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Regulation of fibrinolysis by platelet-released plasminogen activator
inhibitor 1: light scattering and ultrastructural examination of lysis of a
model platelet-fibrin thrombus
JV Braaten, S Handt, WG Jerome, J Kirkpatrick, JC Lewis and RR Hantgan
Department of Biochemistry, Bowman Gray School of Medicine, Wake-Forest
University, Winston-Salem, NC 27157-1016.
We have investigated the role of plasminogen activator inhibitor 1 (PAI- 1)
in the regulation of fibrinolysis using a model thrombus composed of
thrombin-stimulated platelets, fibrin(ogen), plasminogen, and recombinant
tissue-type plasminogen activator. Laser light scattering kinetic
measurements showed that clot lysis was significantly delayed both by
thrombin-stimulated platelets and their cell-free releasate. This delay in
lysis was almost fully reversed by the addition of a PAI- 1-specific
monoclonal antibody that blocks the ability of PAI-1 to inhibit plasminogen
activators. Lysis half-times exhibited a linear dependence on the
concentration of PAI-1 antigen present, as determined by enzyme-linked
immunosorbent assay (ELISA). Sodium dodecylsulfate- polyacrylamide gel
electrophoresis (SDS-PAGE) followed by immunoblotting confirmed the
presence of PAI-1 antigen in the platelet releasates. Scanning electron
micrographs of the model thrombus components sampled late in lysis showed
considerable unproteolyzed fibrin still attached to platelets. Immunogold
cytochemistry detected large amounts of PAI-1 antigen in the partially
lysed platelet-fibrin thrombi. This PAI-1 appeared to be bound to the
fibrin network rather than to the platelet surface itself. We conclude that
the residual clots observed late in lysis represent platelet-associated
fibrin to which platelet-released PAI-1 has bound, rendering it less
susceptible to degradation.
Volume 81,
Issue 5,
pp. 1290-1299,
03/01/1993
Copyright © 1993 by The American Society of Hematology
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