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Please use this identifier to cite or link to this item: http://hdl.handle.net/10373/219

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Title: A Ba2+-resistant, acid-sensitive K+ conductance in Na+-absorbing H441 human airway epithelial cells
Authors: Inglis, Sarah K.
Brown, Sean G.
Constable, Maree J.
McTavish, Niall
Olver, Richard E.
Wilson, Stuart M.
Affiliation: University of Abertay Dundee. School of Social and Health Sciences
Keywords: Airway sodium channel transport
Patch clamping
Ussing chamber
Issue Date: 2-Feb-2007
Publisher: American Physiological Society
Type: Journal Article
Refereed: peer-reviewed
Rights: Published version (c)American Physiological Society, available from DOI: 10.1152/ajplung.00424.2006
Citation: Inglis, S. K., et al. 2007. A Ba2+-resistant, acid-sensitive K+ conductance in Na+-absorbing H441 human airway epithelial cells. American Journal of Physiology: Lung Cellular and Molecular Physiology. 292 : pp.1304-1312. [Online] Available from: DOI: 10.1152/ajplung.00424.2006
Abstract: By analysis of whole cell membrane currents in Na+-absorbing H441 human airway epithelial cells, we have identified a K+ conductance (GK) resistant to Ba2+ but sensitive to bupivacaine or extracellular acidification. In polarized H441 monolayers, we have demonstrated that bupivacaine, lidocaine, and quinidine inhibit basolateral membrane K+ current (IBl) whereas Ba2+ has only a weak inhibitory effect. IBl was also inhibited by basolateral acidification, and, although subsequent addition of bupivacaine caused a further fall in IBl, acidification had no effect after bupivacaine, demonstrating that cells grown under these conditions express at least two different bupivacaine-sensitive K+ channels, only one of which is acid sensitive. Basolateral acidification also inhibited short-circuit current (ISC), and basolateral bupivacaine, lidocaine, quinidine, and Ba2+ inhibited ISC at concentrations similar to those needed to inhibit IBl, suggesting that the K+ channels underlying IBl are part of the absorptive mechanism. Analyses using RT-PCR showed that mRNA encoding several two-pore domain K+ (K2P) channels was detected in cells grown under standard conditions (TWIK-1, TREK-1, TASK-2, TWIK-2, KCNK-7, TASK-3, TREK-2, THIK-1, and TALK-2). We therefore suggest that K2P channels underlie GK in unstimulated cells and so maintain the driving force for Na+ absorption. Since this ion transport process is vital to lung function, K2P channels thus play an important but previously undocumented role in pulmonary physiology.
URI: http://hdl.handle.net/10373/219
ISSN: 1040-0605
Appears in Collections:Social & Health Sciences Collection

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