Abstract
Deliberate production of reactive oxygen species (ROS) are catalyzed by enzymes that belong to the NAD(P)H oxidase (Nox) family. The human genome contains seven members of the Nox family: the superoxide-producing enzymes Nox1 through Nox5 and the dual oxidases Duox1 and Duox2 that release hydrogen peroxide but not superoxide. Among them, the classical member gp91 phox /Nox2 functions as the phagocyte NADPH oxidase, playing a crucial role in host defense. Although Nox2, heterodimerized with its membrane-spanning partner p22 phox , is inactive in resting cells, during phagocytosis it forms an active complex with soluble regulatory proteins such as the organizer p47 phox , the activator p67 phox , and the small GTPase Rac. Here the authors describe how the novel superoxide-producing Nox oxidases (Nox1, 3, 4, and 5) with different functions are regulated by p22 phox , the Nox organizers, the Nox activators, and Rac, and how their expression is controlled at the transcriptional level.
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