Year: 2006
Type: article
Abstract: For many years, reactive oxygen species (ROS), including superoxide, hydrogen peroxide, and hydroxyl radicals, and their reaction products, were classically described as harmful by-products of aerobic metabolism capable of causing DNA mutations, lipid peroxidation, and protein oxidation [1]. The identification of enzymes such as superoxide dismutase, catalase, and peroxidase that served to eliminate these waste products rather substantiated this view. It soon became clear, however, that there existed a family of enzymes whose function it was to deliberately generate ROS. The first of these was NADPH oxidase, which is responsible for the respiratory burst in neutrophils and macrophages in response to microbes or inflammatory cytokines [2]. The catalytic centre of NADPH oxidase is the membrane-associated protein gp91 phox (see Glossary) complexed with p22 phox. Activation requires association with a phosphorylated form of p47 phox (also known as Ncf1), p67 phox, and the small GTPase Rac (Figure 1). p47 phox deficiency in humans leads to neutrophil dysfunction and chronic granulomatous disease (CGD), a primary immunodeficiency disorder characterised by the inability to eradicate bacterial infections [3]. Since the late 1990s, six human gp91phox homologues have been identified, each with distinct functions [1]. Besides a role in phagocyte function and host defence, a large amount of evidence points to important roles for ROS in cell proliferation, apoptosis, angiogenesis, endocrinerelated functions, and oxidative modification of the extracellular The Perspectives section is for experts to discuss the clinical practice or public health implications of a published article that is freely available online.
Source: PLoS Medicine
Author: Andrew P Cope
Institution: Imperial College London
Language: English
Subfield: Immunology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $6,460
OpenAlex ID: W2024868941