Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 279, Issue 7, Pages 5837-5845Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M307547200
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- NIEHS NIH HHS [ES011195] Funding Source: Medline
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The gp91(phox) 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.
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