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Originally published In Press as doi:10.1074/jbc.M211744200 on February 27, 2003

J. Biol. Chem., Vol. 278, Issue 19, 16683-16689, May 9, 2003
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ERK Activation Is Required for Double-stranded RNA- and Virus-induced Interleukin-1 Expression by Macrophages*

Leonard B. Maggi Jr.Dagger §, Jason M. Moran§||, R. Mark L. Buller||, and John A. Corbett||**

From the  Edward A. Doisy Department of Biochemistry and Molecular Biology and the || Department of Molecular Microbiology and Immunology, St. Louis University School of Medicine, St. Louis, Missouri 63104

Double-stranded (ds) RNA, which accumulates during viral replication, activates the antiviral response of infected cells. In this study, we have identified a requirement for extracellular signal-regulated kinase (ERK) in the regulation of interleukin 1 (IL-1) expression by macrophages in response to dsRNA and viral infection. Treatment of RAW 264.7 cells or mouse macrophages with dsRNA stimulates ERK phosphorylation that is first apparent following a 15-min incubation and persists for up to 60 min, the accumulation of iNOS and IL-1 mRNA following a 6-h incubation, and the expression of iNOS and IL-1 at the protein level following a 24-h incubation. Inhibitors of ERK activation prevent dsRNA-induced ERK phosphorylation and IL-1 expression by macrophages. The regulation of macrophage activation by ERK appears to be selective for IL-1, as ERK inhibition does not attenuate dsRNA-induced iNOS expression by macrophages. dsRNA stimulates both ERK activation and IL-1 expression by macrophages isolated from dsRNA-dependent protein kinase (PKR)-deficient mice, indicating that PKR does not participate in this antiviral response. These findings support a novel PKR-independent role for ERK in the regulation of the antiviral response of IL-1 expression and release by macrophages.

* This work was supported by National Institutes of Health Grants DK-52194 and AI-44458 (to J. A. C.).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.

Dagger Present address: Dept. of Internal Medicine, Division of Molecular Oncology, Washington University School of Medicine, St. Louis, MO 63110.

§ These authors contributed equally to this work.

** To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, St. Louis University School of Medicine, 1402 S. Grand Blvd., St. Louis, MO 63104. Tel.: 314-577-8165; Fax: 314-577-8156; E-mail: corbettj@slu.edu.

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