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Hyperoxic Lung Injury Increases HOCl-Modified Lung Proteins and NA,K-Adenosine Triphosphatase Nitrotyrosine Content*

David H. Ingbar, MD, FCCP; R. Bair; P. Jung; J. Heinecke; I.Y. Haddad, MD
Author and Funding Information

*From the Departments of Medicine and Pediatrics, University of Minnesota, Minneapolis, MN, and Department of Medicine, Washington University, St. Louis, MO. Supported by NIH SCOR in Acute Lung Injury HL50152 and an ALA Career Investigator Award.

Correspondence to: David H. Ingbar, MD, FCCP, University of Minnesota School of Medicine, 420 Delaware St SE, Box 276, Minneapolis, MN 55455



Chest. 1999;116(suppl_1):100S. doi:10.1378/chest.116.suppl_1.100S
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Extract

Hyperoxia causes lung injury due to increased oxidants and inflammation. We sought to assess whether oxidative modification of proteins occurred in this model of rat acute lung injury and to determine if specific membrane transport proteins were affected. Using antibodies to hypochlorous acid-modified low-density lipoprotein and tyrosine groups, western blotting revealed marked increases in specific protein bands at approximately 100 and 60 kd in rat lungs at 60 h of hyperoxic exposure. Using the former antibody for immunocytochemistry, there was little reactivity in normal lungs, but hyperoxia induced striking staining of airway and alveolar epithelium that persisted with only moderate decreases through 7 days of recovery. Since in prior data hyperoxia decreased the maximal enzyme velocity of type II cell Na,K-adenosine triphosphatase, we hypothesized that this was due to pump oxidation and assessed whether nitrotyrosine residues were present on this integral membrane protein from normoxic, hyperoxic, and recovering lungs. Using immunoprecipitation and then western blotting, the β1-subunit, but not the α1-subunit, had detectable nitrotyrosine even in normoxic lung. Hyperoxia led to a statistically significant, but small (approximately 30%), increase in nitrotyrosine of the sodium pump β1-subunit. This decreased rapidly during the recovery phase. These data indicate that during in vivo hyperoxia, newer oxidant species cause significant protein modification and suggest that important epithelial cell functional proteins can be affected.


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