Structural organization of the neutrophil NADPH oxidase: phosphorylation and translocation during priming and activation

被引:277
作者
Sheppard, FR
Kelher, MR
Moore, EE
McLaughlin, NJD
Banerjee, A
Silliman, CC
机构
[1] Bonfils Blood Ctr, Denver, CO 80230 USA
[2] Denver Hlth Med Ctr, Dept Surg, Colorado Springs, CO USA
[3] Univ Colorado, Sch Med, Dept Surg, Denver, CO USA
[4] Univ Colorado, Sch Med, Dept Pediat, Denver, CO USA
关键词
review; innate immunity; respiratory burst; oxidase assembly;
D O I
10.1189/jlb.0804442
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidase is part of the microbicidal arsenal used by human polymor-phonuclear nentrophils (PMNs) to eradicate invading pathogens. The production of a superoxide anion (O-2(-)) into the phagolysosome is the precursor for the generation of more potent products, such as hydrogen peroxide and hypochlorite. However, this production of O-2(-) is dependent on translocation of the oxidase subunits, including gp91(phox), p22(phox), p47(phox), p67(phox), p40(phox), and Rac2 from the cytosol or specific granules to the plasma membrane. In response to an external stimuli, PMNs change from a resting, nonadhesive state to a primed, adherent phenotype, which allows for margination from the vasculature into the tissue and chemotaxis to the site of infection upon activation. Depending on the stimuli, primed PMNs display altered structural organization of the NADPH oxidase, in that there is phosphorylation of the oxidase subunits and/or translocation from the cytosol to the plasma or granular membrane, but there is not the complete assembly required for O-2(-) generation. Activation of PMNs is the complete assembly of the membrane-linked and cytosolic NADPH oxidase components on a PMN membrane, the plasma or granular membrane. This review will discuss the individual components associated with the NADPH oxidase complex and the function of each of these units in each physiologic stage of the PMN: rested, primed, and activated.
引用
收藏
页码:1025 / 1042
页数:18
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