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NADPH oxidase activation in neutrophils: Role of the phosphorylation of its subunits
Author(s) -
Belambri Sahra A.,
Rolas Loïc,
Raad Houssam,
HurtadoNedelec Margarita,
Dang Pham MyChan,
ElBenna Jamel
Publication year - 2018
Publication title -
european journal of clinical investigation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.164
H-Index - 107
eISSN - 1365-2362
pISSN - 0014-2972
DOI - 10.1111/eci.12951
Subject(s) - p22phox , nadph oxidase , superoxide , microbiology and biotechnology , phosphorylation , reactive oxygen species , chemistry , oxidase test , biochemistry , cytosol , enzyme , biology
Neutrophils are key cells of innate immunity and during inflammation. Upon activation, they produce large amounts of superoxide anion (O 2 −. ) and ensuing reactive oxygen species ( ROS ) to kill phagocytized microbes. The enzyme responsible for O 2 −. production is called the phagocyte NADPH oxidase. This is a multicomponent enzyme system that becomes active after assembly of four cytosolic proteins (p47 phox , p67 phox , p40 phox and Rac2) with the transmembrane proteins (p22 phox and gp91 phox , which form the cytochrome b 558 ). gp91 phox represents the catalytic subunit of the NADPH oxidase and is also called NOX 2. NADPH oxidase‐derived ROS are essential for microbial killing and innate immunity; however, excessive ROS production induces tissue injury and prolonged inflammatory reactions that contribute to inflammatory diseases. Thus, NADPH oxidase activation must be tightly regulated in time and space to limit ROS production. NADPH oxidase activation is regulated by several processes such as phosphorylation of its components, exchange of GDP / GTP on Rac2 and binding of p47 phox and p40 phox to phospholipids. This review aims to provide new insights into the role of the phosphorylation of the NADPH oxidase components, that is gp91 phox , p22 phox , p47 phox , p67 phox and p40 phox , in the activation of this enzyme.