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J. Biol. Chem., Vol. 265, Issue 29, 17550-17559, Oct, 1990
DN Burnham, DJ Uhlinger and JD Lambeth
The superoxide-generating respiratory burst oxidase (NADPH oxidase) from
human neutrophils can be activated in a cell-free system consisting of
plasma membranes, cytosol, and an anionic amphiphile such as sodium dodecyl
sulfate (SDS) or arachidonate, and guanosine 5'-(3-O- thio)triphosphate
(GTP(gamma)S) augments activation. We report herein that short-chain
diacylglycerols (e.g. dioctanoylglycerol (diC8)) synergize with SDS in the
activation of superoxide generation in a dose- and time-dependent manner,
resulting in rates up to 1400 nmol/min/mg plasma membrane protein, or
250-700% higher than the rate seen with SDS alone. diC8 did not affect
significantly the dose response for either cytosol or SDS, indicating that
the activation was not due to increased sensitivity of the oxidase toward
either of these components. At optimal concentrations of SDS and diC8,
additional activation was observed in the presence of GTP(gamma)S,
indicating that diC8 and GTP activate by separate mechanisms. In contrast
to diC8, other known activators of protein kinase C (phorbol myristate
acetate and mezerein) augmented SDS activation only minimally (typically
20-30%), and neither diacylglycerols nor tumor promoters activated in the
absence of SDS. Activation by diC8 was calcium and phosphatidylserine
independent, and the specificity for neutral lipids was atypical for
protein kinase C. Inhibitors of protein kinase C (staurosporine and a
peptide substrate analog) also failed to inhibit the response.
Nevertheless, phosphorylation of several neutrophil proteins including
p47phox was seen with both SDS and diC8, and synergistic phosphorylation of
p47phox was seen when both activating factors were present. Thus,
diacylglycerol synergizes with SDS in activating both superoxide generation
and p47phox phosphorylation in the cell-free activation system, but the
activation is atypical of a protein kinase C mechanism.
Diradylglycerol synergizes with an anionic amphiphile to activate superoxide generation and phosphorylation of p47phox in a cell-free system from human neutrophils
Department of Biochemistry, Emory University Medical School, Atlanta, Georgia 30322.
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