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Enzyme-linked oxygen sensing by potassium channels

Kemp, Paul J. ORCID:, Telezhkin, Vsevolod ORCID:, Wilkinson, William James, Mears, Ruth, Hanmer, Stuart, Gadeberg, Hanne C., Müller, Carsten T., Riccardi, Daniela ORCID: and Brazier, Stephen Paul 2009. Enzyme-linked oxygen sensing by potassium channels. Annals of the New York Academy of Sciences 1177 , pp. 112-118. 10.1111/j.1749-6632.2009.05025.x

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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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Subjects: Q Science > Q Science (General)
Q Science > QH Natural history > QH301 Biology
Q Science > QP Physiology
Uncontrolled Keywords: hypoxia; ion channel; potassium channel; carotid body; neuroepithelial body; hemeoxygenase; AMP kinase; NADPH oxidase; src protein tyrosine kinase
Publisher: Wiley-Blackwell
ISSN: 0077-8923
Last Modified: 06 Dec 2022 09:35

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