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- W1557776164 endingPage "468" @default.
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- W1557776164 abstract "The membrane-integrated protein gp91phox functions as the catalytic center of the superoxide-producing phagocyte NADPH oxidase. Recent studies have identified homologs of gp91phox in nonphagocytic cells, which constitute the NADPH oxidase (Nox) family. Activation of the Nox oxidases leads to production of reactive oxygen species (ROS), thereby participating in a variety of biological events, such as host defense, hormone biosynthesis, and signal transduction. The activity of the Nox enzymes is regulated by various proteins, including the small GTPase Rac; regulatory mechanisms differ dependent on the type of the Nox proteins. For example, an oxidase activator (p47phox or Noxo1) and an oxidase activator (p67phox or Noxa1) are absolutely required for superoxide production by gp91phox and Nox1, but not by Nox3. Rac, albeit probably dispensable to the Nox3 activity, plays an essential role in activation of gp91phox. Thus, functional reconstitution of Nox systems is crucial for the study of Nox regulation. Here we describe a basic method for the reconstitution of Nox systems by expression of oxidase proteins in transfectable cells." @default.
- W1557776164 created "2016-06-24" @default.
- W1557776164 creator A5029199121 @default.
- W1557776164 creator A5030256357 @default.
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- W1557776164 date "2006-01-01" @default.
- W1557776164 modified "2023-10-14" @default.
- W1557776164 title "Regulation of Superoxide‐Producing NADPH Oxidases in Nonphagocytic Cells" @default.
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- W1557776164 doi "https://doi.org/10.1016/s0076-6879(06)06034-4" @default.
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