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Originally published In Press as doi:10.1074/jbc.M910269199 on March 20, 2000

J. Biol. Chem., Vol. 275, Issue 21, 16373-16381, May 26, 2000
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The C/EBP bZIP Domain Can Mediate Lipopolysaccharide Induction of the Proinflammatory Cytokines Interleukin-6 and Monocyte Chemoattractant Protein-1*

Hsien-Ming HuDagger , Qiang TianDagger , Mark Baer§, Chauncey J. SpoonerDagger , Simon C. Williams, Peter F. Johnson§, and Richard C. SchwartzDagger ||

From the Dagger  Department of Microbiology, Michigan State University, East Lansing, Michigan 48824-1101, the § Eukaryotic Transcriptional Regulation Section, Regulation of Cell Growth Laboratory, NCI, Frederick Cancer Research and Development Center, Frederick, Maryland 21702-1201, and the  Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, Texas 79430

C/EBPalpha , beta , and delta  are all expressed by bone marrow-derived macrophages. Ectopic expression of any of these transcription factors is sufficient to confer lipopolysaccharide (LPS)-inducible expression of interleukin-6 (IL-6) and monocyte chemoattractant protein-1 (MCP-1) to a B lymphoblast cell line, which normally lacks C/EBP factors and does not display LPS induction of proinflammatory cytokines. Thus, the activities of C/EBPalpha , beta , and delta  are redundant in regard to expression of IL-6 and MCP-1. Surprisingly, the bZIP region of C/EBPbeta , which lacks any previously described activation domains, can also confer LPS-inducible expression of IL-6 and MCP-1 in stable transfectants. Transient transfections reveal that the bZIP regions of C/EBPbeta , C/EBPdelta , and, to a lesser extent, C/EBPalpha can activate the IL-6 promoter and augment its induction by LPS. Furthermore, the transdominant inhibitor, LIP, can activate expression from the IL-6 promoter. The ability of the C/EBPbeta bZIP region to activate the IL-6 promoter in transient transfections is completely dependent upon an intact NF-kappa B-binding site, supporting a model where the bZIP protein primarily functions to augment the activity of NF-kappa B. Replacement of the leucine zipper of C/EBPbeta with that of GCN4 yields a chimeric protein that can dimerize and specifically bind to a C/EBP consensus sequence, but shows a markedly reduced ability to activate IL-6 and MCP-1 expression. These results implicate the leucine zipper domain in some function other than dimerization with known C/EBP family members, and suggest that C/EBP redundancy in regulating cytokine expression may result from their highly related bZIP regions.

* This work was supported by American Heart Association, Michigan Affiliate Grant-in-aid 980807W and the American Heart Association Grant-in-aid 9950490N (to R. C. S.), The American Cancer Society Grant DB-110, the Michigan State University Biotechnology Research Center, and the Cancer Center at Michigan State University (to R. C. S.).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: Dept. of Microbiology, Michigan State University, East Lansing, MI 48824-1101. Tel.: 517-353-4816; Fax: 517-353-8957; E-mail: schwart9@pilot.msu.edu.

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