Calmodulin-dependent stimulation of the NADPH oxidase of human neutrophils.

The NADPH oxidase of human neutrophils is highly sensitive to calcium concentration and is inhibited in intact cells and cell-free preparations by various phenothiazine drugs. Addition of calmodulin to preparations of NADPH oxidase stimulates enzymatic rates from 1.4-2.5-fold. Addition of calmodulin and calcium, but not calcium alone, to NADPH oxidase preparations which have been inactivated by EDTA results in the restoration of activity. No activation is observed when membrane preparations containing latent NADPH oxidase are exposed to calcium and calmodulin. These studies suggest a role for calmodulin in the control of NADPH oxidase but that calmodulin alone is not sufficient for activation.