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Plasminogen activation and lysis of blood clots induced by cells in vitro
Author(s) -
Knox Peter,
Crooks Sheila
Publication year - 1988
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041350314
Subject(s) - lysis , fibrin , platelet lysate , in vitro , tissue plasminogen activator , fibrinolysis , antiserum , chemistry , plasminogen activator , platelet , microbiology and biotechnology , biology , immunology , biochemistry , antibody , medicine , endocrinology
When human diploid fibroblasts were seeded onto the surface of blood clots, lysis of the clot occurred as a result of the release of cellular plasminogen activator. A number of aspects of this lysis were studied. 1. There was no significant difference in rates of lysis of whole blood clots, platelet‐rich plasma clots, and platelet‐poor plasma clots brought about by the same number of fibroblasts. 2. Clot lysis was promoted by nondividing cells and by proliferating cells. 3. Using cycloheximide to block protein synthesis it was found that the plasminogen activator released by fibroblasts had an active half‐life of less than an hour. 4. When clots were washed prior to the addition of cells then lysis occurred at an increased rate. This was probably due to the removal of α 2 ‐antiplasmin from the clots, since when antisera to α 2 ‐antiplasmin was added to clots, lysis also proceeded at an increased rate. 5. Medium conditioned by fibroblasts did not promote clot lysis even when antiplasmin was removed by washing or by addition of antisera. 6. Cells had to be in direct contact with the clot in order to bring about lysis; when cells were separated from clots by permeable membranes there was no lysis. 7. When cross‐linking of fibrin was reduced by the inhibition of transglutaminase, the rate of clot lysis was increased.