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Vol. 282, Issue 3, 1658-1665, 1997
In Vitro and In Vivo
via the Cyclooxygenases1
Department of Pediatrics, Philipps University of Marburg, Marburg,
Germany
F2-Isoprostanes are isomers of the prostaglandin
PGF2
. At least one compound of this group,
8-epi-PGF2, exhibits biological activity, and therefore
special interest is focused on the mechanism of isoprostane formation:
enzyme catalyzed or radical mediated. We analyzed the formation of
isoprostanes in vitro and in vivo. In both
systems, purified cyclooxygenase isoenzymes and cell models specific
for the cyclooxygenase isoenzymes, 8-epi-PGF2 formation
could be totally suppressed by cyclooxygenase inhibitors. Indomethacin
inhibited concentration-dependent 8-epi-PGF2 formation
in platelets stimulated with calcium ionophore, arachidonic acid or
thrombin. Nordihydroguaiaretic acid, an antioxidant, blocked isoprostane formation with a similar IC50 value as
thromboxane B2 synthesis, pointing toward cyclooxygenase as
the primary target of inhibition. Based on the turnover number,
cyclooxygenase-2 formed higher levels of 8-epi-PGF2 than
cyclooxygenase-1. Endogenous 8-epi-PGF2 production in
rat mesangial cells correlated well with the mRNA and protein
expression of cyclooxygenase-2 during interleukin-1 induction. However,
in contrast to human platelets, which produced different forms of
isoprostanes, rat mesangial cells appeared to form only
8-epi-PGF2. Further, this indicates that mesangial cells
may represent a cellular origin for renal 8-epi-PGF2
formation. Next, we analyzed the formation of isoprostanes in humans. A
direct correlation was observed between indomethacin treatment and the
decrease in 8-epi-PGF2 and isoprostane levels, but
compared with other prostanoids the inhibition was less pronounced. In
summary, based on the in vitro studies, a clear
cyclooxygenase-dependent formation of isoprostanes, especially 8-epi-PGF2, was observed. However, in vivo
additional formation via cyclooxygenase enzyme-independent
mechanisms is likely.
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