Inhibitory properties of recombinant human monocyte/neutrophil elastase inhibitor
| Autor: | Eileen Remold-O'Donnell, Jessica Cooley, T Sugimori, John R. Hoidal |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Pulmonary and Respiratory Medicine
Proteases Insecta Neutrophils Clinical Biochemistry Biology Serpin Monocytes law.invention Substrate Specificity law Proteinase 3 medicine Animals Humans Enzyme Inhibitors Molecular Biology Pancreatic elastase Cells Cultured Cathepsin Pancreatic Elastase Monocyte Cell Biology Molecular biology Recombinant Proteins medicine.anatomical_structure Biochemistry Neutrophil elastase Recombinant DNA biology.protein Leukocyte Elastase |
| Zdroj: | American journal of respiratory cell and molecular biology. 13(3) |
| ISSN: | 1044-1549 |
| Popis: | Human monocyte/neutrophil elastase inhibitor (HEI) is a serpin superfamily protein that rapidly and irreversibly inhibits neutrophil and pancreatic elastase. We generated a recombinant baculovirus that supports production of HEI in insect cells at approximately 400 times the level in monocytes. Recombinant HEI was found to be indistinguishable from monocyte HEI in its physicochemical properties and ability to inhibit neutrophil elastase and pancreatic elastase. The recombinant protein was used to test for additional functions. HEI was shown to inhibit proteinase 3, an important neutrophil inflammatory protease, by the classical serpin mechanism of forming a covalent protease-protease inhibitor complex. Preliminary evidence suggests that HEI also inhibits neutrophil cathepsin G. On the other hand, HEI does not inhibit u-plasminogen activator (urokinase). These findings suggest that HEI functions as a class-specific regulator of the neutrophil serine proteases characteristically found at inflammatory sites. |
| Databáze: | OpenAIRE |
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