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Multimer size dependence of von Willebrand factor binding to crosslinked or
noncrosslinked fibrin
JA Ribes and CW Francis
Department of Medicine, University of Rochester School of Medicine &
Dentistry, NY.
von Willebrand factor (vWF) is synthesized in endothelial cells (EC) and
may be either secreted constitutively or stored in Weibel-Palade bodies
(WPB) for regulated release. Because fibrin stimulates rapid vWF release
from EC, we examined the binding of EC synthesized vWF to fibrin. Culture
medium containing constitutively secreted vWF was removed from
metabolically labeled primary cultures of human umbilical vein EC, and vWF
released from WPB was obtained after stimulation by A23187. vWF-deficient
fibrinogen with or without factor XIII was added to releasate or media and
clotted with thrombin to form crosslinked or noncrosslinked fibrin. vWF was
immunopurified from releasate or media before and after clotting, and the
amount and multimeric pattern of vWF bound was determined after sodium
dodecyl sulfate agarose gel electrophoresis. High molecular weight
multimers of vWF, whether secreted constitutively or released from WPB,
bound preferentially to fibrin. Multimers of greater than 20 subunits
represented 60% +/- 4% (SEM) of A23187 released vWF and 11% +/- 5% of media
vWF, but binding to fibrin was similar, 96% +/- 1% and 94% +/- 2%,
respectively. A progressively smaller proportion of vWF bound as multimer
size decreased, and dimeric vWF binding was least, with 34% +/- 5% binding
from A23187 releasate and 51% +/- 4% from media. The amount of vWF binding
to crosslinked or noncrosslinked fibrin was similar, and preferential
binding of high molecular weight multimers occurred with both. As measured
by enzyme-linked immunosorbent assay, 45% +/- 2% of constitutively secreted
vWF bound to crosslinked fibrin and 50% +/- 2% to noncrosslinked fibrin.
The propolypeptide of vWF did not bind to fibrin. These findings indicate
that binding of EC secreted vWF binding to fibrin depends on multimeric
size but not on factor XIII crosslinking. This suggests that vWF released
from EC in the presence of fibrin will bind locally, thereby facilitating
platelet adhesion to the hemostatic plug or thrombus.
Volume 75,
Issue 7,
pp. 1460-1465,
04/01/1990
Copyright © 1990 by The American Society of Hematology
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