Abstract
Administration of bacterial endotoxin to rats exposed to greater than 95% O2 results in increased lung superoxide dismutase activity, decreased O2-induced lung damage, and a 3- to 4-fold improvement in survival rate (Frank, L., Yam, J., and Roberts, R. J. (1978) J. Clin. Invest, 61, 269-275). Antibodies to rat liver (Cu,Zn) superoxide dismutase were prepared and utilized to investigate the mechanism by which endotoxin treatment leads to increased lung superoxide dismutase activity. Assay of enzyme activity and of immunodetectable enzyme showed that the increased activity is due to an increase in the number of enzyme molecules rather than activation of existing enzyme. Compared to air controls, lung slices from rats exposed to greater than 95% O2 and treated with endotoxin have elevated rats of synthesis of (Cu,Zn)superoxide dismutase (51%) and of total protein (100%). Lung slices from untreated rats exposed to greater than 95% O2 have no such elevations. Endotoxin treatment thus appears to stimulate lung protein synthesis, leading to greater (Cu,Zn)superoxide dismutase activity due to an increased number of enzyme molecules.
Highlights
RESULTSBy reducing 0 2 - to less reactive speciesaccording following reaction:. + + 2H’ 202- + HZ02 0 2
Mutase were prepared and utilized to investigate the When neonatal rats areexposed to >95% 02,the pulmonary mechanism by which endotoxin treatment leads to increased lung superoxide dismutase activity
Treatment of adult rats with a withendotoxinhave elevated rates of synthesis of single, low dose of bacterial endotoxin at the starot f hyperoxic (Cu,Zn)superoxide dismutase (51%) andtootaf l protein exposurealso results in elevated levels of lung antioxidant
Summary
By reducing 0 2 - to less reactive speciesaccording following reaction:. + + 2H’ 202- + HZ02 0 2. Immunological Studies-Ouchterlony double immunodiffusion of goat antiserum and pure lriavter (Cu,Zn)superoxide dismutase produceda single precipitinline(Fig. 1). No cross-reaction was observed with bovine erythrocyte(Cu,Zn) superoxide dismutase. This articlemusttherefore be hereby Miniprint is read with the aid of a standard magnifying glass. Full size photocopies are included in the microfilm edition of the Journal thaits available from Waverly Press. Rat LuDnigsmSuutpaesreoxide (bottom) showed that this line co-migrated with (Cu,Zn) SU- increased level of (Cu,Zn) superoxide dismutase only in the peroxide dismutase.
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