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Circulation, Vol 87, 1850-1853, Copyright © 1993 by American Heart Association
D Collen and F Van de Werf
BACKGROUND. Staphylokinase (STA), a protein with known profibrinolytic
properties, is produced by transduced Staphylococcus aureus strains. In
experimental animal models, recombinant staphylokinase (STAR) is less
immunogenic and more active toward platelet-rich arterial blood clots than
streptokinase. METHODS AND RESULTS. In the present study, 10 mg STAR given
intravenously over 30 minutes was found to induce angiographically
documented coronary artery recanalization within 40 minutes in four of five
patients with acute myocardial infarction. Plasma fibrinogen and alpha
2-antiplasmin levels were unaffected, and allergic reactions were not
observed. Postinfusion disappearance of STAR antigen followed a biphasic
mode with a t1/2 alpha of 6.3 +/- 0.6 minutes (mean +/- SD) and a t1/2 beta
of 37 +/- 15 minutes, corresponding to a plasma clearance of 270 +/- 100
mL/min. Neutralizing antibodies against STAR could not be demonstrated at
baseline and up to 6 days after infusion, but STAR neutralizing activity,
which did not cross-react with streptokinase, was consistently demonstrable
in plasma at 14-35 days. CONCLUSIONS. STAR can induce clot-selective
coronary thrombolysis in patients with evolving myocardial infarction
without concomitant induction of a systemic lytic state. STAR, a small
protein that can be easily produced by recombinant DNA technology, may
therefore offer promise for thrombolytic therapy in patients with
thromboembolic disease.
ARTICLES
Coronary thrombolysis with recombinant staphylokinase in patients with evolving myocardial infarction
Center for Thrombosis and Vascular Research, University of Leuven, Belgium.
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