Title: Role of alpha2-antiplasmin in fibrin-specific clot lysis with single-chain urokinase-type plasminogen activator in human plasma
Authors: Declerck, Paul ×
Lijnen, Roger
Verstreken, M
Collen, Desire #
Issue Date: Apr-1991
Series Title: Thrombosis and haemostasis vol:65 issue:4 pages:394-8
Abstract: The role of plasma alpha 2-antiplasmin (alpha 2-AP) in the fibrin-specificity of clot lysis by recombinant single-chain urokinase-type plasminogen activator (rscu-PA) and in the conversion of rscu-PA to its two-chain derivative (rtcu-PA, urokinase) was investigated in an in vitro human plasma clot lysis system. Fifty % lysis in 2 h of a 0.1 ml 125I-fibrin labeled human plasma clot immersed in 0.5 ml normal human plasma was obtained with 1.4 +/- 0.15 micrograms/ml rscu-PA (mean +/- SD, n = 8). This was associated with degradation of 23 +/- 7% of fibrinogen and generation of 0.20 +/- 0.09 micrograms/ml rtcu-PA. In alpha 2-AP-depleted plasma 50% clot lysis in 2 h required 2-fold less rscu-PA which was associated with 3-fold more extensive fibrinogen degradation and 2-fold more rtcu-PA generation. Fifty % lysis in 2 h, of a 0.1 ml alpha 2-AP-depleted plasma clot, submersed in 0.5 ml normal plasma, was obtained with 0.80 +/- 0.05 micrograms/ml rscu-PA (n = 3, p less than 0.001 vs normal clot) and was associated with 17 +/- 6% fibrinogen breakdown (p = 0.22 vs normal clot) and 0.08 +/- 0.02 micrograms/ml rtcu-PA generation (p less than 0.05 vs normal clot). In alpha 2-AP-depleted plasma the equipotent rscu-PA concentration was 4-fold lower than in normal plasma and was associated with 3-fold more fibrinogen degradation and a similar extent of rtcu-PA generation.(ABSTRACT TRUNCATED AT 250 WORDS)
ISSN: 0340-6245
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular and Vascular Biology
Laboratory for Pharmaceutical Biology (-)
× corresponding author
# (joint) last author

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