Targeting and Regulation of Reactive Oxygen Species Generation by Nox Family NADPH Oxidases
Publication: Antioxidants & Redox Signaling
Volume 11, Issue Number 10
Abstract
Nox family NADPH oxidases serve a variety of functions requiring reactive oxygen species (ROS) generation, including antimicrobial defense, biosynthetic processes, oxygen sensing, and redox-based cellular signaling. We explored targeting, assembly, and activation of several Nox family oxidases, since ROS production appears to be regulated both spatially and temporally. Nox1 and Nox3 are similar to the phagocytic (Nox2-based) oxidase, functioning as multicomponent superoxide-generating enzymes. Factors regulating their activities include cytosolic activator and organizer proteins and GTP-Rac. Their regulation varies, with the following rank order: Nox2 > Nox1 > Nox3. Determinants of subcellular targeting include: (a) formation of Nox-p22phox heterodimeric complexes allowing plasma membrane translocation, (b) phospholipids-binding specificities of PX domain-containing organizer proteins (p47phox or Nox organizer 1 (Noxo1 and p40phox), and (c) variably splicing of Noxo1 PX domains directing them to nuclear or plasma membranes. Dual oxidases (Duox1 and Duox2) are targeted by different mechanisms. Plasma membrane targeting results in H2O2 release, not superoxide, to support extracellular peroxidases. Human Duox1 and Duox2 have no demonstrable peroxidase activity, despite their extensive homology with heme peroxidases. The dual oxidases were reconstituted by Duox activator 2 (Duoxa2) or two Duoxa1 variants, which dictate maturation, subcellular localization, and the type of ROS generated by forming stable complexes with Duox. Antioxid Redox Signal. 11, 000–000.
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Published In
Antioxidants & Redox Signaling
Volume 11 • Issue Number 10 • October 2009
Pages: 2607 - 2619
PubMed: 19438290
Copyright
Copyright 2009, Mary Ann Liebert, Inc.
History
Published in print: October 2009
Published online: 18 September 2009
Published ahead of print: 5 August 2009
Published ahead of production: 13 May 2009
Accepted: 13 May 2009
Received: 21 April 2009
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