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The superoxide-generating oxidase of phagocytic cells

Physiological, molecular and pathological aspects
  • Françoise Morel
  • Jacques Doussiere
  • Pierre V. Vignais
Part of the EJB Reviews 1991 book series (EJB REVIEWS, volume 1991)

Abstract

Professional phagocytes (neutrophils, eosinophils, monocytes and macrophages) possess an enzymatic complex, the NADPH oxidase, which is able to catalyze the one-electron reduction of molecular oxygen to superoxide, O 2 - . The NADPH oxidase is dormant in non-activated phagocytes. It is suddenly activated upon exposure of phagocytes to the appropriate stimuli and thereby contributes to the microbicidal activity of these cells. Oxidase activation in phagocytes involves the assembly, in the plasma membrane, of membrane-bound and cytosolic components of the oxidase complex, which were disassembled in the resting state. One of the membrane-bound components in resting phagocytes has been identified as a low-potential b-type cytochrome, a heterodimer composed of two subunits of 22-kDa and 91-kDa. The link between NADPH and cytochrome b is probably a flavoprotein whose subcellular localization in resting phagocytes remains to be determined. Genetic defects in the cytochrome b subunits and in the cytosolic factors have been shown to be the molecular basis of chronic granulomatous disease, a group of inherited disorders in the host defense, characterized by severe, recurrent bacterial and fungal infections in which phagocytic cells fail to generate O 2 - upon stimulation. The present review is focused on recent data concerning the signaling pathway which leads to oxidase activation, including specific receptors, the production of second messengers, the organization of the oxidase complex and the molecular defects responsible for granulomatous disease.

Keywords

Oxidase Activation HL60 Cell Respiratory Burst Chronic Granulomatous Disease Cytochrome B558 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Abbreviations

CGD

chronic granulomatous disease

GAP

GTPase activating protein

GDP[S]

guanosine 5′-[γ-thio]-diphosphate

GTP[S]

guanosine 5′-[γ-thio]tripriosphate

fMet

formylmethionyl

IL

interleukin

INF

interferon

InsP3

inositol 1,4,5 triphosphate

nitroblue tetrazolium

2,2′-bis(p-nitrophenyl)-5,5′-diphenyl-3,3′-dimethoxy-4,4′-diphenylene)-ditetrazolium chloride

NAP

neutrophil-activating protein (in early papers NAP was designed under the terms of MDNCF: monocyte-derived neutrophil chemotactic factor; or MONAP: monocyte-derived NAP; or NAF: neutrophil activating factor)

PAF

platelet aggregating factor

PKC

protein kinase C

PtdInsP2

phosphatidylinositol 4,5-bisphosphate

SOC

soluble oxidase component

SOD

superoxide dismutase

TNF

tumor necrosis factor

G

guanosine-nucleotide-binding protein

Gi

inhibitory subunit of guanosine-nucleotide-binding protein

Go

other subunit of guanosine-nucleotide-binding protein.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1991

Authors and Affiliations

  • Françoise Morel
    • 1
  • Jacques Doussiere
    • 1
  • Pierre V. Vignais
    • 1
  1. 1.Laboratoire de Biochimie, Département de Biologie Moléculaire et StructuraleCentre d’Etudes NucléairesGrenobleFrance

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