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Identification of subdomains in NADPH oxidase-4 critical for the oxygen-dependent regulation of TASK-1 K(+) channels
DC Field | Value | Language |
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dc.contributor.author | Park, Su Jung | - |
dc.contributor.author | Chun, Yang-Sook | - |
dc.contributor.author | Park, Kyung Sun | - |
dc.contributor.author | Kim, Sung Joon | - |
dc.contributor.author | Kim, Hye-Lim | - |
dc.contributor.author | Park, Jong-Wan | - |
dc.contributor.author | Choi, Si-On | - |
dc.date.accessioned | 2012-07-02T06:46:04Z | - |
dc.date.available | 2012-07-02T06:46:04Z | - |
dc.date.issued | 2009-10-01 | - |
dc.identifier.citation | AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY; Vol.297 4; C855-C864 | ko_KR |
dc.identifier.issn | 0363-6143 | - |
dc.identifier.uri | https://hdl.handle.net/10371/78103 | - |
dc.description.abstract | Hypoxic inhibition of K+ current is a critical O2-sensing mechanism. Previously, it was demonstrated that the cooperative action of TASK-1 and NADPH oxidase-4 (NOX4) mediated the O2-sensitive K+ current response. Here we addressed the O2-sensing mechanism of NOX4 in terms of TASK-1 regulation. In TASK-1 and NOX4-coexpressing human embryonic kidney 293 cells, hypoxia (5% O2) decreased the amplitude of TASK-1 current (hypoxia-ΔITASK-1). To examine whether reactive oxygen species (ROS) mediate the hypoxia-ΔITASK-1, we treated the cells with carbon monoxide (CO) which is known to reduce ROS generation from the heme-containing NOX4. Unexpectedly, CO failed to mimic hypoxia in TASK-1 regulation, rather blocked the hypoxia-ΔITASK-1. Moreover, the hypoxia-ΔITASK-1 was neither recovered by H2O2 treatment nor prevented by antioxidant such as ascorbic acid. However, the hypoxia-ΔITASK-1 was noticeably attenuated by succinyl acetone, a heme synthase inhibitor. To further evaluate the role of heme, we constructed and expressed various NOX4 mutants, such as HBD(−) lacking the heme binding domain, NBD(−) lacking the NADPH binding domain, FBD(−) lacking the FAD binding domain, and HFBD(−) lacking both heme and FAD domains. The hypoxia-ΔITASK-1 was significantly reduced in HBD(−)-, FBD(−)-, or HFBD(−)-expressing cells, versus wild-type NOX4-expressing cells. However, NBD(−) did not affect the TASK-1 response to hypoxia. We also found that p22 is required for the NOX4-dependent TASK-1 regulation. These results suggest that O2 binding with NOX4 per se controls TASK-1 activity. In this process, the heme moiety and FBD seem to be responsible for the NOX4 regulation of TASK-1, and p22 might support the NOX4-TASK-1 interaction. | ko_KR |
dc.language.iso | en | ko_KR |
dc.publisher | AMER PHYSIOLOGICAL SOC | ko_KR |
dc.subject | hypoxia | ko_KR |
dc.subject | p22 | ko_KR |
dc.subject | background K(+) current | ko_KR |
dc.subject | carbon monoxide | ko_KR |
dc.title | Identification of subdomains in NADPH oxidase-4 critical for the oxygen-dependent regulation of TASK-1 K(+) channels | ko_KR |
dc.type | Article | ko_KR |
dc.contributor.AlternativeAuthor | 박수정 | - |
dc.contributor.AlternativeAuthor | 전양숙 | - |
dc.contributor.AlternativeAuthor | 박경선 | - |
dc.contributor.AlternativeAuthor | 김성준 | - |
dc.contributor.AlternativeAuthor | 최시온 | - |
dc.contributor.AlternativeAuthor | 김혜림 | - |
dc.contributor.AlternativeAuthor | 박종완 | - |
dc.identifier.doi | 10.1152/ajpcell.00463.2008 | - |
dc.citation.journaltitle | AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY | - |
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dc.description.tc | 6 | - |
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