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and interleukin-1 on
heme oxygenase-1 expression in human endothelial cells
Department of Pharmacology and Toxicology, The Veterans Affairs Medical Center and the Department of Internal Medicine, University of Utah, Salt Lake City, Utah 84112
Heme iron exacerbates oxidant damage by
catalyzing the production of free radicals. Heme oxygenase is the
rate-limiting enzyme involved in heme catabolism. An inducible form of
heme oxygenase, heme oxygenase-1 (HO-1), is upregulated in oxidant and
inflammatory settings, and recent work suggests that HO-1 induction may
serve a protective function against oxidant injury. The ability of the endogenous inflammatory mediators, interleukin (IL)-1
, tumor necrosis factor- (TNF-), and IL-6, to enhance HO-1 expression in
cultured human endothelial cells was examined in this study. HO-1 mRNA
and protein expression were upregulated by IL-1 and TNF- exposure
but not by IL-6. Induction of HO-1 mRNA by IL-1 and TNF- occurred
in a concentration- and time-dependent fashion, with maximal expression
occurring by 4 h for both cytokines. Induction depended on protein
synthesis and occurred at the transcriptional level. Inhibition of the
AP-1 transcription factor with curcumin decreased the cytokine
induction of HO-1 mRNA, suggesting the involvement of this
transcription factor in cytokine signaling of HO-1. The results of this
study indicate that the endogenous inflammatory cytokines IL-1 and
TNF- induce HO-1 in endothelial cells, providing further evidence
that HO-1 may be an important cellular response to inflammatory stress.
cytokine; inflammation; heme oxygenase
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