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PMID: 17602947 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Review

Regulation of Nox and Duox enzymatic activity and expression.

Free radical biology & medicine ·Vol. 43 ·No. 3 ·2007-08-01 ·Pages 319-31

Lambeth JD, Kawahara T, Diebold B

Abstract

In recent years, it has become clear that reactive oxygen species (ROS, which include superoxide, hydrogen peroxide, and other metabolites) are produced in biological systems. Rather than being simply a by-product of aerobic metabolism, it is now recognized that specific enzymes--the Nox (NADPH oxidase) and Duox (Dual oxidase) enzymes--seem to have the sole function of generating ROS in a carefully regulated manner, and key roles in signal transduction, immune function, hormone biosynthesis, and other normal biological functions are being uncovered. The prototypical Nox is the respiratory burst oxidase or phagocyte oxidase, which generates large amounts of superoxide and other reactive species in the phagosomes of neutrophils and macrophages, playing a central role in innate immunity by killing microbes. This enzyme system has been extensively studied over the past two decades, and provides a basis for comparison with the more recently described Nox and Duox enzymes, which generate ROS in a variety of cells and tissues. This review first considers the structure and regulation of the respiratory burst oxidase, and then reviews recent studies relating to the regulation of the activity of the novel Nox/Duox enzymes. The regulation of Nox and Duox expression in tissues and by specific stimuli is also considered here. An accompanying review considers biological and pathological roles of the Nox family of enzymes.

MeSH Terms
Animals Dual Oxidases Flavoproteins/genetics,metabolism Gene Expression Regulation, Enzymologic/physiology Humans Membrane Glycoproteins/metabolism Membrane Proteins/metabolism NADPH Oxidase 1 NADPH Oxidase 2 NADPH Oxidase 4 NADPH Oxidase 5 NADPH Oxidases/genetics,metabolism Phagocytes/physiology Phosphoproteins/metabolism Promoter Regions, Genetic/physiology Protein Structure, Tertiary Protein Subunits/metabolism
Chemicals
Flavoproteins Membrane Glycoproteins Membrane Proteins Phosphoproteins Protein Subunits neutrophil cytosol factor 67K Dual Oxidases CYBB protein, human NADPH Oxidase 1 NADPH Oxidase 2 NADPH Oxidase 4 NADPH Oxidase 5 NADPH Oxidases NOX1 protein, human NOX5 protein, human Nox4 protein, mouse DUOX1 protein, human neutrophil cytosolic factor 1 superoxide-forming enzyme
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Lambeth J David
Department of Pathology and Laboratory Medicine, 148 Whitehead Biomedical Research Building, Emory University, 615 Michael Street, Atlanta, GA 30322, USA. [email protected]
Kawahara Tsukasa
Diebold Becky
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Article Info
Journal
Free radical biology & medicine
Abbr.
Free Radic Biol Med
ISSN
0891-5849
DOI
10.1016/j.freeradbiomed.2007.03.028
Email
[email protected]
Published
2007-08-01
Epub
2007-00-01
Pages
319-31
Language
English
Region
United States
NLM ID
8709159
PMCID
PMC1989153
Subset
IM
Grants
NCI NIH HHS · R01 CA105116 · United States
NIGMS NIH HHS · R01 GM067717 · United States
NCI NIH HHS · R01 CA105116-04 · United States
NCI NIH HHS · CA084138 · United States
NCI NIH HHS · R01 CA084138-05S1 · United States
NCI NIH HHS · CA105116 · United States
NCI NIH HHS · R56 CA105116 · United States
NIGMS NIH HHS · R01 GM067717-04 · United States
NCI NIH HHS · R01 CA084138 · United States
External Links
PubMed source DOI: 10.1016/j.freeradbiomed.2007.03.028 PMC Full Text View journal details
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