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Originally published In Press as doi:10.1074/jbc.M005406200 on August 7, 2000

J. Biol. Chem., Vol. 275, Issue 42, 32566-32571, October 20, 2000
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A Regulatory Role for ADP-ribosylation Factor 6 (ARF6) in Activation of the Phagocyte NADPH Oxidase*

Raya R. DanaDagger , Calvin Eigsti§, Kevin L. Holmes§, and Thomas L. LetoDagger

From the Dagger  Laboratory of Host Defenses and the § Flow Cytometry Section, NIAID, National Institutes of Health, Bethesda, Maryland 20892

In activated neutrophils NADPH oxidase is regulated through various signaling intermediates, including heterotrimeric G proteins, kinases, GTPases, and phospholipases. ADP-ribosylation factor (ARF) describes a family of GTPases associated with phospholipase D (PLD) activation. PLD is implicated in NADPH oxidase activation, although it is unclear whether activation of PLD by ARF is linked to receptor-mediated oxidase activation. We explored whether ARF participates in NADPH oxidase activation by formyl-methionine-leucine-phenylalanine (fMLP) and whether this involves PLD. Using multicolor forward angle light scattering analyses to measure superoxide production in differentiated neutrophil-like PLB-985 cells, we tested enhanced green fluorescent fusion proteins of wild-type ARF1 or ARF6, or their mutant counterparts. The ARF6(Q67L) mutant defective in GTP hydrolysis caused increased superoxide production, whereas the ARF6(T27N) mutant defective in GTP binding caused diminished responses to fMLP. The ARF1 mutants had no effect on fMLP responses, and none of the ARF proteins affected phorbol 12-myristate 13-acetate-elicited oxidase activity. PLD inhibitors 1-butanol and 2,3-diphosphoglycerate, or the ARF6(N48R) mutant assumed to be defective in PLD activation, blocked fMLP-elicited oxidase activity in transfected cells. The data suggest that ARF6 but not ARF1 modulates receptor-mediated NADPH oxidase activation in a PLD-dependent mechanism. Because PMA-elicited NADPH oxidase activation also appears to be PLD-dependent, but ARF-independent, ARF6 and protein kinase C may act through distinct pathways, both involving PLD.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: National Institutes of Health, Bldg. 10, Rm. 11N106, Bethesda, MD 20892. Tel.: 301-402-5120; Fax: 301-402-4369; E-mail: tleto@niaid.nih.gov.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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