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Nucleic Acids Research 2006 34(1):217-231; doi:10.1093/nar/gkj422
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Published online 5 January 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

Functional role of NF-IL6ß and its sumoylation and acetylation modifications in promoter activation of cyclooxygenase 2 gene

Ju-Ming Wang1, Chiung-Yuan Ko1, Lei-Chin Chen1,2, Wen-Lin Wang1 and Wen-Chang Chang1,*

1Department of Pharmacology, College of Medicine, National Cheng Kung University Tainan, Taiwan 2Department of Medical Nutrition, I-Shou University Dashu Township, Kaohsiung County, Taiwan

*To whom correspondence should be addressed. Tel: +886 6 235 3535 Ext. 5496; Fax: +886 6 274 9296; Email: wcchang{at}mail.ncku.edu.tw

Received September 13, 2005. Revised December 14, 2005. Accepted December 14, 2005.

NF-IL6ß regulates gene expression and plays function roles in many tissues. The EGF-regulated cyclooxygenase-2 (cox-2) expression is mediated through p38MAPK signaling pathway and positively correlates with NF-IL6ß expression in A431 cells. NF-IL6ß coordinated with c-Jun on cox-2 transcriptional activation by reporter and small interfering RNA assays. NF-IL6ß could directly bind to CCAAT/enhancer-binding protein (C/EBP) and cyclic AMP-response element (CRE) sites of the cox-2 promoter by in vitro-DNA binding assay. The C/EBP site was important for basal and, to a lesser extent, for EGF-regulated cox-2 transcription, while the CRE site was a more specific response to EGF inducibility of cox-2 gene. SUMO1 expression attenuated EGF- and NF-IL6ß-induced cox-2 promoter activities. NF-IL6ß was found to be sumoylated by in vivo- and in vitro-sumoylation assays, and the SUMO1-NF-IL6ß (suNF-IL6ß) lost its ability to interact with p300 in in vitro-binding assay. NF-IL6ß was also acetylated by p300, and acetylation of NF-IL6ß enhanced the cox-2 promoter activity stimulated by NF-IL6ß itself. In vivo-DNA binding assay demonstrated that EGF stimulated the recruitment of p300 and NF-IL6ß to the cox-2 promoter, yet promoted the dissociation of SUMO1-modificated proteins from the promoter. These results indicated that NF-IL6ß plays a pivotal role in the regulation of basal and EGF-induced cox-2 transcription.


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