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Vol. 290, Issue 3, 1250-1257, September 1999
Dependent1
Department of Pharmacology, Emory University, Atlanta, Georgia
(T.B.B., M.B.S., L.F., E.T.M.); Laboratory of Metabolism, National
Cancer Institute, National Institutes of Health, Bethesda, Maryland
(J.M.P., F.J.G.); and Centre du Medicament, Université de Nancy
I, Nancy, France (L.F.)
Administration of the bacterial endotoxin lipopolysaccharide (LPS)
causes induction of cytochrome P-450 (CYP) 4A mRNAs in rat liver
and kidney. Because induction of the CYP4A subfamily by chemicals
requires peroxisome proliferator-activated receptor-
(PPAR), we
determined whether CYP4A induction by LPS also requires PPAR by
comparing the responses of PPAR-null (
/) and wild-type (+/+)
mice. Renal expression of CYP4A10, CYP4A14, and acyl-CoA oxidase was
induced by LPS treatment in (+/+) mice, and these effects were absent
in the (/) mice. In contrast, hepatic expression of CYP4A10 was
down-regulated in the (+/+) animals, and no significant induction of
acyl-CoA oxidase or CYP4A14 was detected in liver. Expression of the
peroxisomal bifunctional enzyme was not significantly affected by LPS
treatment. These results indicate that PPAR is activated in mouse
kidney after LPS treatment and that this leads to modulation of some
PPAR-regulated genes. However, the species and tissue specificity of
these effects suggest that inflammatory pathways may modulate the
induction via PPAR. Mice pair fed with LPS-treated mice showed no
induction of renal CYP4A10 or CYP4A14, indicating that renal CYP4A
induction during endotoxemia is not due to hypophagia. Down-regulation
of CYP2A5, CYP2C29, and CYP3A11 by LPS was attenuated or blocked in the
(/) mice, suggesting a role for PPAR in CYP
down-regulation as well. Finally, we found that clofibrate caused an
acute induction of two hepatic acute-phase mRNAs that was only
partially dependent on PPAR.
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