Abstract
The discovery of protein C and its effects upon blood coagulation, fibrinolysis, and inflammation has changed the way we now think about the pathophysiology of thromboembolic disease and related disorders. Interestingly, this discovery was not the result of a planned approach to understanding a disease, but rather from a basic approach of attempting to understand the biochemistry of the vitamin K-dependent family of proteins. In fact all of the clinical information about protein C stems from information obtained in basic research laboratories. The first clue of the existence of protein C can be found in a 1947 paper that reports that factor Va is unstable in serum (1). It was subsequently observed that the instability could be removed if the plasma was adsorbed with aluminum hydroxide, an insoluble support that was known to adsorb vitamin K-dependent proteins. Seegers group observed that treatment of prothrombin with thrombin could elicit an inhibitor of coagulation. This led to the inhibitor’s characterization and designation as autoprothrombin IIa (2). Marciniak (3) confirmed the observation and noted that the inhibitor was species specific. Some time later, Stenflo characterized a new vitamin K-dependent protein (4), named protein C (5) which turned out to be the zymogen of autoprothrombin IIa (6). Characterization of protein C and the discovery that activated protein C was a potent inhibitor of blood coagulation lead to the realization that protein C may be one of the keys to understanding the molecular basis of thrombotic disease. This paper describes structural properties that give rise both to its unique functional — properties as well as the complex scheme by which it is regulated.
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References
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© 1991 Springer Science+Business Media New York
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Walker, F.J. (1991). Structural and Functional Properties of Protein C. In: Hoyer, L.W., Drohan, W.N. (eds) Recombinant Technology in Hemostasis and Thrombosis. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3698-7_6
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DOI: https://doi.org/10.1007/978-1-4615-3698-7_6
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