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Knockdown of TSP50 inhibits cell proliferation and induces apoptosis in P19 cells

✍ Scribed by Liang-Zhou; Yong-Li Bao; Yu Zhang; Yin Wu; Chun-Lei Yu; Yan-Xin Huang; Ying Sun; Li-Hua Zheng; Yu-Xin Li


Publisher
John Wiley and Sons
Year
2010
Tongue
English
Weight
365 KB
Volume
62
Category
Article
ISSN
1521-6543

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✦ Synopsis


Abstract

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. © 2010 IUBMB IUBMB Life, 2010


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