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Arachidonic acid activates NADPH oxidase by a direct, calmodulin-regulated mechanism
1Department of Cell Biology, Neurobiology and Anatomy, Ohio State University, Columbus 43210, USA. P.Hartfield@flinders.edu.au
Abstract:
In intact neutrophils, arachidonic acid rapidly and transiently activated NADPH oxidase-mediated superoxide generation. Inhibitors of protein kinases (staurosporine and H-7) failed to markedly attenuate arachidonic acid-stimulated superoxide generation. Conversely, the calmodulin antagonist W-7 blocked this arachidonic acid-stimulated response. Similarly, diphenylene iodonium potently inhibited superoxide release. These results suggest that arachidonic acid directly activates the membrane-associated NADPH oxidase and calmodulin and/or calmodulin-binding proteins are required for the assembly of the active oxidase.