Human tissue plasminogen activator, purified, glycosylated, 355 residues purified from CHO cells. Retavase is considered a "third-generation" thrombolytic agent, genetically engineered to retain and delete certain portions of human tPA. Retavase is a deletion mutein of human tPA formed by deleting various amino acids present in endogenous human tPA. Retavase contains 355 of the 527 amino acids of native human tPA (amino acids 1-3 and 176-527), and retains the activity-related kringle-2 and serine protease domains of human tPA. Three domains are deleted from retavase - kringle-1, finger, and epidermal growth factor (EGF). |
Brands | Retavase (Centocor) Retavase (Roche)
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Categories | Thrombolytic Agents
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Packagers | EKR Therapeutics Inc. Hospira Inc. PDL BioPharma Inc.
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Synonyms | t- PA t-plasminogen activator Tissue-type plasminogen activator precursor tPA
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indication
For lysis of acute pulmonary emboli, intracoronary emboli and management of myocardial infarction
pharmacology
Reteplase cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction.
mechanism of action
Reteplase binds to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain. The protease domain then cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action.
drug interactions
Ginkgo biloba: Additive anticoagulant/antiplatelet effects may increase bleed risk. Concomitant therapy should be avoided.
Ticlopidine: Increased bleeding risk. Monitor for signs of bleeding.