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J Biol Chem, Vol. 274, Issue 17, 11660-11666, April 23, 1999
From the Division of Pulmonary and Critical Care Medicine,
University of Michigan Medical Center, Ann Arbor, Michigan 48109
The two cyclooxygenase isoforms, cyclooxygenase-1
and cyclooxygenase-2, both metabolize arachidonic acid to prostaglandin H2, which is subsequently processed by downstream
enzymes to the various prostanoids. In the present study, we asked if
the two isoforms differ in the profile of prostanoids that ultimately arise from their action on arachidonic acid. Resident peritoneal macrophages contained only cyclooxygenase-1 and synthesized (from either endogenous or exogenous arachidonic acid) a balance of four
major prostanoids: prostacyclin, thromboxane A2,
prostaglandin D2, and 12-hydroxyheptadecatrienoic acid.
Prostaglandin E2 was a minor fifth product, although these
cells efficiently converted exogenous prostaglandin H2 to
prostaglandin E2. By contrast, induction of
cyclooxygenase-2 with lipopol- ysaccharide resulted in the preferential
production of prostacyclin and prostaglandin E2. This shift
in product profile was accentuated if cyclooxygenase-1 was permanently
inactivated with aspirin before cyclooxygenase-2 induction. The
conversion of exogenous prostaglandin H2 to prostaglandin E2 was only modestly increased by lipopolysaccharide
treatment. Thus, cyclooxygenase-2 induction leads to a shift in
arachidonic acid metabolism from the production of several prostanoids
with diverse effects as mediated by cyclooxygenase-1 to the
preferential synthesis of two prostanoids, prostacyclin and
prostaglandin E2, which evoke common effects at the
cellular level.
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