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Factor XIIIa binding to activated platelets is mediated through activation
of glycoprotein IIb-IIIa
AD Cox and DV Devine
Department of Pathology, University of British Columbia, Vancouver, Canada.
Stabilization of a clot is dependent on fibrin cross-linking mediated by
the transglutaminase, factor XIIIa (FXIIIa). In addition to fibrin
stabilization, FXIIIa acts on a number of platelet-reactive proteins,
including fibronectin and vitronectin, as well as the platelet proteins,
glycoprotein (GP) IIb-IIIa, myosin, and actin. However, conditions inducing
the platelet-activation dependent binding of FXIIIa have not been
characterized nor have the sites mediating FXIIIa binding been identified.
The generation of FXIIIa and consequent detection of FXIIIa on the platelet
surface were compared with other thrombin- induced activation events; the
rate at which FXIIIa bound to activated platelets was much slower than
platelet degranulation or fibrin(ogen) binding. Whereas platelets could be
rapidly induced to express a functional receptor for FXIIIa, the rate of
FXIIIa binding to platelets is limited by the rate of conversion of FXIII
to FXIIIa. Immunoprecipitation of radiolabeled platelets using polyclonal
anti- FXIII A-chain antibody identified two proteins corresponding to GPIIb
and GPIIIa. Preincubation of intact platelets with 7E3, a monoclonal
antibody that blocks the fibrinogen binding site, or GRGDSP peptide
inhibited FXIIIa binding by about 95% when measured by flow cytometry;
FXIIIa binding to purified GPIIb-IIIa was also inhibited by 7E3. The
binding of FXIIIa to purified GPIIb-IIIa was enhanced by the addition of
fibrinogen, but not by that of fibronectin or thrombospondin, suggesting
that FXIIIa also binds to fibrinogen associated with the complex. These
observations suggest that activated platelets bearing FXIIIa may enhance
stabilization of platelet-rich thrombi through surface-localized
cross-linking events.
Volume 83,
Issue 4,
pp. 1006-1016,
02/15/1994
Copyright © 1994 by The American Society of Hematology
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