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Originally published In Press as doi:10.1074/jbc.M101801200 on April 5, 2001

J. Biol. Chem., Vol. 276, Issue 25, 22941-22947, June 22, 2001
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Activator Protein-1 Transcription Factor Mediates Bombesin-stimulated Cyclooxygenase-2 Expression in Intestinal Epithelial Cells*

Yan-Shi GuoDagger , Mark R. HellmichDagger §, Xiao Dong WenDagger , and Courtney M. Townsend Jr.Dagger

From the Departments of Dagger  Surgery and § Physiology and Biophysics, University of Texas Medical Branch, Galveston, Texas 77555

Colorectal carcinogenesis is a complex, multistep process involving genetic alterations and progressive changes in signaling pathways regulating intestinal epithelial cell proliferation, differentiation, and apoptosis. Although cyclooxygenase-2 (COX-2), gastrin-releasing peptide (GRP), and its receptor, GRP-R, are not normally expressed by the epithelial cells lining the human colon, the levels of all three proteins are aberrantly overexpressed in premalignant adenomatous polyps and colorectal carcinomas of humans. Overexpression of these proteins is associated with altered epithelial cell growth, adhesion, and tumor cell invasiveness, both in vitro and in vivo; however, a mechanistic link between GRP-R-mediated signaling pathways and increased COX-2 overexpression has not been established. We report that bombesin, a homolog of GRP, potently stimulates the expression of COX-2 mRNA and protein as well as the release of prostaglandin E2 from a rat intestinal epithelial cell line engineered to express GRP-R. Bombesin stimulation of COX-2 expression requires an increase in [Ca2+]i, activation of extracellular signal-regulated kinase (ERK)-1 and -2 and p38MAPK, and increased activation and expression of the transcription factors Elk-1, ATF-2, c-Fos, and c-Jun. These data suggest that the expression of GRP-R in intestinal epithelial cells may play a role in carcinogenesis by stimulating COX-2 overexpression through an activator protein-1-dependent pathway.

* This work was supported by National Institutes of Health Grants PO1 DK35608 and R01 DK48345.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 Surgery, University of Texas Medical Branch, 301 University Blvd., Galveston, TX 77555-0527. Tel.: 409-772-1285; Fax: 409-772-5611; E-mail: ctownsen@utmb.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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