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Am J Physiol Lung Cell Mol Physiol (May 24, 2002). doi:10.1152/ajplung.00014.2002
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Articles in PresS, published online ahead of print May 24, 2002
Am J Physiol Lung Cell Mol Physiol, 10.1152/ajplung.00014.2002
Submitted on January 11, 2002
Accepted on May 17, 2002

Hypoxic but not anoxic stabilization of HIF-1alpha requires mitochondrial reactive oxygen species

Clara Schroedl1, David S. McClintock1, G.R. Scott Budinger1, and Navdeep S. Chandel1*

1 Division of Pulmonary & Critical Care Medicine, Northwestern University Medical School, Chicago, IL, USA

* To whom correspondence should be addressed. E-mail: nav{at}northwestern.edu.

The molecular mechanisms by which cells detect hypoxia (1.5% O2) resulting in the stabilization of hypoxia-inducible factor 1 alpha (HIF-1{alpha}) protein remain unclear. One model proposes that mitochondrial generation of reactive oxygen species (ROS) are required to stabilize HIF-1{alpha} 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 ({rho}° cells) fail to generate ROS or stabilize HIF-1{alpha} protein in response to hypoxia. In the present study, we investigated the role of mitochondria in regulating HIF-1{alpha} protein stabilization under anoxia (0% O2). Wild-type A549 and HT1080 cells stabilized HIF-1{alpha} protein in response to hypoxia and anoxia. {rho}°-A549 cells and {rho}°-HT1080 cells failed to accumulate HIF-1{alpha} protein in response to hypoxia. However, both {rho}°-A549 and {rho}°-HT1080 were able to stabilize HIF-1{alpha} protein levels in response to anoxia. Rotenone inhibited hypoxic but not anoxic stabilization of HIF-1{alpha} protein. These results indicate that a functional electron transport chain is required for hypoxic but not anoxic stabilization of HIF-1{alpha} protein.




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