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• W2097510880 abstract "Hypoxic inhibition of K + current is a critical O 2 -sensing mechanism. Previously, it was demonstrated that the cooperative action of TASK-1 and NADPH oxidase-4 (NOX4) mediated the O 2 -sensitive K + current response. Here we addressed the O 2 -sensing mechanism of NOX4 in terms of TASK-1 regulation. In TASK-1 and NOX4-coexpressing human embryonic kidney 293 cells, hypoxia (5% O 2 ) decreased the amplitude of TASK-1 current (hypoxia-Δ I TASK-1 ). To examine whether reactive oxygen species (ROS) mediate the hypoxia-Δ I TASK-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-Δ I TASK-1 . Moreover, the hypoxia-Δ I TASK-1 was neither recovered by H 2 O 2 treatment nor prevented by antioxidant such as ascorbic acid. However, the hypoxia-Δ I TASK-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-Δ I TASK-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 O 2 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." @default.
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• W2097510880 date "2009-10-01" @default.
• W2097510880 modified "2023-09-23" @default.
• W2097510880 title "Identification of subdomains in NADPH oxidase-4 critical for the oxygen-dependent regulation of TASK-1 K⁺ channels" @default.
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• W2097510880 doi "https://doi.org/10.1152/ajpcell.00463.2008" @default.
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