NDLI: Activation of the Leukocyte NADPH Oxidase by Protein Kinase C in a Partially Recombinant Cell-free System

Content Provider	Journal of Biological Chemistry (JBC)
Author	Lopes, Lucia Rossetti Hoyal, Carolyn R. Knaus, Ulla G. Babior, Bernard M.
Abstract	The leukocyte NADPH oxidase is an enzyme present in phagocytes and B lymphocytes that when activated catalyzes the production of O⨪2 from oxygen at the expense of NADPH. A correlation between the activation of the oxidase and the phosphorylation of p47PHOX, a cytosolic oxidase component, is well recognized in whole cells, and direct evidence for a relationship between the phosphorylation of this oxidase component and the activation of the oxidase has been obtained in a number of cell-free systems containing neutrophil membrane and cytosol. Using superoxide dismutase-inhibitable cytochrome c reduction to quantify O⨪2 production, we now show that p47PHOX phosphorylated by protein kinase C activates the NADPH oxidase not only in a cell-free system containing neutrophil membrane and cytosol, but also in a system in which the cytosol is replaced by the recombinant proteins p67PHOX, Rac2, and phosphorylated p47PHOX, suggesting that neutrophil plasma membrane plus those three cytosolic proteins are both necessary and sufficient for oxidase activation. In both the cytosol-containing and recombinant cell-free systems, however, activation by SDS yielded greater rates of O⨪2 production than activation by protein kinase C-phosphorylated p47PHOX, indicating that a system that employs protein kinase C-phosphorylated p47PHOX as the sole activating agent, although more physiological than the SDS-activated system, is nevertheless incomplete.
Related Links	http://www.jbc.org/content/274/22/15533.abstract
Ending Page	15537
Starting Page	15533
Page Count	5
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	22
Volume Number	274
DOI	10.1074/jbc.274.22.15533
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1999-05-28
Access Restriction	Open
Subject Keyword	Guanosine 5-O-(3-thiotriphosphate) (GTPγS) 1,4-piperazinediethanesulfonic acid (PIPES) GlutathioneS-transferase (GST) Guanosine 5′-O-(2-thiodiphosphate) (GDPβS) Polyacrylamide gel electrophoresis (PAGE) CELL BIOLOGY AND METABOLISM
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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