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J. Biol. Chem., Vol. 262, Issue 12, 5563-5569, 04, 1987
JT Curnutte, R Kuver and PJ Scott
The superoxide-generating enzyme of human neutrophils, NADPH oxidase, is
converted from an inactive to an active form upon stimulation of the
neutrophil. This activation process was examined using a recently developed
cell-free system in which dormant oxidase is activated by arachidonic acid
in the presence of a soluble factor from the neutrophil (Curnutte, J. T.
(1985) J. Clin. Invest. 75, 1740-1743). NADPH oxidase from unstimulated
human neutrophils was detected only in the membrane fraction. The soluble
activation factor was localized entirely to the cytosolic fraction and
exhibited two peaks of activity when partially purified under nondenaturing
conditions: a major peak with a molecular mass of approximately 250 kDa and
a variable minor peak with a mass of approximately 40 kDa. Both forms
activated NADPH oxidase in a similar manner and did not exhibit synergy
when combined. The cytosolic factor is not protein kinase C (or another
kinase) as both peaks of factor activity could be resolved from the protein
kinase C peak and neither required calcium or ATP to activate the oxidase.
Activation of NADPH oxidase did require the simultaneous presence of the
membrane fraction, the cytosolic factor, arachidonic acid, and magnesium.
Following activation, however, only the membrane fraction was then required
for O2- production. Cytosolic factor levels were normal in five patients
with either X-linked or autosomal recessive cytochrome b-negative chronic
granulomatous disease. In contrast, the membrane fractions from each failed
to generate O2-, indicating that the defects in these two genetic forms of
chronic granulomatous disease reside either in the oxidase itself or in a
membrane component required for activation.
Activation of neutrophil NADPH oxidase in a cell-free system. Partial purification of components and characterization of the activation process
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