NOX5: from basic biology to signaling and disease

Free Radic Biol Med. 2012 Feb 15;52(4):725-34. doi: 10.1016/j.freeradbiomed.2011.11.023. Epub 2011 Dec 14.

Abstract

In mammals, the NADPH oxidase family of enzymes comprises seven members: NOXs 1-5, DUOX1, and DUOX2. All of these enzymes function to move an electron across cellular membranes, transferring it to oxygen to generate the superoxide anion. This generation of reactive oxygen species has important physiological and pathophysiological roles. NOX5 is perhaps the least well understood of these NOX isoforms, in part because the gene is not present in mice or rats. In recent years, however, there has been a rapid increase in our understanding of the NOX5 gene, the structural and biochemical aspects of the NOX5 enzyme, the role NOX5 plays in health and disease, and the development of novel NOX inhibitors. This review takes a look back at some historical aspects of the discovery of NOX5 and summarizes our current understanding of the enzyme.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Evolution, Molecular
  • Humans
  • Isoenzymes / antagonists & inhibitors
  • Isoenzymes / chemistry
  • Isoenzymes / genetics
  • Isoenzymes / physiology
  • Membrane Proteins / antagonists & inhibitors
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / physiology*
  • Molecular Sequence Data
  • NADPH Oxidase 5
  • NADPH Oxidases / antagonists & inhibitors
  • NADPH Oxidases / chemistry
  • NADPH Oxidases / genetics
  • NADPH Oxidases / physiology*
  • Organ Specificity
  • Polymorphism, Single Nucleotide
  • Protein Structure, Tertiary
  • Superoxides / metabolism

Substances

  • Isoenzymes
  • Membrane Proteins
  • Superoxides
  • NADPH Oxidase 5
  • NADPH Oxidases
  • NOX5 protein, human