Tissue-type plasminogen activator increases the binding of glu-plasminogen to clots

Porcine tissue-type plasminogen activator (t-PA) increases the binding of 125I-glu-plasminogen to clots made from human plasma or purified fibrinogen in a time and t-PA concentration dependent fashion. The accumulation of plasminogen was faster and greater on noncrosslinked plasma clots than on clot...

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Bibliographic Details
Published in:The Journal of clinical investigation 1984-12, Vol.74 (6), p.2009-2016
Main Authors: CHIEN TRAN-THANG, KRUITHOF, E. K. O, BACHMANN, F
Format: Article
Language:English
Subjects:
Animals
Aprotinin - pharmacology
Biological and medical sciences
Blood Coagulation
Blood coagulation. Blood cells
Electrophoresis, Polyacrylamide Gel
Fibrin - metabolism
Fundamental and applied biological sciences. Psychology
General aspects, investigation methods, hemostasis, fibrinolysis
Humans
Isoflurophate - pharmacology
Kinetics
Molecular and cellular biology
Plasminogen - metabolism
Plasminogen Activators - pharmacology
Swine
Time Factors
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Summary:Porcine tissue-type plasminogen activator (t-PA) increases the binding of 125I-glu-plasminogen to clots made from human plasma or purified fibrinogen in a time and t-PA concentration dependent fashion. The accumulation of plasminogen was faster and greater on noncrosslinked plasma clots than on clots which had been crosslinked by Factor XIIIa. Furthermore, the uptake of plasminogen to crosslinked fibrin clots occurred at a slower rate in the presence of alpha 2-plasmin inhibitor (alpha 2 PI) than in its absence. The kinetics of the uptake of 125I-plasminogen were analyzed using SDS-polyacrylamide gel electrophoresis and radioautography of solubilized plasma clots formed in the presence of t-PA. During the initial phase there was a decrease of clot-bound glu-plasminogen; simultaneously, there was a slight increase in clot-bound glu-plasmin and in plasmin complexed to alpha 2 PI that was crosslinked to alpha-chain polymers of fibrin. This was followed by a marked increase in clot-bound plasminogen having glutamic acid as NH2-terminal (glu-plasminogen) and gluplasmin. t-PA-induced enhancement of glu-plasminogen uptake appears to be mediated by plasmin but does not require the conversion of glu-plasminogen to plasminogen having lysine or methionine as NH2-terminal. The described mechanism assures an adequate supply of clot-bound plasmin, which is the enzyme ultimately involved in the degradation of fibrin.
ISSN:0021-9738
1558-8238
DOI:10.1172/JCI111623