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

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.
AuthorsLiang Zhou, Yong-Li Bao, Yu Zhang, Yin Wu, Chun-Lei Yu, Yan-Xin Huang, Ying Sun, Li-Hua Zheng, Yu-Xin Li
JournalIUBMB life (IUBMB Life) Vol. 62 Issue 11 Pg. 825-32 (Nov 2010) ISSN: 1521-6551 [Electronic] England
PMID21086474 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Tumor Suppressor Protein p53
  • Doxorubicin
  • Serine Endopeptidases
  • testis-specific protease 50
  • Animals
  • Apoptosis (drug effects)
  • Cell Line, Tumor
  • Cell Movement (drug effects)
  • Cell Proliferation (drug effects)
  • Down-Regulation
  • Doxorubicin (pharmacology)
  • Gene Knockdown Techniques
  • Mice
  • RNA Interference
  • Serine Endopeptidases (genetics, physiology)
  • Tumor Suppressor Protein p53 (physiology)

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