NADPH-oxidase activation by protein kinase C-isotypes.
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.
Sharma
P
P
Department of Pharmacognosy, School of Pharmacy, University of London, U.K.
Evans
A T
AT
Parker
P J
PJ
Evans
F J
FJ
D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D002462:Cell Membrane / Q000201:enzymology; D002474:Cell-Free System; D004789:Enzyme Activation; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008264:Macrophages / Q000201:enzymology*; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D019255:NADPH Oxidases; D011493:Protein Kinase C / Q000302:isolation & purification / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D007527:Isoenzymes; D009247:NADH, NADPH Oxidoreductases; D019255:NADPH Oxidases; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate; D002118:Calcium