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An elastase-specific inhibitor from human bronchial mucus. Isolation and characterization.
Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie
|October 1, 1981
Summary
Human bronchial mucus contains two proteinase inhibitors. One inhibitor, BSI-ATE, targets multiple proteases, while the newly identified BSI-E specifically inhibits elastase. This elastase-specific inhibitor is found in patients with obstructive airway disease.
Area of Science:
- Biochemistry
- Pulmonary Medicine
Background:
- Human bronchial mucus contains acid-stable proteinase inhibitors.
- A known inhibitor, BSI-ATE, targets trypsin, chymotrypsin, polymorphonuclear granulocyte elastase, and cathepsin G.
Purpose of the Study:
- To characterize a second, elastase-specific inhibitor (BSI-E) in human bronchial mucus.
- To investigate the presence of BSI-E in patients with obstructive airway disease.
Main Methods:
- Isolation of BSI-E using affinity chromatography.
- Analysis of molecular mass and amino acid composition.
- Immunological cross-reactivity testing.
Main Results:
- BSI-E specifically inhibits porcine pancreatic and human granulocytic elastase, but not trypsin, chymotrypsin, or cathepsin G.
- BSI-E shares similarities in molecular mass and amino acid composition with BSI-ATE.
- No immunological cross-reactivity was observed between BSI-E and BSI-ATE.
- In obstructive airway disease patients, BSI-E is present in a bound form, liberated by acidification.
Conclusions:
- Human bronchial mucus contains at least two distinct acid-stable proteinase inhibitors.
- BSI-E is a novel elastase-specific inhibitor found in bronchial mucus.
- The altered form of BSI-E in obstructive airway disease warrants further investigation.