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NADPH-oxidase activation by protein kinase C-isotypes
P Sharma1, A T Evans, P J Parker
1Department of Pharmacognosy, School of Pharmacy, University of London, U.K.
Biochemical and Biophysical Research Communications
|June 28, 1991
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 Ca2+ for activation of the oxidase. In the presence of TPA, the activation of the oxidase was greatly enhanced, and alpha-, and gamma-subtypes were strongly Ca2+ dependent in this system. Beta-, delta- and epsilon-subtypes were active both in the presence and absence of free Ca2+ ions. The results suggest that at resting Ca2+ levels certain PKC-isotypes can activate NADPH-oxidase.