Abstract
Current concepts of cellular oxygen-sensing include an isoform of the neutrophil NADPH oxidase, different electron carrier units of the mitochondrial electron transport chain (ETC), heme oxygenase-2 (HO-2), and a subfamily of 2-oxoglutarate dependent dioxygenases termed HIF (hypoxia inducible factor) prolyl hydroxylases (PHDs) and HIF asparagyl hydroxylase FIH-1 (factor-inhibiting HIF). Different oxygen sensitivities, cell-specific distribution and subcellular localization of specific oxygen-sensing cascades involving reactive oxygen species (ROS) as second messengers may help to tailor various adaptive responses according to differences in tissue oxygen availability. Herein, we propose an integrated model for these various oxygen-sensing mechanisms that very efficiently regulate HIF-alpha activity and plasma membrane potassium-channel (PMPC) conductivity.
Keywords
Reactive oxygen speciesOxygenBiochemistryNADPH oxidaseHemeMitochondrionChemistryHypoxia-inducible factorsOxidase testCell biologyElectron transport chainOxygenaseGene isoformEnzymeBiologyGene
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Publication Info
- Year
- 2006
- Type
- review
- Volume
- 71
- Issue
- 2
- Pages
- 195-207
- Citations
- 110
- Access
- Closed
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Cite This
Till Acker,
Joachim Fandrey,
H. Acker
(2006).
The good, the bad and the ugly in oxygen-sensing: ROS, cytochromes and prolyl-hydroxylases.
Cardiovascular Research
, 71
(2)
, 195-207.
https://doi.org/10.1016/j.cardiores.2006.04.008
Identifiers
- DOI
- 10.1016/j.cardiores.2006.04.008