NADPH oxidase subunit gp91phox:: a proton pathway
NADPH oxidase subunit gp91phox:: a proton pathway
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DOI:
10.1007/bf01289411
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发表时间:
2001-01-01
期刊:
影响因子:
2.9
通讯作者:
Henderson, LM
中科院分区:
文献类型:
--
作者:
Henderson, LM
The generation of superoxide by the NADPH oxidase is an electrogenic process resulting in a rapid depolarisation of the membrane potential of the cell. The efflux of H+ ions through an arachidonate-activatable, Zn2+-inhibitable HC pathway accompanies the efflux of electrons and provides the necessary charge compensation. Inhibition of H+ flux leads to inhibition of superoxide generation. The protein gp91(phox), a transmembrane component of the NADPH oxidase, was demonstrated to be capable of acting as the NADPH oxidase-associated H+ channel in a stable CHO cell line, CHO91. The N-terminal 230 amino acids contain all that is required for the protein to form an Ht channel and specifically histidine 115 is important to the ability of gp91(phox) to conduct H+ ions. The recording of outward currents from CHO91 cells, in the whole-cell configuration, demonstrated that gp91(phox) is also capable of functioning as a voltage-gated He conductance pathway. The similarity in properties between voltage-elicited outward currents, from both wild type and the mutations, and the arachidonate-activated Hi flux strongly suggests that these H+ pathways are one in the same. Among the recently identified homologues of gp91(phox) only NOH-1S has so far been demonstrated to also act as an Ht conductance pathway.