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J Biol Chem, Vol. 275, Issue 20, 14838-14845, May 19, 2000

Microtubule-interfering Agents Stimulate the Transcription of Cyclooxygenase-2
EVIDENCE FOR INVOLVEMENT OF ERK1/2 AND p38 MITOGEN-ACTIVATED PROTEIN KINASE PATHWAYS*

Kotha SubbaramaiahDagger §, Janice C. HartDagger , Larry Norton, and Andrew J. DannenbergDagger

From the Dagger  Department of Medicine, New York Presbyterian Hospital-Cornell and Strang Cancer Prevention Center and  Breast Cancer Medicine Service, Memorial Sloan-Kettering Cancer Center, New York, New York 10021

We investigated whether microtubule-interfering agents (MIAs: taxol, colchicine, nocodazole, vinblastine, vincristine, 17-beta -estradiol, 2-methoxyestradiol) altered cyclooxygenase-2 (COX-2) expression in human mammary epithelial cells. MIAs enhanced prostaglandin E2 synthesis and increased levels of COX-2 protein and mRNA. Nuclear run-off assays revealed increased rates of COX-2 transcription after treatment with MIAs. Calphostin C, an inhibitor of protein kinase C, blocked the induction of COX-2 by MIAs. The stimulation of COX-2 promoter activity by MIAs was inhibited by overexpressing dominant negative forms of Rho and Raf-1. MIAs stimulated ERK, JNK, and p38 mitogen-activated protein kinases (MAPK); pharmacological inhibitors of MAPK kinase and p38 MAPK blocked the induction of COX-2 by MIAs. Overexpressing dominant negative forms of ERK1 or p38 MAPK inhibited MIA-mediated activation of the COX-2 promoter. MIAs stimulated the binding of the activator protein-1 transcription factor complex to the cyclic AMP response element in the COX-2 promoter. A dominant negative form of c-Jun inhibited the activation of the COX-2 promoter by MIAs. Additionally, cytochalasin D, an agent that inhibits actin polymerization, stimulated COX-2 transcription by the same signaling pathway as MIAs. Thus, microtubule- or actin-interfering agents stimulated MAPK signaling and activator protein-1 activity. This led, in turn, to induction of COX-2 gene expression via the cyclic AMP response element site in the COX-2 promoter.


* This work was supported in part by S/G 2P01 CA68425 and the James E. Olson Memorial Fund.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: New York Presbyterian Hospital-Cornell, Div. of Gastroenterology and Hepatology, Rm. F-203, 1300 York Ave., New York, NY 10021. Tel.: 212-746-4402; Fax: 212-746-4885; E-mail: ksubba@mail.med.cornell.edu.


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

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