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(Received for publication, July 17, 1996, and in revised form, February 18, 1997)
From the The elicitation of an oxidative burst
in phagocytes rests on the assembly of a multicomponental complex
(NADPH oxidase) consisting of a membrane-associated flavocytochrome
(cytochrome b559), representing the redox
element responsible for the NADPH-dependent reduction of
oxygen to superoxide (O
Volume 272, Number 20,
Issue of May 16, 1997
pp. 13292-13301
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
Julius Friedrich Cohnheim-Minerva Center for
Phagocyte Research, Department of Human Microbiology, Sackler School of
Medicine, Tel Aviv University, Tel Aviv 69978, Israel and
§ Pentapharm Ltd., Engelgasse 109, CH-4002, Basel, Switzerland
2), two cytosolic components
(p47phox, p67phox), and the small GTPase Rac (1 or 2).
We found that 4-(2-aminoethyl)-benzenesulfonyl fluoride (AEBSF), an
irreversible serine protease inhibitor, prevented the elicitation of
O2 production in intact macrophages and the amphiphile-dependent activation of NADPH oxidase in a
cell-free system, consisting of solubilized membrane or purified
cytochrome b559 combined with total cytosol or
a mixture of recombinant p47phox, p67phox, and Rac1.
AEBSF acted at the activation step and did not interfere with the
ensuing electron flow. It did not scavenge oxygen radicals and did not
affect assay reagents. Five other serine protease inhibitors (three
irreversible and two reversible) were found to lack an inhibitory
effect on cell-free activation of NADPH oxidase. A structure-function
study of AEBSF analogues demonstrated that the presence of a sulfonyl
fluoride group was essential for inhibitory activity and that compounds
containing an aminoalkylbenzene moiety were more active than
amidinobenzene derivatives. Exposure of the membrane fraction or of
purified cytochrome b559, but not of cytosol or
recombinant cytosolic components, to AEBSF, in the presence of a
critical concentration of the activating amphiphile lithium dodecyl
sulfate, resulted in a marked impairment of their ability to support
cell-free NADPH oxidase activation upon complementation with untreated
cytosol or cytosolic components. Kinetic analysis of the effect of
varying the concentration of each of the three cytosolic components on
the inhibitory potency of AEBSF indicated that this was inversely
related to the concentrations of p47phox and, to a lesser
degree, p67phox. AEBSF also prevented the amphiphile-elicited
translocation of p47phox and p67phox to the membrane.
These results are interpreted as indicating that AEBSF interferes with
the binding of p47phox and/or p67phox to cytochrome
b559, probably by a direct effect on cytochrome b559.
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