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Papers In Press, published online ahead of print December 10, 2001
Internal Medicine-Hematology, University of Texas-Houston Medical School, Houston, TX 77030-1503
Corresponding Author: Kenneth.K.Wu{at}uth.tmc.edu
To elucidate the mechanism by which isoforms of CCAAT/enhancer binding proteins regulate cyclooxygenase-2 expression, we determined by a novel technique binding of six isoforms of this transactivator to two sequence-specific CCAAT/enhancer binding protein (-132/-125) and cyclic AMP (-59/-53) regulatory elements in human foreskin fibroblasts treated with phorbol 12-myristate 13-acetate for 4 h. The
J. Biol. Chem, 10.1074/jbc.M108075200
Submitted on August 22, 2001
Revised on November 5, 2001
Accepted on December 8, 2001
Dynamic regulation of cyclooxygenase-2 promoter activity by isoforms of CCAAT/ehancer binding proteins
isoform bound to these two elements at basal state which was displaced by full-length as well as two truncated 
isoforms, a 41 kDa liver-enriched activating protein and a 16 kDa liver-enriched inhibitory protein after phorbol ester stimulation. Kinetic analysis shows time-dependent changes in and binding which were concordant with time-dependent increase in cyclooxygenase-2 induction. Overexpression of the 16 kDa isoform blocked the promoter activity and protein level induced by phorbol ester. Paradoxically, it increased binding of isoforms to the sequence-specific promoter DNA but suppressed cyclooxygenase-2 promoter activation by p300 cotransfection. These findings provide new insight into the regulation of cyclooxygenase-2 promoter by an interplay between two opposite isoforms and p300 coactivator.
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