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Serine antiproteinase administration preserves innate superoxide dismutase levels after acid aspiration and hyperoxia
Nader D Nader1, Bruce A Davidson, Alan R Tait
1Department of Anesthesiology, State University of New York at Buffalo, Buffalo, NY 14215, USA. nnader@buffalo.edu
Anesthesia and Analgesia
|June 25, 2005
Summary
Serine proteinases degrade lung antioxidants like copper/zinc superoxide dismutase (SOD) after acid aspiration. Inhibiting these enzymes protected SOD but did not reduce lung injury severity.
Area of Science:
- Pulmonary Medicine
- Biochemistry
- Toxicology
Background:
- Acute lung injury (ALI) involves oxidative damage and reduced lung antioxidants.
- Increased serine proteinase activity in airways suggests a role in antioxidant degradation.
Purpose of the Study:
- To investigate the role of serine proteinases in degrading lung antioxidants during ALI.
- To assess the impact of serine proteinase inhibition on lung antioxidant levels and ALI severity.
Main Methods:
- Rats underwent acid aspiration with hyperoxia, with some pretreated with a serine proteinase inhibitor (aprotinin).
- Assayed lung superoxide dismutase (SOD) activity and protein levels (Cu/Zn SOD, Mn SOD).
- Evaluated ALI severity using albumin leakage, blood gases, and inflammatory markers.
Main Results:
- Acid aspiration and hyperoxia decreased total SOD and Cu/Zn SOD levels.
- Serine proteinase inhibition attenuated the decrease in Cu/Zn SOD.
- Mn SOD activity remained unchanged.
- Antiproteinase treatment did not significantly reduce ALI markers.
Conclusions:
- Serine proteinases contribute to the degradation of Cu/Zn SOD, reducing pulmonary antioxidant capacity.
- The direct role of this antioxidant degradation in ALI pathogenesis remains unclear.