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Proton accumulation and efflux associated specifically with
NADPH oxidation in neutrophils remains to be elucidated. Using confocal
fluorescence and patch-clamp recordings from single human neutrophils,
in the presence of protein kinase C inhibitors, we studied the
transient cytosolic acidification and whole-cell H
current induced by
N-formyl-methionyl-leucyl-phenylalanine (fMLP) and
recombinant human tumor necrosis factor
(rhTNF).
Intracellular pH changes were monitored utilizing the ratiometric
imaging of the dual emission fluoroprobe,
carboxyseminaphthorhodafluor-1, AM acetate. Bath application of 1000
units/ml rhTNF or 0.1 µM fMLP changed the
fluorescence of fluoroprobe-loaded cells, indicating generation of
cytosolic H ions. In the absence of Ca
in the pipette solution, exposure of cells to rhTNF
or fMLP
for 10 s activated voltage-dependent H currents. From
tail current analysis, the threshold voltage for H
current activation was
-50 mV. These fMLP- or
rhTNF-activated voltage-dependent H currents were
augmented further in the presence of 0.1 mM of NADPH in the
pipette solution, and they were inhibited by bath application of 50
µM of apocynin, an NADPH oxidase inhibitor. These results
indicate that rhTNF
- or fMLP-induced NADPH oxidase in human
neutrophils gives rise to the activation of voltage-dependent
H currents.
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