Cellular and Molecular Life Sciences CMLS

, Volume 62, Issue 19–20, pp 2173–2193 | Cite as

Regulation and termination of NADPH oxidase activity

  • T. E. DeCourseyEmail author
  • E. Ligeti


NADPH oxidase of phagocytes plays a crucial role in host defense by producing reactive oxygen species (ROS) that are intended to kill invading microbes. Many other cells produce ROS for signaling purposes. The respiratory burst oxidase in human neutrophils is the main but not exclusive subject of this review, because it is archetypical and has been studied most extensively. The activity of this enzyme must be controlled in phagocytes to prevent collateral damage, and in non-phagocytic cells to perform its signaling role. With many stimuli, NADPH oxidase activity is transient. Various forms of evidence indicate that sustained NADPH oxidase activity requires continuous renewal of the enzyme complex, without which rapid deactivation occurs. This review considers mechanisms that have been proposed to terminate the phagocyte respiratory burst. Changes in the phosphorylation state of p47 phox and in the species of nucleotide bound to Rac seem to be the dominant factors in deactivation.

Key words.

Respiratory burst phagocytes reactive oxygen species leukocytes neutrophil Rac G proteins phosphatase 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Copyright information

© Birkhäuser Verlag, Basel 2005

Authors and Affiliations

  1. 1.Department of Molecular Biophysics and PhysiologyRush University Medical CenterChicagoUSA
  2. 2.Department of PhysiologySemmelweis UniversityBudapest 8Hungary

Personalised recommendations