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(Received for publication, August 13, 1996, and in revised form, February 28, 1997)
From the Department of Pediatrics, Stanford University School of
Medicine, Stanford, California 94305 and the § Department of
Radiology, Cancer/Biology Section, Washington University, St. Louis,
Missouri 63108
The role of heme oxygenase (HO)-1 was evaluated
in the oxygen-resistant hamster fibroblast cell line,
O2R95, which moderately overexpress HO when compared
with the parental cell line, HA-1. To suppress HO-1 expression,
O2R95 were transfected with HO-1 antisense oligonucleotide
or treated with tin-mesoporphyrin (SnMP). To increase HO-1 expression,
cells were transfected with HO-1 cDNA in a pRC/cytomegalovirus
(CMV) vector. All cells were challenged with a 48-h exposure to 95%
O2 (hyperoxia). When HO activity was suppressed,
O2R95 cells had significantly decreased cell viability, increased susceptibility to lipid peroxidation, and increased protein
oxidation in hyperoxia. In contrast, further overexpression of HO-1 did
not improve resistance to oxygen toxicity. Antisense-transfected cells and SnMP-treated cells with lowered HO activity showed increased levels of cellular heme compared with controls. In the HO-1
cDNA-transfected O2R95 cells, cellular heme was
lowered compared with controls; however, cellular redox active iron
levels were increased. We conclude that HO mediates cytoprotection to
oxygen toxicity within a narrow range of expression. We speculate that
this protective effect may be mediated in part through increased
metabolism of the pro-oxidant heme but that higher levels of HO
activity obviate protection by increased redox active iron
release.
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