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Papers In Press, published online ahead of print December 5, 2003
J. Biol. Chem, 10.1074/jbc.M306267200
Submitted on June 13, 2003
Revised on December 3, 2003
Accepted on December 5, 2003

Transcriptional regulation of cyclooxygenase-2 gene in macrophages by PU.1

Myungsoo Joo, Gye Young Park, Jeffrey G. Wright, Timothy S. Blackwell, Michael L. Atchison, and John W. Christman

Department of Allergy, Pulmonary and Critical Care Medicine, Vanderbilt University Medical Center, Nashville, TN 37232-2650

Corresponding Author: john.christman{at}vanderbilt.edu

Macrophages are an abundant source of COX-2 enzymatic products, but a specific mechanism for macrophage COX-2 gene expression has not been described. We examined whether PU.1, a myeloid specific Ets family transcription factor, is involved. Sequence analysis revealed two potential c-Ets binding sites in the COX-2 promoter (COX-2p) that bind to immunoreactive PU.1. Chromatin immunoprecipitation (ChIP) analysis shows inducible PU.1 binding to these sites in response to LPS, and COX-2 protein production is augmented by ectopic expression of PU.1 but not by PU.1S148A, indicating that PU.1 phosphorylation is likely involved. Interestingly, expression of PU.1 results in acetylation of C/EBP-ß and increased production of COX-2 protein. Co-immunoprecipitation experiments suggest a role for p300 in C/EBP-ß acetylation and COX-2 expression. In contrast, E1A inhibits acetylation of C/EBP-ß and is correlated with decreased COX-2 expression. Together, these data suggest that PU.1 is activated by phosphorylation of Ser148 in response to LPS treatment and subsequently binds to sequences in the endogenous COX-2p in a time-dependent manner. Concomitantly, C/EBP-ß becomes acetylated and expression of the COX-2 gene increases. We speculate that a combinatorial role of PU.1 and C/EBP-ß mediates the robust production of COX-2 products by macrophages that occurs in gram negative bacterial sepsis.


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