Abstract
Destruction of components of the extracellular matrix of the lung by neutrophil elastase is believed to be a critical event in the development of obstructive lung disease. The local synthesis of alpha1-proteinase inhibitor, the controlling inhibitor of this enzyme, may provide a partial mechanism for neutrophil elastase regulation, especially during inflammation, when proteolytic enzymes are released from phagocytes. In this study, we show that lung-derived epithelial cells not only have the capacity to synthesize functional alpha1-PI but also to increase the rate of its production when stimulated by specific inflammatory mediators, including oncostatin M, interleukin-1, and the glucocorticoid analogue, dexamethasone.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Antineoplastic Agents / pharmacology
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Cell Line
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Dexamethasone / pharmacology
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Dose-Response Relationship, Drug
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Epithelium / drug effects
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Epithelium / metabolism
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Extracellular Matrix / drug effects
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Extracellular Matrix / metabolism
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Humans
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Inflammation Mediators / pharmacology*
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Interleukin-1 / pharmacology
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Interleukin-6 / pharmacology
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Liver / cytology
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Liver / metabolism
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Lung / cytology*
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Lung / drug effects
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Lung / metabolism
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Oncostatin M
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Peptides / pharmacology
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Serine Proteinase Inhibitors / biosynthesis*
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Trypsin Inhibitors / biosynthesis*
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Tumor Cells, Cultured
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alpha 1-Antitrypsin / biosynthesis*
Substances
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Antineoplastic Agents
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Inflammation Mediators
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Interleukin-1
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Interleukin-6
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OSM protein, human
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Peptides
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Serine Proteinase Inhibitors
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Trypsin Inhibitors
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alpha 1-Antitrypsin
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Oncostatin M
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Dexamethasone