α2-Plasmin Inhibitor Inactivation by Human Granulocyte Elastase

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Abstract
Plasminogen-binding human .alpha.2-plasmin inhibitor is converted by human granulocyte elastase into its non-plasminogen-binding and finally into the inactive form of the inhibitor. This degradation of the plasmin inhibitor, described earlier as spontaneously occurring conversion, is shown in dodecyl sulfate polyacrylamide gel electrophoresis, in 2-dimensional immunoelectrophoresis and by measuring the kinetics of plasmin inhibition. Experiments in the presence of normal human plasma required unphysiologically high concentrations of elastase to inactivate .alpha.2-plasmin inhibitor, suggesting a role of elastase in this type of indirect fibrinolysis in a microenvironment only and not in systemic events.