National Engineering Laboratory for Druggable Gene and Protein Screening, Northeast Normal University, Changchun 130024, China.
IUBMB Life. 2010 Nov;62(11):825-32. doi: 10.1002/iub.390.
Earlier studies identified testes-specific protease 50 (TSP50), which encodes a threonine protease, and showed that it was abnormally reactivated in many breast cancer biopsies. Further, it was shown to be negatively regulated by the p53 gene. However, little is known about the biological function of TSP50. In this study, we applied RNA interference to knockdown TSP50 gene expression in P19 murine embryonal carcinoma stem cells and tested whether this modulated the cell phenotype. The results showed that downregulation of TSP50 expression not only reduced cell proliferation, colony formation, and migration but also induced cell apoptosis. Further investigation revealed that knockdown of TSP50 resulted in greater sensitivity to doxorubicin-induced apoptosis and that activation of caspase-3 was involved in this process.
早期研究鉴定了睾丸特异性蛋白酶 50（TSP50），它编码一种苏氨酸蛋白酶，并表明它在许多乳腺癌活检中异常激活。此外，研究表明它受到 p53 基因的负调控。然而，关于 TSP50 的生物学功能知之甚少。在这项研究中，我们应用 RNA 干扰技术敲低 P19 鼠胚胎癌细胞干细胞中的 TSP50 基因表达，并测试了这是否调节了细胞表型。结果表明，下调 TSP50 表达不仅降低了细胞增殖、集落形成和迁移能力，而且诱导了细胞凋亡。进一步的研究表明，敲低 TSP50 导致对阿霉素诱导的细胞凋亡更加敏感，并且半胱氨酸天冬氨酸蛋白酶-3 的激活参与了这个过程。
