| First Author | Go YM | Year | 2004 |
| Journal | J Biol Chem | Volume | 279 |
| Issue | 7 | Pages | 5837-45 |
| PubMed ID | 14638694 | Mgi Jnum | J:88482 |
| Mgi Id | MGI:3033514 | Doi | 10.1074/jbc.M307547200 |
| Citation | Go YM, et al. (2004) H2O2-dependent activation of GCLC-ARE4 reporter occurs by mitogen-activated protein kinase pathways without oxidation of cellular glutathione or thioredoxin-1. J Biol Chem 279(7):5837-45 |
| abstractText | The gp91phox homologue Nox1 produces H2O2, which induces cell growth, transformation, and tumorigenicity. However, it has not been clear whether H2O2 effects are mediated indirectly via a generally oxidizing cellular environment or whether H2O2 more directly targets specific signaling pathways. Here, we investigated signaling by H2O2 induced by Nox1 overexpression using a luciferase reporter regulated by the antioxidant response element ARE4. Surprisingly, Nox1-derived H2O2 activated the reporter gene 15-fold with no effect on the redox state of the major thiol antioxidant substances, glutathione and thioredoxin. H2O2 signaling to ARE4 was mediated by activation of both the c-Jun N-terminal kinase and ERK1/2 pathways modulated by Ras. Thus, 'redox signaling' resulting in kinase signaling pathways is distinct from 'oxidative stress,' and is mediated by discrete, localized redox circuitry. |
