Arachidonic acid activates NADPH oxidase by a direct, calmodulin-regulated mechanism.

P J Hartfield, J M Robinson

Index: Prostaglandins Other Lipid Mediat. 56(1) , 1-6, (1998)

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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.