the goal of the current investigation. Trypsin digestion of combined CRC tissue samples from 10 individuals with stage II and stage III was followed by additional processing and lyophilization. Methylargininecontaining peptides were isolated and then subjected to high-resolution LC-MS/MS analysis using monomethyl- or asymmetric dimethyl arginine (MMA or ADMA, respectively) motif kits. Colon cancer cells from DLD1 and HCT116 were treated with type I PRMTs inhibitor (MS023) alone or in combination with SN-38. The medicines' impact on CRC cell proliferation and apoptosis was assessed using the WST-1 test and FACS analysis, respectively.