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Characterization of thrombin derived from human recombinant prothrombin.

Ann Lövgren¹, Johanna Deinum, Steffen Rosén

¹aCVMD iMED, AstraZeneca R&D, Mölndal bRossix AB, Taljegårdsgatan 3B, Mölndal, Sweden.

Blood Coagulation & Fibrinolysis : an International Journal in Haemostasis and Thrombosis

|March 27, 2015

Summary

Recombinant human prothrombin (rhFII) forms thrombin (FIIa) with properties very similar to plasma-derived thrombin. Minor differences in Factor V activation and antithrombin inhibition were observed, but rhFIIa is likely functionally equivalent for therapeutic use.

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Area of Science:

Biochemistry
Hematology
Biotechnology

Background:

Thrombin (FIIa) is central to hemostasis, regulating clot formation and platelet activation.
Understanding the properties of recombinant human prothrombin (rhFII)-derived thrombin is crucial for its therapeutic application.
Endogenous thrombin is formed via prothrombin (FII) cleavage during coagulation.

Purpose of the Study:

To compare the enzymatic and hemostatic properties of thrombin derived from recombinant human prothrombin (rhFIIa) versus plasma-derived human FII (pdhFIIa).
To assess the functional similarity of rhFIIa and pdhFIIa in various coagulation substrates and settings.
To evaluate potential differences in substrate activation, enzyme kinetics, and inhibition by antithrombin.

Main Methods:

Isolation of pure FIIa from rhFII and pdhFII following cleavage by recombinant ecarin.
Development of analytical methods to compare FIIa activity against multiple substrates.
Assessment of FIIa-mediated activation of FVIII, FXIII, protein C, platelet aggregation, and coagulation in plasma and whole blood.

Main Results:

FIIa from rhFII and pdhFII demonstrated highly similar activation of FVIII, FXIII, protein C, platelet aggregation, and plasma/whole blood coagulation.
Similar turnover rates and Michaelis constants (KM) were observed for the S-2366 substrate.
rhFIIa showed ~25% greater efficacy in activating Factor V (FV) and significantly more efficient heparin-enhanced inhibition by antithrombin compared to pdhFIIa.

Conclusions:

Thrombin derived from recombinant human prothrombin (rhFIIa) exhibits largely comparable enzymatic and hemostatic properties to plasma-derived thrombin (pdhFIIa).
Observed differences in FV activation and antithrombin inhibition suggest distinct kinetic profiles but do not negate functional similarity.
rhFIIa is expected to possess very similar activity and function to endogenous thrombin when administered to humans, supporting its therapeutic potential.