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Hypoxic and oxidant stresses can coexist in biological systems, and oxidant stress has been proposed to activate hypoxia pathways through the inactivation of the oxygen-sensing hypoxia-inducible factor (HIF) prolyl and asparaginyl hydroxylases. Here, we show that despite reduced sensitivity to cellular hypoxia, the HIF asparaginyl hydroxylase-known as FIH, factor inhibiting HIF-is strikingly more sensitive to peroxide than the HIF prolyl hydroxylases. These contrasting sensitivities indicate that oxidant stress is unlikely to signal hypoxia directly to the HIF system, but that hypoxia and oxidant stress can interact functionally as distinct regulators of HIF transcriptional output. © 2012 European Molecular Biology Organization.

Original publication

DOI

10.1038/embor.2012.9

Type

Journal article

Journal

EMBO Reports

Publication Date

01/03/2012

Volume

13

Pages

251 - 257