| الملخص: |
Among women in the US, breast cancer is the second leading cause of cancer related death, only preceded by lung cancer. This study primarily focuses on HER2, an oncogene involved in approximately 20% of all breast cancer cases. Our previous studies have found that there is a link between HER2 and nitric oxide (NO). This study aims to address the mechanistic bases of the link between HER2 and NO. Here, the primarily focus is on S nitrosylation, a post translational modification mediated by NO and its effect on the HER2 function. For this purpose, cysteine to alanine substitution were generated at predicted S nitrosylation sites of HER2 to determine their actual involvement in S nitrosylation. The results suggests that mutation at residues 7 and 600 impacts HER2 S nitrosylation, while also affecting HER2 expression (C7A) and activity (C7A and C600A). However, future experiments are essential to investigate whether S nitrosylation of HER2 is indeed involved in breast cancer initiation and progression. Such information could be utilized for the development of a therapeutic method that prevents S nitrosylation of HER2. |
