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Review
. 2005 Dec 29;360(1464):2301-8.
doi: 10.1098/rstb.2005.1767.

Dual oxidases

Affiliations
Review

Dual oxidases

Agnes Donkó et al. Philos Trans R Soc Lond B Biol Sci. .

Abstract

Reactive oxygen species (ROS) have an important role in various physiological processes including host defence, mitogenesis, hormone biosynthesis, apoptosis and fertilization. Currently, the most characterized ROS-producing system operates in phagocytic cells, where ROS generated during phagocytosis act in host defence. Recently, several novel homologues of the phagocytic oxidase have been discovered and this protein family is now designated as the NOX/DUOX family of NADPH oxidases. NOX/DUOX enzymes function in a variety of tissues, including colon, kidney, thyroid gland, testis, salivary glands, airways and lymphoid organs. Importantly, members of the enzyme family are also found in non-mammalian species, including Caenorhabditis elegans and sea urchin. The physiological functions of novel NADPH oxidase enzymes are currently largely unknown. This review focuses on our current knowledge about dual oxidases.

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Figures

Figure 1
Figure 1
Membrane topology and domain structure of dual oxidases.
Figure 2
Figure 2
Comparison of amino acid sequences of thyroperoxidase (TPO) and the peroxidase-like domain of human DUOX1. Positions of conserved histidines in the TPO sequence are marked by arrows.
Figure 3
Figure 3
Alternative models for the role of DUOX proteins in protein cross-linking reactions.
Figure 4
Figure 4
Sea urchin dual oxidase (Udx1) produces hydrogen peroxide during sea urchin fertilization.
Figure 5
Figure 5
A model of the expression and assembly of the DUOX–lactoperoxidase system in salivary glands. LPO is synthesized in early stages of saliva formation in serous acini (a), anionic LPO substrates are transported by the sodium iodide symporter in intermediate stages (b), and the system is completed in late stages, where DUOX provides H2O2 within terminal ducts (c).

References

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