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Nox enzymes in immune cells

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Abstract

The nicotinamide adenine dinucleotide phosphate (NADPH) oxidase of phagocytes is a multi-component electron transferase that uses cytoplasmic NADPH to convert molecular oxygen to superoxide anion, consequently delivering reactive oxygen species to the site of invading microorganisms. Together with soluble factors and other phagocyte-derived agents, the resultant toxic species kill and degrade the ingested microbe. Flavocytochrome b 558, a heterodimeric protein composed of gp91phox and p22phox, is the membrane component of the NADPH oxidase and was previously thought to be uniquely expressed in phagocytes. Based on structural homology with gp91phox, recent studies have defined a family of NADPH oxidase proteins (Nox) that is widely distributed throughout the plant and animal kingdoms and in many tissues in multicellular organisms. The goals of this review are to review features of the phagocyte NADPH oxidase that serve as a paradigm for exploiting oxidants for host defense, and to discuss contributions of other Nox proteins to innate immunity.

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Acknowledgements

Work in the Nauseef laboratory is supported by grants from the National Institutes of Health (AI 34879, HL 53592, AI 44642) and the Veterans Administration (Merit Review).

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  1. Inflammation Program and Department of Medicine, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, D160 MTF, 2501 Crosspark Road, Coralville, IA, 52241, USA

    William M. Nauseef

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Nauseef, W.M. Nox enzymes in immune cells. Semin Immunopathol 30, 195–208 (2008). https://doi.org/10.1007/s00281-008-0117-4

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