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.
journal_name
Cell Signaljournal_title
Cellular signallingauthors
Lee YM,Kim BJ,Chun YS,So I,Choi H,Kim MS,Park JWdoi
10.1016/j.cellsig.2005.05.025subject
Has Abstractpub_date
2006-04-01 00:00:00pages
499-507issue
4eissn
0898-6568issn
1873-3913pii
S0898-6568(05)00130-0journal_volume
18pub_type
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