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Activation/inactivation of human factor V by plasmin
CD Lee and KG Mann
Department of Biochemistry, University of Vermont, College of Medicine,
Burlington 05405-0068.
The effect of human plasmin on human coagulation factor V was studied using
isolated proteins. Incubation of factor V with plasmin resulted in a rapid
increase in procoagulant activity, followed by a subsequent decline in the
ability of factor V to serve as a cofactor in the prothrombinase complex.
Identical results were obtained when these reactions were conducted in the
presence of dansylarginine-N-(3-ethyl- 1,5-pentanediyl) amide (DAPA),
indicating that the changes observed could not have occurred as a
consequence of cleavage by alpha-thrombin. Analysis of the products of the
reaction by sodium dodecyl sulfate- polyacrylamide gel electrophoresis
(SDS-PAGE) revealed a temporal correlation between the rise and fall in
factor V activity and the presence of several transient intermediates.
These fragments are distinct from the subunits of alpha-thrombin-activated
factor V (factor Va). The activation phase of the reaction was not
significantly affected by the presence of phospholipid. In contrast, the
rate of degradation of active fragments of factor V and the accompanying
loss of activity were markedly enhanced in the presence of phospholipid
vesicles. These data suggest that the action of plasmin upon factor V
results in the transient formation of proteolytic fragments which express
significant procoagulant activity.
Volume 73,
Issue 1,
pp. 185-190,
01/01/1989
Copyright © 1989 by The American Society of Hematology
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