The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel

The membrane potential of cytoplasts, derived from human neutrophils, was depolarized by the activation of the superoxide-generating NADPH-dependent oxidase. The extent of the depolarization was inhibited by diphenylene iodonium and was therefore due directly to the activity of the oxidase, which mu...

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Bibliographic Details
Published in:Biochemical journal 1987-09, Vol.246 (2), p.325-329
Main Authors: Henderson, L M, Chappell, J B, Jones, O T
Format: Article
Language:English
Subjects:
Biological Transport - drug effects
Humans
Hydrogen-Ion Concentration
In Vitro Techniques
Membrane Potentials
NADH, NADPH Oxidoreductases - blood
NADPH Oxidases
Neutrophils - metabolism
Onium Compounds - pharmacology
Protons
Superoxides - metabolism
Tetradecanoylphorbol Acetate - pharmacology
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Summary:The membrane potential of cytoplasts, derived from human neutrophils, was depolarized by the activation of the superoxide-generating NADPH-dependent oxidase. The extent of the depolarization was inhibited by diphenylene iodonium and was therefore due directly to the activity of the oxidase, which must be electrogenic. The extent of the depolarization was influenced by alteration of the delta pH across the cytoplast membrane, indicating that the outward translocation of H+ eventually compensates for superoxide generation. The depolarization of the potential is enhanced by Cd2+, a blocker of H+ currents, suggesting that the compensatory movement is via an H+ channel.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2460325