NADPH oxidase does not account fully for O2-sensing in model airway chemoreceptor cells
NADPH oxidase does not account fully for O2-sensing in model airway chemoreceptor cells
A key feature of O2 sensing by chemoreceptor tissues is the hypoxic inhibition of K+ channels. However, mechanisms coupling a fall of pO2 to channel closure differ between tissues: O2 regulation of K+ channels in chemoreceptive neuroepithelial bodies and their immortal counterparts, H146 cells, involves altered reactive oxygen species generation by NADPH oxidase. In contrast, this enzyme complex is not involved in O2 sensing by the carotid body and pulmonary vasculature. Here, we provide pharmacological evidence to support a role for NADPH oxidase in hypoxic inhibition of K+ currents in H146 cells. Two structurally unrelated NADPH oxidase inhibitors, diphenylene iodonium and phenylarsine oxide, suppressed hypoxic inhibition of K+ currents recorded using the patch-clamp technique. Most importantly, however, neither inhibitor fully blocked this response. Our findings provide the first evidence that multiple mechanisms may coexist within a specific cell type to account for hypoxic suppression of K+ channel activity
reactive oxygen species, kinetics, nadph oxidase, potassium, onium compounds, activity, chemoreceptors, membrane potentials, potassium channels, cell hypoxia, oxygen, humans, research support, inhibition, role, pharmacology, patch-clamp techniques, physiology, cytology, research, drug effects, metabolism, enzyme inhibitors, arsenicals, cell line
1131-1134
O'Kelly, I.
e640f28a-42f0-48a6-9ce2-cb5a85d08c66
Peers, C.
25d5cc41-76e1-43b6-8759-223e06ba1f5f
Kemp, P.J.
954a798c-02bd-40e9-beb6-ad12df9613ed
25 May 2001
O'Kelly, I.
e640f28a-42f0-48a6-9ce2-cb5a85d08c66
Peers, C.
25d5cc41-76e1-43b6-8759-223e06ba1f5f
Kemp, P.J.
954a798c-02bd-40e9-beb6-ad12df9613ed
O'Kelly, I., Peers, C. and Kemp, P.J.
(2001)
NADPH oxidase does not account fully for O2-sensing in model airway chemoreceptor cells.
Biochemical and Biophysical Research Communications, 283 (5), .
(doi:10.1006/bbrc.2001.4919).
Abstract
A key feature of O2 sensing by chemoreceptor tissues is the hypoxic inhibition of K+ channels. However, mechanisms coupling a fall of pO2 to channel closure differ between tissues: O2 regulation of K+ channels in chemoreceptive neuroepithelial bodies and their immortal counterparts, H146 cells, involves altered reactive oxygen species generation by NADPH oxidase. In contrast, this enzyme complex is not involved in O2 sensing by the carotid body and pulmonary vasculature. Here, we provide pharmacological evidence to support a role for NADPH oxidase in hypoxic inhibition of K+ currents in H146 cells. Two structurally unrelated NADPH oxidase inhibitors, diphenylene iodonium and phenylarsine oxide, suppressed hypoxic inhibition of K+ currents recorded using the patch-clamp technique. Most importantly, however, neither inhibitor fully blocked this response. Our findings provide the first evidence that multiple mechanisms may coexist within a specific cell type to account for hypoxic suppression of K+ channel activity
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Published date: 25 May 2001
Keywords:
reactive oxygen species, kinetics, nadph oxidase, potassium, onium compounds, activity, chemoreceptors, membrane potentials, potassium channels, cell hypoxia, oxygen, humans, research support, inhibition, role, pharmacology, patch-clamp techniques, physiology, cytology, research, drug effects, metabolism, enzyme inhibitors, arsenicals, cell line
Identifiers
Local EPrints ID: 60097
URI: http://eprints.soton.ac.uk/id/eprint/60097
ISSN: 0006-291X
PURE UUID: 39cbafe5-1d9f-4214-a587-6ea29c9146b5
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Date deposited: 05 Sep 2008
Last modified: 15 Mar 2024 11:19
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Author:
I. O'Kelly
Author:
C. Peers
Author:
P.J. Kemp
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