Protease and elastase of Pseudomonas aeruginosa: inactivation of human plasma alpha 1-proteinase inhibitor

Abstract

The present study indicates that crystalline elastase of Pseudomonas aeruginosa is a very potent inactivator of human plasma alpha 1-proteinase inhibitor, the enzyme (E) inactivated the inhibitor (I) almost completely within 1 h at 25 degrees C at a molar ratio of E/I = 1:100. The crystalline P. aeruginosa protease also inactivated the inhibitor, but 100-fold less. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that the alpha 1-proteinase inhibitor inactivated by the elastase and protease showed decreases in molecular weight of approximately 5,000 and 10,000, respectively. Regeneration of trypsin was negligible even when bovine trypsin-alpha 1-proteinase inhibitor complex (E/I = 1.0) was treated with the elastase. The affinity of alpha 1-proteinase inhibitor to trypsin was much higher than that to elastase. It was suggested that, assuming the pseudomonal proteases are produced and can inactivate alpha 1-proteinase inhibitor in vivo during pseudomonal diseases, the loss of alpha 1-proteinase inhibitor activity may permit the endogenous serine proteases to cause tissue destruction.