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requires
mitochondrial reactive oxygen species
Division of Pulmonary and Critical Care Medicine, Department of Medicine, Northwestern University Medical School, Chicago, Illinois 60611
The molecular mechanisms by which cells
detect hypoxia (1.5% O2), resulting in the stabilization
of hypoxia-inducible factor 1
(HIF-1) protein remain
unclear. One model proposes that mitochondrial generation of
reactive oxygen species is required to stabilize HIF-1 protein.
Primary evidence for this model comes from the observation that cells
treated with complex I inhibitors, such as rotenone, or cells that lack
mitochondrial DNA (
0-cells) fail to generate reactive
oxygen species or stabilize HIF-1 protein in response to hypoxia. In
the present study, we investigated the role of mitochondria in
regulating HIF-1 protein stabilization under anoxia (0%
O2). Wild-type A549 and HT1080 cells stabilized HIF-1
protein in response to hypoxia and anoxia. The 0-A549
cells and 0-HT1080 cells failed to accumulate HIF-1
protein in response to hypoxia. However, both 0-A549 and
0-HT1080 were able to stabilize HIF-1 protein levels
in response to anoxia. Rotenone inhibited hypoxic, but not anoxic,
stabilization of HIF-1 protein. These results indicate that a
functional electron transport chain is required for hypoxic but not
anoxic stabilization of HIF-1 protein.
rho zero; rotenone; complex I
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