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Regulation of plasma factor XIII binding to fibrin in vitro
CS Greenberg, JV Dobson and CC Miraglia
The binding of plasma factor XIII to fibrinogen or fibrin that has been
chemically or enzymatically induced to polymerize was studied. Factor XIII
binding was assayed using a 3H-putrescine incorporation assay and an
125I-plasma factor XIII binding assay. More than 80% of the native and
radiolabeled plasma factor XIII was bound to fibrin I formed by reptilase
in EDTA, citrate, or heparin anticoagulated plasma. Plasma factor XIII and
125I-factor XIII was bound (89.6% to 92.5%) to fibrin II formed by thrombin
in either citrate or EDTA anticoagulated plasma. Sodium dodecyl
sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of 125I-plasma factor
XIII bound to fibrin I or fibrin II formed by reptilase or thrombin in the
presence of EDTA demonstrated the b2- subunit remained bound to the
a-chains or thrombin-cleaved a-chains. In the presence of calcium chloride
and thrombin, the b2-subunit dissociated and factor XIIIa was bound.
Protamine sulfate caused fibrinogen polymerization in the absence of
divalent cations and reduced both plasma factor XIII and immunologic
fibrinogen levels. Fibrinogen polymerized by protamine sulfate bound plasma
factor XIII and the a2-subunit of 125I-platelet factor XIII. Plasma factor
XIII was also bound to sonicated non-cross-linked fibrin II in either
normal plasma or afibrinogenemic plasma. Plasma levels of several
coagulation proteins were unchanged after the addition of reptilase,
protamine sulfate, or sonicated fibrin to plasma. These results demonstrate
that a specific binding site for the a2-subunit of plasma factor XIII is
present on polymerized fibrinogen, fibrin I, and fibrin II. Furthermore,
the presence of divalent cations, thrombin-cleavage of plasma factor XIII,
and release of fibrinopeptides A or B are not required for plasma factor
XIII binding to polymerized fibrinogen and fibrin.
Volume 66,
Issue 5,
pp. 1028-1034,
11/01/1985
Copyright © 1985 by The American Society of Hematology
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