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J Biol Chem, Vol. 274, Issue 22, 15533-15537, May 28, 1999
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From the The leukocyte NADPH oxidase is an enzyme present
in phagocytes and B lymphocytes that when activated catalyzes the
production of O Department of Molecular and Experimental
Medicine and the Department of Immunology, The Scripps Research
Institute, La Jolla, California 92037
2 from oxygen at the expense of NADPH. A
correlation between the activation of the oxidase and the
phosphorylation of p47PHOX, a cytosolic oxidase component, is
well recognized in whole cells, and direct evidence for a relationship
between the phosphorylation of this oxidase component and the
activation of the oxidase has been obtained in a number of cell-free
systems containing neutrophil membrane and cytosol. Using superoxide
dismutase-inhibitable cytochrome c reduction to quantify
O2 production, we now show that p47PHOX phosphorylated
by protein kinase C activates the NADPH oxidase not only in a cell-free
system containing neutrophil membrane and cytosol, but also in a system
in which the cytosol is replaced by the recombinant proteins
p67PHOX, Rac2, and phosphorylated p47PHOX, suggesting
that neutrophil plasma membrane plus those three cytosolic proteins are
both necessary and sufficient for oxidase activation. In both the
cytosol-containing and recombinant cell-free systems, however,
activation by SDS yielded greater rates of O2 production than
activation by protein kinase C-phosphorylated p47PHOX,
indicating that a system that employs protein kinase C-phosphorylated p47PHOX as the sole activating agent, although more
physiological than the SDS-activated system, is nevertheless incomplete.
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