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NOX4 as an oxygen sensor to regulate TASK-1 activity
Cited 88 time in
Web of Science
Cited 94 time in Scopus
- Authors
- Issue Date
- 2006-07-16
- Publisher
- Elsevier
- Citation
- Cell Signal. 2006 Apr;18(4):499-507. Epub 2005 Jul 14.
- Keywords
- Anoxia/metabolism ; Biosensing Techniques/*methods ; Cell Line ; Cell Membrane/metabolism ; Enzyme Inhibitors/pharmacology ; Humans ; Hypoxia-Inducible Factor 1, alpha Subunit/drug effects/metabolism ; NADPH Oxidase/antagonists & inhibitors/genetics/*physiology ; Nerve Tissue Proteins ; Onium Compounds/pharmacology ; Oxygen/analysis/*metabolism ; Potassium/metabolism/physiology ; Potassium Channels, Tandem Pore Domain/antagonists & ; inhibitors/*metabolism ; RNA, Small Interfering/genetics/pharmacology/physiology ; Signal Transduction/drug effects/physiology
- Abstract
- When oxygen sensing cells are excited by hypoxia, background K+ currents are inhibited. TASK-1, which is commonly expressed in oxygen sensing cells and makes a background K+ current, is inactivated by hypoxia. Thus TASK-1 is a candidate molecule responsible for hypoxic excitation. However, TASK-1 per se cannot sense oxygen and may require a regulatory protein that can. In the present study, we propose that the NADPH oxidase NOX4 functions as an oxygen-sensing partner and that it modulates the oxygen sensitivity of TASK-1. Confocal imaging revealed the co-localization of TASK-1 and NOX4 in the plasma membrane. In HEK293 cells expressing NOX4 endogenously, the activity of expressed TASK-1 was moderately inhibited by hypoxia, and this oxygen response was significantly augmented by NOX4. Moreover, the oxygen sensitivity of TASK-1 was abolished by NOX4 siRNA and NADPH oxidase inhibitors. These results suggest a novel function for NOX4 in the oxygen-dependent regulation of TASK-1 activity.
- ISSN
- 0898-6568 (Print)
- Language
- English
- URI
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16019190
https://hdl.handle.net/10371/23437
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