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Thrombolytic Treatment with Recombinant Tissue-Type Plasminogen Activator in a Patient with Massive Pulmonary Embolism

HENRI BOUNAMEAUX, M.D.; JOSEPH VERMYLEN, M.D.; and COLLEN DÉSIRÉ, M.D.; Ph.D.
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Grant support: Dr. Bounameaux was supported by a grant from the Swiss National Research Foundation.

▸Requests for reprints should be addressed to Désiré Collen, M.D., Ph.D.; Center for Thrombosis and Vascular Research, Campus Gasthuisberg, University of Leuven, Herestraat 49; B-3000 Leuven, Belgium.


University of Leuven; Leuven, Belgium


Ann Intern Med. 1985;103(1):64-65. doi:10.7326/0003-4819-103-1-64
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This excerpt has been provided in the absence of an abstract.

Physiologic thrombolysis appears to be regulated via adsorption of tissue-type plasminogen activator and plasminogen on the fibrin surface, and generation of plasmin out of reach of circulating alpha 2-antiplasmin (1). The thrombolytic agents streptokinase and urokinase, which have no specific affinity for fibrin, activate circulating and fibrin-bound plasminogen without preference. Extensive plasminogen activation and plasmin generation will exhaust alpha 2-antiplasmin, and then free circulating plasmin will degrade several plasma coagulation proteins such as fibrinogen, factor V, and factor VIII. This hemostatic breakdown may cause bleeding. Therefore, fibrinspecific plasminogen activators could constitute safer thrombolytic agents. Promising results have been reported in

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