<I>The role of the protease-protease-inhibitor complexes</I>
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概要
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It is well known that at the site of inflammation neutrophils release proteolytic enzymes which cause tissue damage.<BR>These proteases combine with protease inhibitors such as α<SUB>1</SUB>-antitrypsin and α<SUB>2</SUB>-macroglobulins and lose their biological activity. We examined the fate of these proteaseprotease inhibitor complexes, α<SUB>1</SUB>-antitrypsin was used as a protease inhibitor and purified by passing through the blue sepharose and sephadex columns. Trypsin was used as a proteolytic enzyme and mixed with purified α<SUB>1</SUB>-antitrypsin at 37°C to make a proteaseprotease inhibitor complex. This complex was separated from native α<SUB>1</SUB>-antitrypsin by isoelectric focusing and then incubated with normal human neutrophils.<BR>Significant lysosomal enzyme release was seen when neutrophils were incubated with this protease-protease inhibitor complex, but such enzyme release was not observed when neutrophils were incubated with native α<SUB>1</SUB>-antitrypsin or trypsin.<BR>The amount of lysosomal enzyme release was proportional to the amount of complex added. From these result we presume that this complex can promote the further protease release from the cells and worsen the in flammation.
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