Biochemical and Functional Characterization of LIZ, a Marine-Derived Serine Protease That Degrades Cross-Linked Fibrin and Attenuates Experimental Thrombosis

Background/Objectives: Direct fibrin-degrading proteases may provide a mechanistically distinct approach to clot proteolysis, but their development requires definition of catalytic behavior, fibrin selectivity, molecular identity, and safety. We characterized an activity-containing preparation from the marine polychaete Lepidasthenia izukai, designated LIZ.

Methods

LIZ was obtained by ammonium sulfate fractionation and sequential chromatography. N-terminal sequencing, inhibitor profiling, chromogenic-substrate screening and S-2288 kinetics, fibrinogenolysis, direct fibrin-degradation assays, a κ-carrageenan rat-tail thrombosis model, and cell viability were evaluated.