What is the mechanism of action for reteplase in thrombolytic therapy?

Updated: Dec 31, 2017
  • Author: Wanda L Rivera-Bou, MD, FAAEM, FACEP; Chief Editor: Erik D Schraga, MD  more...
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Answer

Answer

Reteplase is a second-generation recombinant tissue-type plasminogen activator that seems to work more rapidly and to have a lower bleeding risk than the first-generation agent alteplase. It is a synthetic nonglycosylated deletion mutein of tPA that contains 355 of the 527 amino acids of native tPA. The drug is produced in Escherichia coli by means of recombinant DNA techniques. [6]

Because reteplase does not bind fibrin as tightly as native tPA does, it can diffuse more freely through the clot rather than bind only to the surface as tPA does. At high concentrations, reteplase does not compete with plasminogen for fibrin-binding sites, allowing plasminogen at the site of the clot to be transformed into clot-dissolving plasmin. These characteristics help explain why clots resolve faster in patients receiving reteplase than in those receiving alteplase.

The biochemical modifications also resulted in a molecule with a longer half-life (~13-16 minutes), which allows bolus administration. Reteplase is FDA-approved for AMI and is administered as two boluses of 10 U given 30 minutes apart, with each bolus administered over 2 minutes. [6] The result is more convenient administration and faster thrombolysis with reteplase than with alteplase, which is given in a bolus followed by intravenous (IV) infusion.

Like alteplase, reteplase may be readministered as necessary; it is not antigenic and almost never is associated with any allergic manifestations.


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