Serpins in Fasciola hepatica: insights into host–parasite interactions

The authors of the publication below utilized human cathepsin Ghuman tissue plasminogen activator, >85% single chain, and active mouse urokinase, HMW from Molecular Innovations.


“We characterized four serpins from the liver fluke Fasciola hepatica. Biochemical characterization revealed that recombinant FhS-2 inhibits the activity of human neutrophil cathepsin G, while recombinant FhS-4 inhibits the activity of bovine pancreatic chymotrypsin and cathepsin G. Consistent with inhibitor function profiling data, FhS-4 inhibited cathepsin G-activated platelet aggregation in a dose-responsive manner.”

A variety of proteases including cathepsin G, tPA, and uPA were incubated with a molar excess of recombinant F. hepatica serpins followed by measurement of residual protease activity using enzyme appropriate chromogenic substrates. Cathepsin G was preincubated with recombinant FhS-4 before addition to bovine platelet rich plasma for platelet aggregation assays.


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