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Thrombolytic and pharmacokinetic properties of chimeric tissue-type and urokinase-type plasminogen activators.
Author(s) -
D Collen,
H. R. Lu,
H.R. Lijnen,
L Nelles,
Jean Marie Stassen
Publication year - 1991
Publication title -
circulation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.795
H-Index - 607
eISSN - 1524-4539
pISSN - 0009-7322
DOI - 10.1161/01.cir.84.3.1216
Subject(s) - plasminogen activator , urokinase , medicine , pharmacokinetics , potency , pharmacology , fibrin , tissue plasminogen activator , endocrinology , immunology , biochemistry , biology , in vitro
Chimeric molecules comprising the A-chain of tissue-type plasminogen activator (t-PA) and the catalytic domain of urokinase-type plasminogen activator (u-PA) have intact enzymatic characteristics of u-PA, partial fibrin-binding properties of t-PA, and thrombolytic properties in animal models comparable with but not superior to those of single-chain u-PA (scu-PA). Deletion of the finger and growth factor domains (t-PA-delta FE/scu-PA-e) in such chimeras further reduces their affinity for fibrin.

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