JBC Transcription and Nuclear Factor Monoclonals

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Originally published In Press as doi:10.1074/jbc.M210314200 on March 4, 2003

J. Biol. Chem., Vol. 278, Issue 19, 17210-17217, May 9, 2003
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p47phox Participates in Activation of RelA in Endothelial Cells*

Ying GuDagger , You Cheng XuDagger , Ru Feng WuDagger , Fiemu E. Nwariaku§, Rhonda F. SouzaDagger , Sonia C. Flores, and Lance S. TeradaDagger ||

From the Departments of Dagger  Internal Medicine and § Surgery, University of Texas Southwestern and the Dallas Veterans Affairs Medical Center, Dallas, Texas 75216 and the  Webb-Waring Institute, Denver, Colorado 80262

Activation of endothelial cell NF-kappa B by interleukin (IL)-1 constitutes an event critical to the progression of the innate immune response. In this context, oxidants have been associated with NF-kappa B activation, although the molecular source and mechanism of targeting have remained obscure. We found that RelA, essential for NF-kappa B activation by IL-1, was associated with the NADPH oxidase adapter protein p47phox in yeast two-hybrid, coprecipitation, and in vitro binding studies. RelA and p47-GFP also colocalized in endothelial cells in focal submembranous dorsoventral protrusions. Overexpression of p47phox synergized with IL-1beta in the activation of an artificial kappa B-luciferase reporter and specifically augmented IL-1beta -induced RelA transactivation activity. p47phox overexpression also greatly increased IL-1beta -stimulated RelA phosphorylation, whereas it had no effect on I-kappa B degradation or on RelA nuclear translocation or kappa B binding. The tandem SH3 domains of p47phox were found to associate with a proline-rich mid-region of RelA (RelA-PR) located between the Rel homology and transactivation domains. The RelA-PR peptide blocked interaction of p47phox and RelA, and ectopic expression of RelA-PR abrogated IL-1beta -induced transactivation of the NF-kappa B-dependent E-selectin promoter. Further, suppression of NADPH oxidase function through the inhibitor diphenylene iodonium, the superoxide dismutase mimetic Mn(III) tetrakis(4-benzoic acid)porphyrin (MnTBAP), or expression of a dominant interfering mutant of a separate NADPH oxidase subunit (p67(V204A)) decreased IL-1beta -induced E-selectin promoter activation, suggesting that p47phox facilitates NF-kappa B activation through linkage with the NADPH oxidase. IL-1beta rapidly increased tyrosine phosphorylation of IL-1 type I receptor-associated proteins, suggesting that oxidants may operate through inactivation of local protein-tyrosine phosphatases in the proximal IL-1beta signaling pathway leading to RelA activation.

* This work was supported by National Institutes of Health Grants R01-HL61897 and R01-HL67256 and by the Medical Research Service of the Department of Veterans Affairs and the Robert Wood Johnson Foundation.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: Dallas VAMC, MC 151, 4500 S. Lancaster Rd., Dallas, TX 75216. Tel.: 214-857-0753; Fax: 214-857-0340; E-mail: lance.terada@med.va.gov.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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