Retavase Reteplase recombinant - Rapid Reperfusion With Fixed Dosing For the Way You Treat AMI Today Retavase Flows With You™
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Retavase and Alteplase Differ in Vitro
Molecular structure distinguishes Retavase among plasminogen activators
Molecular structure distinguishes Retavase among plasminogen activators
Retavase consists of the protease and kringle 2 domains of human tissue plasminogen activator, which are associated with fibrin specificity and low fibrin-binding affinity, respectively1–3
Retavase lacks the fibronectin-like finger domain of alteplase that promotes high fibrin-binding affinity2
These differences affect interactions with fibrin and may explain the in vitro clot penetration observed with Retavase2,4
Significant difference in lysis of aged clots (24 hours old) in vitro
Retavase Retavase achieved significantly lower maximal lysis rates of aged clots than alteplase
Retavase achieved significantly lower maximal lysis rates of aged clots than alteplase (p<0.05)3
Penetration throughout the clot demonstrated in vitro
photo
photo
Retavase Penetration throughout the clot demonstrated in vitro
Difference in color illustrates difference
in fibrin interaction.
Penetration was observed by applying increasing concentrations of Retavase and alteplase to 1 mL of plasma clot. The plasminogen activators inside the clot were determined by immunostaining.4
Retavase facilitates in vitro clot penetration and a homogenous distribution inside the clot because it does not bind completely to fibrin
Retavase facilitates in vitro clot penetration and a homogenous distribution inside the clot because it does not bind completely to fibrin4
Alteplase is unable to penetrate or activate the plasminogen inside the clot in vitro because it binds tightly to the surface of the clot
Alteplase is unable to penetrate or activate the plasminogen inside the clot in vitro because it binds tightly to the surface of the clot4
The relationship between clinical efficacy and the high fibrin specificity, lower fibrin-binding affinity, and activation of plasminogen at the interior of the thrombus by Retavase has not been established. The differences noted are derived from a single study and are not indicative of comparative clinical efficacy or safety.
Important Safety Information
Because thrombolytic therapy increases the risk of bleeding, including internal bleeding (such as intracranial, retroperitoneal, gastrointestinal, genitourinary, or respiratory), Retavase should be used only in those patients for whom its use is indicated in the prescribing information (see "Indications" in the prescribing information). In addition, thrombolytic therapy increases the absolute risk of stroke, including hemorrhagic stroke, in patients of advanced age. Cholesterol embolism has been reported rarely in patients treated with thrombolytic agents. Coronary thrombolysis may result in arrhythmias associated with reperfusion (see "Warnings" in the prescribing information).
References: 1. Van de Werf FJ. The ideal fibrinolytic: can drug design improve clinical results? Eur Heart J. 1999;20:1452–1458. 2. Weaver WD. The role of thrombolytic drugs in the management of myocardial infarction: comparative clinical trials. Eur Heart J. 1996;17(suppl F):9–15. 3. Martin U, Sponer G, Strein K. Differential fibrinolytic properties of the recombinant plasminogen activator BM 06.022 in human plasma and blood clot systems in vitro. Blood Coagul Fibrinolysis. 1993;4:235–242. 4. Fischer S, Kohnert U. Major mechanistic differences explain the higher clot lysis potency of reteplase over alteplase: lack of fibrin binding is an advantage for bolus application of fibrin-specific thrombolytics. Fibrinolysis & Proteolysis. 1997;11:129–135.
Please see full prescribing information.
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© EKR Therapeutics, Inc. All rights reserved. January 2010.