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Factor XII-independent activation of factor XI in plasma: effects of
sulfatides on tissue factor-induced coagulation
D Gailani and GJ Broze
Division of Hematology Research, Jewish Hospital, Washington University, St
Louis, MO 63110.
Factor XI (FXI) may be activated in a purified system by thrombin and by
autoactivation in the presence of negatively charged substances such as
dextran sulfate or sulfatides. The current studies were performed to
determine if these processes occur during the coagulation of plasma.
FXII--deficient plasma was supplemented with 125I-FXI and clot formation
was induced with tissue factor and/or sulfatides. Cleavage of FXI was
studied by standard polyacrylamide gel electrophoresis and autoradiography.
Activated FXI (FXIa) was detected after 20 minutes of incubation with
sulfatides alone and this process was markedly accelerated by the addition
of tissue factor (TF). The enhancing effect of TF was blocked by hirudin,
which indicated thrombin involvement in FXI activation. The contribution of
FXIa to FIX activation in this system was studied using a 3H-FIX activation
peptide release assay. Sulfatides increased FIX activation about twofold in
plasma induced to clot with TF but had no effect if the plasma was
immunodepleted of FXI. FIX activation was also increased in plasma induced
to clot with FXa if sulfatides were present. The enhanced generation of
FIXa was dependent on FXI and was blocked by hirudin. Some activation was
seen in the reactions with sulfatides and hirudin and is likely solely
caused by FXI autoactivation. The data indicate that during the coagulation
of plasma in the presence of sulfatides, FXI is activated by a mechanism
that is thrombin dependent and does not require FXII.
Volume 82,
Issue 3,
pp. 813-819,
08/01/1993
Copyright © 1993 by The American Society of Hematology
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