Ozmen, EsmaAyan, DurmusOnder, Cagatay EmirAkin, Dilara FatmaKose, BurcuSari, IsmailYazici, Cevat2024-11-072024-11-0720242667-663Xhttps://doi.org/10.4328/ACAM.22100https://hdl.handle.net/11480/15921Aim: Epoxyeicosanoids function as signal mediators in critical biological processes such as platelet aggregation, vasodilation, and anti -inflammation. With all these properties, Epoxyeicosanoids have been associated with many diseases. Metabolism of epoxyeicosanoids is carried out by soluble epoxide hydrolase enzymes, and as a result dihydroxyeicosatrienoic acids, which is a less active form than epoxyeicosanoids, are formed. In our study, SNP/mutation analysis was performed in the gene region responsible for the hydrolase activity of EPHX2, which encodes the soluble epoxide hydrolase enzyme. Material and Methods: The study consisted of two groups: a healthy group with 30 individuals and a T2DM patient group with 40 individuals. SNP/mutation analysis in the gene region responsible for the hydrolase activity of EPHX2 in both groups was performed by Sanger sequencing using appropriate primers. Result: A total of 12 mutations were detected in both groups as a result of Sanger sequencing. Two of the 12 detected mutations were missense mutations (p.Asn359Thr and p.Ser412Arg). It was determined that the pathogenic scores of these mutations were close to 1 for Poly-Phen2 and 0-100 for SNAP. In addition, two (c.1058+165C>T and c.1058+146G>A) SNPs were detected in the intron we observed in the T2DM group, which has not been detected and defined before in our study. Discussion: We believe that the mutations detected in our study, especially those that cause amino acid changes, may cause T2DM susceptibility in healthy individuals and progression of the disease pathogenesis in the T2DM group. We think that the detection of c.1058+165C>T and c.1058+146G>A mutations for the first time in our study will guide the next studies.eninfo:eu-repo/semantics/openAccessT2DMMutationsEHEPHX2Article15534434910.4328/ACAM.22100WOS:001222910000006N/A