On September 18th, the international academic journal Clinical Cancer Research published the latest research result "Functional silencing of HSD17B2 in prostate cancer promotes disease progression" by Li Zhenfei Research Group of the Institute of Biochemistry and Cell Biology of the Chinese Academy of Sciences.
The development of prostate cancer is closely related to androgen. Therefore, steroid metabolism enzymes involved in androgen synthesis are important targets for clinical treatment of prostate cancer. 17βHSD2 is an important steroid metabolism enzyme in the process of androgen synthesis. This metabolic enzyme catalyzes the conversion of the 17th hydroxyl group of the steroid to the keto group. The 17th hydroxyl group has an important effect on androgenic activity, and the 17th keto group loses the activity of androgen. 17βHSD2 finely regulates the androgen concentration of the active form in vivo by regulation of this site. However, the progress of this type of enzyme and prostate cancer and its related regulatory mechanisms have not been clarified.
Li Zhenfei's research group is dedicated to the study of steroid hormone metabolism and prostate cancer treatment. Through the exploration of key enzymes of steroid metabolism and targeted drugs combined with clinical experiments, new biomarkers and therapeutic targets for clinical diagnosis and treatment of prostate cancer are explored. The team found that the expression of the steroid-metabolizing enzyme 17βHSD2 gradually decreased with the progression of prostate cancer. 17βHSD2 metabolizes testosterone (T) and dihydrotestosterone (DHT) into their precursor small molecules to reduce the androgen concentration of the active form in vivo. Further in vitro and in vivo experiments confirmed that up-regulation of 17βHSD2 expression can inhibit androgen-induced cell proliferation and ectopic tumor growth. After further study, they found that the expression level of 17βHSD2 is regulated by DNA methylation, androgen stress, and variable splicing of mRNA. Interestingly, 17βHSD2 is capable of producing two new splicing bodies, regulated by the shearing factors SRSF1 and SRSF5. These two new shears lose catalytic activity and can promote their degradation by interacting with the full length 17βHSD2.
The study was conducted in collaboration with the Li Zhenfei research team, the Wu Denglong research team of Tongji Hospital affiliated to Tongji University, and the Nima Sharifi research team at the Cleveland Clinic. The work was funded by the Ministry of Science and Technology Key Research and Development Program, the Chinese Academy of Sciences' Strategic Science and Technology Pilot Project, the National Natural Science Foundation, the Chinese Academy of Sciences Youth Innovation Promotion Association, the American Prostate Cancer Foundation and the National Cancer Institute. Thanks to the Protein Science Facility (Shanghai) Zhangjiang Laboratory Mass Spectrometry Platform, Biochemical and Cell Institute Public Technical Service Center and animal platform support.
Source: Chinese Academy of Sciences
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