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Am J Physiol Lung Cell Mol Physiol 263: L679-L691, 1992;
1040-0605/92 $5.00
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AJP - Lung Cellular and Molecular Physiology, Vol 263, Issue 6 679-L691, Copyright © 1992 by American Physiological Society

ARTICLES

Immunolocalization of antioxidant enzymes and isozymes of glutathione S-transferase in normal rat lung

D. B. Coursin, H. P. Cihla, T. D. Oberley and L. W. Oberley
Department of Anesthesiology, School of Medicine, University of Wisconsin, Madison.

Polyclonal antisera to manganese and copper-zinc superoxide dismutases, catalase, glutathione peroxidase (GPx), and isozymes of glutathione S-transferase (liver and placental isolates, GST-L and GST-P, respectively) were used to localize these enzymes in normal rat lung by immunostaining. Light-microscopic results, using an immunoperoxidase technique, were expanded on by electron-microscopic immunogold localization. The findings were consistent with previous biochemical work. However, both GPx and GST-P were predominantly localized to extracellular connective tissue of the lung. These findings demonstrate the basal antioxidant enzyme phenotypes for parenchymal lung tissue at light- and electron-microscopic levels. Significant components of enzymatic defense to oxidant stress are heterogeneously distributed throughout rat lung tissue including both epithelial cell surfaces and the extracellular matrix.


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