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Abstract
The cell free activation of NADPH-Oxidase in membranes of mouse peritoneal macrophages by purified PKC-isotypes was investigated. Unstimulated intrinsic activity of PKC-isotypes showed little dependence on Ca 2+ for activation of the oxidase. In the presence of TPA, the activation of the oxidase was greatly enhanced, and α-, and γ-subtypes were strongly Ca 2+ dependent in this system. β-, δ- and ϵ-subtypes were active both in the presence and absence of free Ca 2+ ions. The results suggest that at resting Ca 2+ levels certain PKC-isotypes can activate NADPH-oxidase.
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