| Title | Enzyme-linked oxygen sensing by potassium channels. | | Author(s) | Kemp PJ, Telezhkin V, Wilkinson WJ, Mears R, Hanmer SB, Gadeberg HC, Müller CT, Riccardi D, Brazier SP | | Institution | School of Biosciences, Cardiff University, Cardiff, United Kingdom. | | Source | Ann N Y Acad Sci 2009 Oct.:112-8. | | Abstract | The ability of ion channels to respond to an acute perturbation in oxygen tension is a widespread phenomenon, which encompasses many of the major ion channel families. Integral to the ability of several ion channels to respond to acute hypoxic challenge is modulation by upstream enzymatic reactions, suggesting that many ion channels sense oxygen via enzyme-linked processes. Several enzyme-linked oxygen sensing systems have been proposed, including nicotinamide adenine dinucleotide phosphate (NADPH) oxidase-dependent production of hydrogen peroxide, hemoxygenase-dependent generation of carbon monoxide, adenosine monophosphate (AMP) kinase-dependent channel phosphorylation, and src-Lck protein tyrosine kinase, via a currently undetermined mechanism. Each of these enzymes has been shown to endow specific ion channels with the ability to respond to changes in oxygen, with hypoxia exclusively evoking channel inhibition. This article reviews these proposed mechanisms and presents new insights into how one system, hemeoxygenase-2, confers oxygen sensitivity to large conductance, voltage- and calcium-activated potassium channels. | | Language | eng | | Pub Type(s) | Journal Article
| | PubMed ID | 19845613 |
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