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J. Biol. Chem., Vol. 278, Issue 4, 2124-2130, January 24, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/4/2124    most recent M202443200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Liu, G. Articles by Dong, Z. Search for Related Content PubMed PubMed Citation Articles by Liu, G. Articles by Dong, Z. Social Bookmarking                      What's this?

NS-398 and Piroxicam Suppress UVB-induced Activator Protein 1 Activity by Mechanisms Independent of Cyclooxygenase-2^*

Guangming Liu, Wei-Ya Ma, Ann M. Bode, Yiguo Zhang, and Zigang Dong

From the Hormel Institute, University of Minnesota, Austin, Minnesota 55912

Cyclooxygenases (COX) are rate-limiting enzymes that catalyze the conversion of arachidonic acid to prostaglandins, which are involved in many physiological and pathophysiological responses. COX-2, one of two isoforms of COX, was recently found to play an important role in carcinogenesis in many cell and tissue types. COX-2 inhibitors, which belong to the family of nonsteroidal anti-inflammatory drugs, are believed to be effective in many biological activities such as tumor chemoprevention because of their inhibition of COX-2. However, in the present study we found that both piroxicam, a general COX inhibitor, and NS-398, a COX-2 selective inhibitor, effectively suppressed the activation of transcription factor activator protein 1 (AP-1) induced by ultraviolet B (UVB) or 12-O-tetradecanoylphorbol-13-acetate in mouse epidermal JB6 cells. These COX-2 inhibitors could also inhibit 12-O-tetradecanoylphorbol-13-acetate-induced cell transformation. UVB significantly increased AP-1 activity in Cox-2^/ fibroblasts transfected with an AP-1 luciferase reporter gene, and this increase was blocked by NS-389 or piroxicam. In JB6, Cox-2^/, or wild-type Cox-2^+/+ cells, both NS-398 and piroxicam inhibited UVB-induced phosphorylation of c-Jun NH₂-terminal kinases, the kinases that activate the AP-1/c-Jun complex. Based on our results, we propose that the inhibition of AP-1 activity by COX-2 inhibitors NS-398 or piroxicam may occur by a mechanism that is independent of COX-2.

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