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Related Experiment Videos

Expression of functionally active human antithrombin III.

A W Stephens, A Siddiqui, C H Hirs

    Proceedings of the National Academy of Sciences of the United States of America
    |June 1, 1987
    PubMed
    Summary
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    Researchers successfully produced functional human antithrombin III in COS cells. This recombinant protein demonstrates effective thrombin inhibition, comparable to plasma-derived antithrombin III, with and without heparin.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Recombinant Protein Expression

    Background:

    • Antithrombin III is a critical inhibitor of coagulation proteases.
    • Efficient production of functional antithrombin III is essential for therapeutic applications.

    Purpose of the Study:

    • To clone and express human antithrombin III (ATIII) in COS cells.
    • To characterize the secreted ATIII for its functional activity and heparin binding.

    Main Methods:

    • cDNA cloning into an expression vector for COS cell transfection.
    • Quantification of secreted ATIII using ELISA.
    • Heparin-agarose chromatography for assessing heparin binding.
    • Assays to evaluate thrombin inhibition activity.

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    Main Results:

    • COS cells secreted a 58-kDa immunoreactive protein.
    • Secretion levels reached 48 +/- 5 ng/10(6) cells/24 hr.
    • The protein bound to heparin-agarose, eluting between 0.3-1.0 M NaCl.
    • COS cell-derived ATIII formed stoichiometric complexes with thrombin.
    • Functional assays showed comparable thrombin inactivation rates to plasma ATIII, with enhanced activity in the presence of heparin.

    Conclusions:

    • COS cells can be utilized for the efficient expression of functional human antithrombin III.
    • The recombinant ATIII exhibits heparin-dependent and independent thrombin inhibition.
    • This expression system offers a viable method for producing therapeutic antithrombin III.