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J Biol Chem, Vol. 275, Issue 20, 14838-14845, May 19, 2000
§,,
From the We investigated whether microtubule-interfering
agents (MIAs: taxol, colchicine, nocodazole, vinblastine, vincristine,
17- 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
-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.
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