AI Article Synopsis
- - The study focuses on the testes-specific protease 50 (TSP50), which is linked to breast cancer and negatively regulated by the p53 gene, but its biological function is not well understood.
- - Researchers used RNA interference to decrease TSP50 expression in embryonal carcinoma cells and found that this led to reduced cell growth, colony formation, and migration, along with increased cell apoptosis.
- - Furthermore, TSP50 knockdown made the cells more sensitive to doxorubicin (a chemotherapy drug), indicating that caspase-3 activation plays a key role in the apoptosis process triggered by TSP50 reduction.
Article 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.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1002/iub.390 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!