AI Article Synopsis
- The p53 tumor suppressor is an important target for cancer therapies, and previous research showed that protoporphyrin IX (PpIX) disrupts its interaction with MDM2, leading to increased p53 levels and triggering cell death in cancer cells.
- Recent findings demonstrate that PpIX directly binds to the N-terminal domain of p53, which is key for its activation.
- The study also indicates that PpIX can induce apoptosis in p53-null cancer cells by interacting with p73, suggesting a broader mechanism of action in promoting cancer cell death.
Article Abstract
The p53 tumor suppressor is recognized as a promising target for anti-cancer therapies. We previously reported that protoporphyrin IX (PpIX) disrupts the p53/murine double minute 2 (MDM2) complex and leads to p53 accumulation and activation of apoptosis in HCT 116 cells. Here we show the direct binding of PpIX to the N-terminal domain of p53. Furthermore, we addressed the induction of apoptosis in HCT 116 p53-null cells by PpIX and revealed interactions between PpIX and p73. We propose that PpIX disrupts the p53/MDM2 or MDMX and p73/MDM2 complexes and thereby activates the p53- or p73-dependent cancer cell death.
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| http://dx.doi.org/10.1016/j.febslet.2010.12.004 | DOI Listing |
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