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Am J Physiol Lung Cell Mol Physiol 276: L452-L458, 1999;
1040-0605/99 $5.00
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Vol. 276, Issue 3, L452-L458, March 1999

Localization of a candidate surfactant convertase to type II cells, macrophages, and surfactant subfractions

Howard Clark, Lennell Allen, Erin Collins, Frederick Barr, Leland Dobbs, Gunther Putz, Jon Goerke, and Samuel Hawgood

Cardiovascular Research Institute and Department of Pediatrics, University of California, San Francisco, California 94118-1245

Pulmonary surfactant exists in the alveolus in several distinct subtypes that differ in their morphology, composition, and surface activity. Experiments by others have implicated a serine hydrolase in the production of the inactive small vesicular subtype of surfactant (N. J. Gross and R. M. Schultz. Biochim. Biophys. Acta 1044: 222-230, 1990). Our laboratory recently identified this enzyme in the rat as the serine carboxylesterase ES-2 [F. Barr, H. Clark, and S. Hawgood. Am. J. Physiol. 274 (Lung Cell. Mol. Physiol. 18): L404-L410, 1998]. In the present study, we determined the cellular sites of expression of ES-2 in rat lung using a digoxygenin-labeled ES-2 riboprobe. ES-2 mRNA was localized to type II cells and alveolar macrophages but not to Clara cells. Using a specific ES-2 antibody, we determined the protein distribution of ES-2 in the lung by immunohistochemistry, and it was found to be consistent with the sites of mRNA expression. Most of the ES-2 in rat bronchoalveolar lavage is in the surfactant-depleted supernatant, but ES-2 was also consistently localized to the small vesicular surfactant subfraction presumed to form as a consequence of conversion activity. These results are consistent with a role for endogenous lung ES-2 in surfactant metabolism.

carboxylesterase; ES-2; diisopropyl fluorophosphate-binding protein


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Am J Physiol Lung Cell Mol Physiol, January 1, 2000; 278(1): L19 - L24.
[Abstract] [Full Text] [PDF]


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