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(Received for publication, August 9, 1996, and in revised form, September 18, 1996)
From the Julius Friedrich Cohnheim-Minerva Center for Phagocyte
Research, Department of Human Microbiology, Sackler School of Medicine,
Tel Aviv University, Tel Aviv 69978, Israel
The superoxide (O
Volume 271, Number 48,
Issue of November 29, 1996
pp. 30326-30329
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
2)-generating NADPH
oxidase of phagocytes is a multicomponent complex consisting of a
membrane-associated flavocytochrome (cytochrome
b559), bearing the NADPH binding site and two
redox centers (FAD and heme) and three cytosolic activating components:
p47phox, p67phox, and the small GTPase Rac (1 or 2).
The canonical view is that the induction of O2 generation
involves the stimulus-dependent assembly of all three
cytosolic components with cytochrome b559, a
process mimicked in vitro by a cell-free system activated
by anionic amphiphiles. We studied the requirement for individual cytosolic components in the activation of NADPH oxidase in a cell-free system consisting of purified and relipidated cytochrome
b559, recombinant p47phox,
p67phox, and Rac1, and the amphiphile, lithium dodecyl sulfate.
We found that pronounced activation of NADPH oxidase can be achieved by exposing cytochrome b559 to p67phox and
Rac1, in the total absence of p47phox (turnover = 60 mol O2/s/mol cytochrome b559).
However, maximal activation (turnover = 153 mol
O2/s/mol cytochrome b559) could only
be obtained in the presence of p47phox. O2 production,
in the absence of p47phox, was dependent on: high molar ratios
of p67phox and Rac1 to cytochrome b559,
Rac1 being in the GTP-bound form, cytochrome
b559 being saturated with FAD, and an optimal
concentration of amphiphile. Single cytosolic components or
combinations of two cytosolic components, other than p67phox
and Rac1, were incapable of activation. We conclude that
p67phox and Rac1 are the only cytosolic components directly
involved in the induction of electron transport in cytochrome
b559. p47phox appears to facilitate or
stabilize the interaction of p67phox and, possibly, Rac1 with
cytochrome b559, and is required for optimal
generation of O2 under physiological conditions.
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