Phosphorylation of p68 RNA helicase by p38 MAP kinase contributes to colon cancer cells apoptosis induced by oxaliplatin.

Abstract

BACKGROUND:

We previously demonstrated that p68 phosphorylation at threonine residues correlates with cancer cell apoptosis under the treatments of TNF-α and TRAIL (Yang, L. Mol Cancer Res Vol 3, pp 355-63 2005).

RESULTS:

In this report, we characterized the role of p68 phosphorylation in apoptosis induction under the treatment of oxaliplatin in the colon cancer cells. Our data suggest that oxaliplatin treatment activates p38 MAP kinase, which subsequently phosphorylates p68 at T564 and/or T446. The phosphorylation of p68, at least partially, mediates the effects of the drug on apoptosis induction, as mutations at these two sites greatly reduce the cancer cell death.

CONCLUSION:

Our studies reveal an important molecular mechanism that mediates the effects of anti-cancer drug, providing a potential strategy for improving cancer treatment.

• Authors: Heena Dey, Zhi-Ren Liu
• Journal: BMC cell biology (BMC Cell Biol) Vol. 13 Pg. 27 (Oct 31 2012) ISSN: 1471-2121 [Electronic] England
• PMID: 23110695 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't)

Chemical References

• Antineoplastic Agents
• Organoplatinum Compounds
• Oxaliplatin
• p38 Mitogen-Activated Protein Kinases
• DEAD-box RNA Helicases

Topics

• Antineoplastic Agents (toxicity)
• Apoptosis (drug effects)
• DEAD-box RNA Helicases (metabolism)
• HCT116 Cells
• Humans
• Organoplatinum Compounds (toxicity)
• Oxaliplatin
• Phosphorylation
• p38 Mitogen-Activated Protein Kinases (metabolism)