Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases
- PMID: 11753072
- DOI: 10.1097/00062752-200201000-00003
Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases
Abstract
Reactive oxygen species are classically described as occurring as an accidental byproduct of respiration, and are generally thought to be deleterious to biologic systems. The phagocyte nicotinamide adenine dinucleotide phosphate oxidase provides an example of deliberate reactive oxygen species generation, but the function of this enzyme is to oxidatively modify bacteria as part of bactericidal mechanisms. The discovery of a family of nicotinamide adenine dinucleotide (phosphate) oxidases related to the phagocyte oxidase, the Nox/Duox family, provides additional examples of deliberate generation of reactive oxygen species. This article describes this new family of enzymes and considers hypotheses for their function. Potential roles of Nox/Duox in generation of reactive oxygen species that function in cell signaling (related to growth and angiogenesis), immune function, hypoxic response, and oxidative modification of extracellular matrix proteins are discussed.
Similar articles
-
The NOX Family of Proteins Is Also Present in Bacteria.mBio. 2017 Nov 7;8(6):e01487-17. doi: 10.1128/mBio.01487-17. mBio. 2017. PMID: 29114025 Free PMC article.
-
Regulation of Nox and Duox enzymatic activity and expression.Free Radic Biol Med. 2007 Aug 1;43(3):319-31. doi: 10.1016/j.freeradbiomed.2007.03.028. Epub 2007 Apr 1. Free Radic Biol Med. 2007. PMID: 17602947 Free PMC article. Review.
-
The Dual Role of Reactive Oxygen Species-Generating Nicotinamide Adenine Dinucleotide Phosphate Oxidases in Gastrointestinal Inflammation and Therapeutic Perspectives.Antioxid Redox Signal. 2020 Aug 10;33(5):354-373. doi: 10.1089/ars.2020.8018. Epub 2020 Feb 26. Antioxid Redox Signal. 2020. PMID: 31968991
-
Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox.J Cell Biol. 2001 Aug 20;154(4):879-91. doi: 10.1083/jcb.200103132. J Cell Biol. 2001. PMID: 11514595 Free PMC article.
-
Antimicrobial actions of dual oxidases and lactoperoxidase.J Microbiol. 2018 Jun;56(6):373-386. doi: 10.1007/s12275-018-7545-1. Epub 2018 Jun 1. J Microbiol. 2018. PMID: 29858825 Free PMC article. Review.
Cited by
-
Antioxidant therapeutics: Pandora's box.Free Radic Biol Med. 2014 Jan;66:58-64. doi: 10.1016/j.freeradbiomed.2013.05.047. Epub 2013 Jul 12. Free Radic Biol Med. 2014. PMID: 23856377 Free PMC article. Review.
-
PPARgamma as a potential therapeutic target in pulmonary hypertension.Ther Adv Respir Dis. 2010 Jun;4(3):143-60. doi: 10.1177/1753465809369619. Ther Adv Respir Dis. 2010. PMID: 20530063 Free PMC article. Review.
-
Reactive oxygen species as mediators of angiogenesis signaling: role of NAD(P)H oxidase.Mol Cell Biochem. 2004 Sep;264(1-2):85-97. doi: 10.1023/b:mcbi.0000044378.09409.b5. Mol Cell Biochem. 2004. PMID: 15544038 Review.
-
Chloride Channel 3 Channels in the Activation and Migration of Human Blood Eosinophils in Allergic Asthma.Am J Respir Cell Mol Biol. 2015 Aug;53(2):235-45. doi: 10.1165/rcmb.2014-0300OC. Am J Respir Cell Mol Biol. 2015. PMID: 25514499 Free PMC article.
-
Expression of NADPH oxidase homologues and accessory genes in human cancer cell lines, tumours and adjacent normal tissues.Free Radic Res. 2009 Jun;43(6):523-32. doi: 10.1080/10715760902918683. Free Radic Res. 2009. PMID: 19431059 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases