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J. Biol. Chem., Vol. 276, Issue 28, 26499-26508, July 13, 2001
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From the Neuroepithelial bodies act as airway oxygen
sensors. The lung carcinoma line H146 is an established model for
neuroepithelial body cells. Although O2 sensing in
both cells is via NADPH oxidase H2O2/free
radical production and acute hypoxia promotes K+ channel
closure and cell depolarization, the identity of the K+
channel is still controversial. However, recent data point toward the
involvement of a member of the tandem P domain family of K+
channels. Reverse transcription-polymerase chain reaction
screening indicates that all known channels other than hTWIK1 and
hTRAAK are expressed in H146 cells. Our detailed pharmacological
characterization of the O2-sensitive K+ current
described herein is compatible with the involvement of hTASK1 or hTASK3
(pH dependence, tetraethylammonium and dithiothreitol insensitivity,
blockade by arachidonic acid, and halothane activation). Furthermore,
we have used antisense oligodeoxynucleotides directed against hTASK1
and hTASK3 to suppress almost completely the hTASK1 protein and show
that these cells no longer respond to acute hypoxia; this behavior was
not mirrored in liposome-only or missense-treated cells.
Finally, we have used Zn2+ treatment as a maneuver
able to discriminate between these two homologues of hTASK and show
that the most likely candidate channel for O2 sensing in
these cells is hTASK3.
Combined Antisense and Pharmacological Approaches
Implicate hTASK as an Airway O2 Sensing K+
Channel*
,,,§,¶
School of Biomedical Sciences, Worsley
Medical and Dental Building and the § Institute for
Cardiovascular Research, University of Leeds,
Leeds LS2 9JT, United Kingdom
*
This work was funded by the British Heart Foundation and the
Wellcome Trust.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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