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Blood Cells Mol Dis. 1995;21(3):201-6.

Cell-free activation of the respiratory burst oxidase by protein kinase C.

Author information

1
Department of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, CA 92037, USA.

Abstract

In 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.

PMID:
8673472
DOI:
10.1006/bcmd.1995.0023
[Indexed for MEDLINE]

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