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pubmed-article:8673472pubmed:abstractTextIn intact neutrophils, phorbol ester treatment activates the respiratory burst oxidase, the enzyme responsible for O2-production by phagocytes. This effect is thought to be dependent on protein kinase C and on the phosphorylation of p47phox. In this paper, we report that protein kinase C activates the respiratory burst oxidase in a cell-free system consisting of isolated neutrophil cytosol and membrane. Oxidase activation required a highly active protein kinase C, recombinant p47phow and ATP, and was inhibited by the protein kinase C inhibitors H-7 and GF-109203X. PERIl depletion of cytosolic ATP by dialysis reduced oxidase activation by over 50% In contrast, neither protein kinase C inhibitors nor ATP depletion affected oxidase activation by SDS. These findings strongly suggest that in the cell-free system, the oxidase can be activated by the phosphorylation of p47phox.lld:pubmed
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pubmed-article:8673472pubmed:articleTitleCell-free activation of the respiratory burst oxidase by protein kinase C.lld:pubmed
pubmed-article:8673472pubmed:affiliationDepartment of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, CA 92037, USA.lld:pubmed
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pubmed-article:8673472pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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