Dual oxidases

Philos Trans R Soc Lond B Biol Sci. 2005 Dec 29;360(1464):2301-8. doi: 10.1098/rstb.2005.1767.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Autoantigens / genetics
  • Autoantigens / metabolism*
  • Dual Oxidases
  • Extracellular Matrix / enzymology
  • Flavoproteins / genetics
  • Flavoproteins / metabolism*
  • Humans
  • Iodide Peroxidase / genetics
  • Iodide Peroxidase / metabolism*
  • Iron-Binding Proteins / genetics
  • Iron-Binding Proteins / metabolism*
  • Models, Molecular*
  • Molecular Sequence Data
  • Mucous Membrane / enzymology
  • NADPH Oxidases / genetics
  • NADPH Oxidases / metabolism*
  • Phagocytosis / physiology*
  • Reactive Oxygen Species / metabolism*
  • Salivary Glands / enzymology
  • Thyroid Gland / enzymology


  • Autoantigens
  • Flavoproteins
  • Iron-Binding Proteins
  • Reactive Oxygen Species
  • Dual Oxidases
  • TPO protein, human
  • Iodide Peroxidase
  • NADPH Oxidases
  • DUOX1 protein, human
  • DUOX2 protein, human