Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0014-5793(03)00338-7
Title: Redox stress regulates cell proliferation and apoptosis of human hepatoma through Akt protein phosphorylation
Authors: Shi, D.-Y.
Deng, Y.-R. 
Liu, S.-L.
Zhang, Y.-D.
Wei, L.
Keywords: Akt phosphorylation
Antioxidant
Apoptosis
Electron spin resonance
Reactive oxygen species
Redox state
Issue Date: 8-May-2003
Source: Shi, D.-Y., Deng, Y.-R., Liu, S.-L., Zhang, Y.-D., Wei, L. (2003-05-08). Redox stress regulates cell proliferation and apoptosis of human hepatoma through Akt protein phosphorylation. FEBS Letters 542 (1-3) : 60-64. ScholarBank@NUS Repository. https://doi.org/10.1016/S0014-5793(03)00338-7
Abstract: Employing a spin trapping agent combined with electron spin resonance spectroscopy, we were able to capture reactive oxygen species (ROS) in living hepatoma cells and first found that the trapped ROS was superoxide anion (O2 .-). O2 .- suppressed by treatment with diphenylene iodonium, a flavoprotein inhibitor, was generated by the flavoprotein-containing NADPH-oxidase complex. Applying endogenous/exogenous pro-oxidant or antioxidant causes different redox states in hepatoma cells. Akt activity and cell growth were significantly stimulated by treating hepatoma cells with low concentration of ROS, which could be abolished by adding antioxidants. The phosphatidylinositol 3-kinase (PI3K) inhibitor wortmannin (0.15 μM) inhibited Akt phosphorylation induced by ROS. Our results indicate that hepatoma cell growth is ROS-dependent, and fluctuation of the intracellular redox state may regulate hepatoma cell growth through Akt phosphorylation and the PI3K/Akt pathway, resulting in a broad array of responses from cellular proliferation to apoptosis. © 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societes.
Source Title: FEBS Letters
URI: http://scholarbank.nus.edu.sg/handle/10635/107487
ISSN: 00145793
DOI: 10.1016/S0014-5793(03)00338-7
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