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Originally published In Press as doi:10.1074/jbc.M201126200 on March 23, 2002

J. Biol. Chem., Vol. 277, Issue 22, 19530-19537, May 31, 2002
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Surfactant Protein D Gene Regulation
INTERACTIONS AMONG THE CONSERVED CCAAT/ENHANCER-BINDING PROTEIN ELEMENTS*

Yanchun He and Erika CrouchDagger

From the Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, Missouri 63110

Surfactant protein D (SP-D) plays roles in pulmonary host defense and surfactant homeostasis and is increased following acute lung injury. Given the importance of CCAAT/enhancer-binding protein (C/EBP)-binding elements in the systemic acute-phase response and lung development and the expression of C/EBP isoforms by lung epithelial cells, we hypothesized that conserved C/EBP motifs in the near-distal and proximal promoters contribute to the regulation of SP-D expression by C/EBPs. Five SP-D motifs (-432, -340, -319, -140, and -90) homologous to the C/EBP consensus sequence specifically bound to C/EBPs in gel shift assays, and four of the five sites (-432, -340, -319, and -90) efficiently competed for the binding of C/EBPalpha , C/EBPbeta , or C/EBPdelta to consensus oligomers. Cotransfection of C/EBPalpha , C/EBPbeta , or C/EBPdelta cDNA in H441 lung adenocarcinoma cells significantly increased the luciferase activity of a wild-type SP-D promoter construct containing 698 bp of upstream sequence (SS698). Transfection of C/EBP also increased the level of endogenous SP-D mRNA in H441 cells. Transactivation of the reporter construct was abrogated by deletion of sequences upstream of -205. Independent site-directed mutagenesis of the sites at -432, -340, and -319 reduced C/EBP-mediated activation by ~50%, and mutagenesis of the site at -432 in combination with either of the tandem sites at -340 and -319 blocked activation. The conserved AP-1 element at -109 was required for maximal promoter activity, but not for the transactivation of SS698 by C/EBPs. Thus, interactions among C/EBP elements in the near-distal promoter can modulate the promoter activity of SP-D.

* This work was supported by National Institutes of Health Grants HL-44015 and HL-29594.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 To whom correspondence should be addressed: Dept. of Pathology and Immunology, Barnes-Jewish Hospital, Rm. 2457, North Campus, Surgical Pathology Mailstop 90-31-649, 216 S. Kingshighway Blvd., St. Louis, MO 63110. Tel.: 314-454-8462; Fax: 314-454-5505; E-mail: crouch@path.wustl.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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