S-Space College of Medicine/School of Medicine (의과대학/대학원) Dept. of Physiology (생리학교실) Journal Papers (저널논문_생리학교실)
NOX4 as an oxygen sensor to regulate TASK-1 activity
- Lee, Young-Mee; Kim, Byung-Joo; Chun, Yang-Sook; So, Insuk; Choi, Hyunsung; Kim, Myung-Suk; Park, Jong-Wan
- Issue Date
- Cell Signal. 2006 Apr;18(4):499-507. Epub 2005 Jul 14.
- 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
- 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.
- 0898-6568 (Print)
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