Abstract |
Cell lysates from cultured human alveolar macrophages contain detectable amounts of an elastinolytic enzyme. Although particulate elastin was solubilized only after prolonged incubations, lysates readily hydrolyzed T-OC-alanyl- p-nitrophenol- ester. Hydrolysis of the latter substrate was inhibited by the leukocyte elastase site-specific inhibitor, N-ac-(ala)4-chloromethyl ketone. In addition, radioimmunoelectrophoresis of concentrated alveolar macrophage lysates, previously incubated with 3H diisopropyl-phosphofluoridate ( DFP), revealed the presence of DFP binding material that comigrated with inactivated human leukocyte elastase. Human leukocyte elastase can cause lung lesions resembling pulmonary emphysema in experimental animals; therefore, the clearance of this enzyme by alveolar macrophages may represent a significant route for the removal of this potentially pathogenic enzyme from the lung.
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Authors | R White, A Janoff, R Gordon, E Campbell |
Journal | The American review of respiratory disease
(Am Rev Respir Dis)
Vol. 125
Issue 6
Pg. 779-81
(Jun 1982)
ISSN: 0003-0805 [Print] United States |
PMID | 6920250
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
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Topics |
- Cells, Cultured
- Humans
- Leukocytes
(enzymology)
- Macrophages
(enzymology)
- Pancreatic Elastase
(metabolism)
- Pulmonary Alveoli
(cytology)
- Smoking
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