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The Journal of Immunology, 2004, 173: 7462-7470.
Copyright © 2004 by The American Association of Immunologists

Reconstitution of Chemotactic Peptide-Induced Nicotinamide Adenine Dinucleotide Phosphate (Reduced) Oxidase Activation in Transgenic COS-phox Cells1

Rong He*, Masakatsu Nanamori*, Hairong Sang*, Hong Yin*, Mary C. Dinauer{dagger} and Richard D. Ye2,*

* Department of Pharmacology, College of Medicine, University of Illinois, Chicago, IL 60612; and {dagger} Herman B. Wells Center for Pediatric Research, Riley Hospital for Children, Indiana University School of Medicine, Indianapolis, IN 46202

A whole-cell-based reconstitution system was developed to study the signaling mechanisms underlying chemoattractant-induced activation of NADPH oxidase. This system takes advantage of the lack of formyl peptide receptor-mediated response in COS-phox cells expressing gp91phox, p22phox, p67phox, and p47phox, which respond to phorbol ester and arachidonic acid with O

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2 production. By exogenous expression of signaling molecules enriched in neutrophils, we have identified several critical components for fMLP-induced NADPH oxidase activation. Expression of PKC{delta}, but not PKC{alpha}, -{beta}II, and -{zeta}, is necessary for the COS-phox cells to respond to fMLP. A role of PKC{delta} in neutrophil NADPH oxidase was confirmed based on the ability of fMLP to induce PKC{delta} translocation and the sensitivity of fMLP-induced O

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2 production to rottlerin, a PKC{delta}-selective inhibitor. Optimal reconstitution also requires phospholipase C-{beta}2 and PI3K-{gamma}. We found that formyl peptide receptor could use the endogenous Rac1 as well as exogenous Rac1 and Rac2 for NADPH oxidase activation. Exogenous expression of p40phox potentiated fMLP-induced O

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2 production and raised the level of O

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2 in unstimulated cells. Collectively, these results provide first direct evidence for reconstituting fMLP-induced O

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2 production in a nonhemopoietic cell line, and demonstrate the requirement of multiple signaling components for optimal activation of NADPH oxidase by a chemoattractant.




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