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Mini-plasminogen: a mechanism for leukocyte modulation of plasminogen
activation by urokinase
LA Moroz
Urokinase activation of blood fibrinolysis involves polymorphonuclear
leukocytes. To determine if a leukocyte proteinase can modulate plasminogen
activation, plasminogen was digested with leukocyte elastase. A major
product was a small, approximately 34,000 dalton fragment
(mini-plasminogen), without lysine-binding function, but with
fibrin-binding activity. After urokinase activation, the resulting mini-
plasmin had amidolytic activity for a tripeptide plasmin substrate and
fibrinolytic activity. By 125I-fibrin assay, activities of mini-plasmin and
plasmin (12 nmole/liter) were 38 and 20 ng fibrin lysed/min, respectively.
Lysis times of fibrin clots containing urokinase, and mini-plasminogen or
plasminogen (800 nmole/liter), were 282 and 290 sec, respectively.
Mini-plasmin and plasmin were inhibited similarly by epsilon-aminocaproic
acid and normal plasma, but differed in responses to gel filtration
fractions of plasma containing alpha 2-antiplasmin and alpha
2-macroglobulin, the primary and secondary plasmin inhibitors. With
purified inhibitors, mini-plasmin required higher concentrations of, or
longer preincubation with, alpha 2-antiplasmin, and lower concentrations
of, or shorter preincubation with, alpha 2- macroglobulin, to produce
inhibition equivalent to that observed with plasmin. Leukocyte elastase
digests plasminogen to generate a mini- plasminogen which, when activated
by urokinase, has a novel pattern of response to the major plasmin
inhibitors in plasma.
Volume 58,
Issue 1,
pp. 97-104,
07/01/1981
Copyright © 1981 by The American Society of Hematology
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