ABSTRACT
Reteplase is a novel recombinant plasminogen activator consisting of the kringle 2 and protease
domains of tissue-type plasminogen activator (t-PA). Because of its production in Escherichia
coli cells, reteplase is not glycosylated. As shown experimentally, consequences of the structural
changes are a virtual lack of functional fibrin binding and a lower affinity to endothelial cells and
liver cells, resulting in a longer half-life. The longer half-life of reteplase compared with t-PA has
an influence on pharmacodynamic characteristics: It contributes to the higher thrombolytic
potency, allowing dose reduction, and it enables intravenous-bolus injection, which is associated
with more rapid reperfusion than after administration of reference thrombolytic agents. The
double-bolus regimen of reteplase stabilizes coronary artery blood flow after successful
reperfusion. At equieffective doses, the degree of systemic lytic state after reteplase is
comparable with that after t-PA.
