Abstract
Aim: p53 is reportedly activated without any genotoxicity through redox modulation of redox factor 1 (REF1). REF1 is documented to modulate the redox status under selenomethionine (SeMet). In this study, we investigated the mechanism of p53 stabilization by SeMet. Materials and Methods: We mainly used ubiquitination assay and immunoprecipitation to determine the potential role of REF1 and c-jun N-terminal kinase 1 (JNK) in modulation of p53 stabilization by SeMet. Results: The amount of ubiquitinated p53 decreased significantly under SeMet treatment, suggesting that SeMet might inhibit the proteasome-dependent degradation of p53. In addition, we observed that JNK was considerably associated with p53 in REF1 siRNA-treated cells, implying a possible role for SeMet-induced REF1 activity in modulation of the interaction between JNK and p53 via changes in p53 redox status. Conclusion: Our results suggest that the alternate mechanism of p53 stabilization by SeMet might provide an important clue in elucidating the molecular mechanism of chemopreventative compounds against various oxidative stresses.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3645-3652 |
| Number of pages | 8 |
| Journal | Anticancer Research |
| Volume | 33 |
| Issue number | 9 |
| State | Published - Sep 2013 |
Keywords
- Cancer prevention
- JNK
- P53
- Protein stability
- Redox factor 1
- Selenomethionine
- Ubiquitination
ASJC Scopus subject areas
- Oncology
- Cancer Research
