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Vol. 288, Issue 3, 1235-1241, March 1999
Instituto de Bioquímica, Facultad de Farmacia, Universidad
Complutense, Madrid, Spain
Primary cultures of fetal hepatocytes expressed cyclooxygenase-2
(COX-2) upon stimulation with bacterial lipopolysaccharide (LPS) or
peroxisomal proliferators. This enzyme was active and a good
correlation between the mRNA levels, the amount of protein, and the
synthesis of prostaglandin E2 was observed. However, when cells were incubated in the presence of indomethacin or the
COX-2-specific inhibitor NS398, the amount of COX-2 protein increased
5-fold after activation with LPS and 2-fold after treatment with
clofibrate. This up-regulation of COX-2 was not observed at the mRNA
level. The mechanism of protein accumulation might involve either a
direct stabilization of the enzyme by the inhibitors or the absence of prostaglandins involved in the regulation of its turnover. Among the
prostaglandins assayed, only 15-deoxy-Prostaglandin
J2 exerted a statistically significant decrease in
the COX-2 levels in cells stimulated with LPS or LPS plus NS398. The
accumulation of COX-2 in the presence of inhibitors was also observed
in peritoneal macrophages treated under identical conditions. These
results indicate that COX-2 protein accumulates after enzyme
inhibition, and because removal of the inhibitors restored the enzyme
activity, suppression of treatment with reversible COX-2 inhibitors may cause a transient overproduction of prostaglandins.
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