During phagocytosis, the NADPH oxidase in neutrophils produces superoxide, a precursor of microbicidal oxidants, thereby playing a crucial role in host defense. The phagocyte oxidase contains the two subunits p22phox and gp91phox, the latter of which contains binding sites for the heme, FAD, and NADPH, forming the complete electron-transporting apparatus. Recent studies have revealed that four nonphagocytic homologues of gp91phox exist, including Nox4, whose cDNA we have currently cloned. Here we describe the molecular nature of Nox4, in comparison with those of other members of the NAD(P)H oxidase family.
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