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1 Department of Pediatrics, Stanford University School of Medicine, Stanford, California 94304; 2 Department of Pediatrics, Baylor College of Medicine, Houston, Texas 77030; and 3 Department of Pediatrics, Ohio State University, Columbus, Ohio 43210
Rat fetal lung
cells (RFL-6) were transiently transfected with a full-length rat heme
oxygenase (HO)-1 cDNA construct and then exposed to hyperoxia (95%
O2-5%
CO2) for 48 h. Total HO activity and HO-1 protein were measured as well as cell viability, lactate dehydrogenase (LDH) release, protein oxidation, lipid peroxidation, and
total glutathione to measure oxidative injury. HO-1 overexpression resulted in increased total HO activity (2-fold), increased HO-1 protein (1.5-fold), and increased cell proliferation.
Immunohistochemistry revealed perinuclear HO-1 localization, followed
by migration to the nucleus by day 3.
Decreased cell death, protein oxidation, and lipid peroxidation but
increased LDH release and glutathione depletion were seen with HO-1
overexpression. Reactive iron content could not explain the apparent
loss of cell membrane integrity. With the addition of tin
mesoporphyrin, total HO activity was decreased and all changes in
injury parameters were normalized to control values. We conclude that
moderate overexpression of HO-1 is protective against oxidative injury,
but we speculate that there is a beneficial threshold of HO-1 expression.
heme oxygenase-1; antioxidant; oxidative stress; cell proliferation; nuclear protein
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