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Biophys J, July 2002, p. 194-205, Vol. 83, No. 1
-vWF Tether Bond
and
*Division of Newborn Medicine, Department of Pediatrics and
Department of Pathology, Department of Bioengineering,
Washington University and St. Louis Children's Hospital, St. Louis,
Missouri 63110 USA; and Institute for Medicine and
Engineering, Department of Chemical Engineering, 1024 Vagelos Research
Laboratories, University of Pennsylvania, Philadelphia, Pennsylvania
19004 USA
The ability of platelets to tether to and translocate on
injured vascular endothelium relies on the interaction between the platelet glycoprotein receptor Ib 
(GPIb) and the A1 domain of
von Willebrand factor (vWF-A1). To date, limited information exists on
the kinetics that govern platelet interactions with vWF in hemodynamic
flow. We now report that the GPIb-vWF-A1 tether bond displays
similar kinetic attributes as the selectins including: 1) the
requirement for a critical level of hydrodynamic flow to initiate
adhesion, 2) short-lived tethering events at sites of vascular injury
in vivo, and 3) a fast intrinsic dissociation rate constant,
k
1). Values for koff, as
determined by pause time analysis of transient capture/release events,
were also found to vary exponentially (4.2 ± 0.8 s1
to 7.3 ± 0.4 s1) as a function of the force applied
to the bond (from 36 to 217 pN). The biological importance of rapid
bond dissociation in platelet adhesion is demonstrated by kinetic
characterization of the A1 domain mutation, I546V that is associated
with type 2B von Willebrand disease (vWD), a bleeding disorder that is
due to the spontaneous binding of plasma vWF to circulating platelets.
This mutation resulted in a loss of the shear threshold phenomenon, a
approximately sixfold reduction in koff, but
no significant alteration in the ability of the tether bond to resist
shear-induced forces. Thus, flow dependent adhesion and rapid and
force-dependent kinetic properties are the predominant features of the
GPIb-vWF-A1 tether bond that in part may explain the preferential
binding of platelets to vWF at sites of vascular injury, the lack of
spontaneous platelet aggregation in circulating blood, and a mechanism
to limit thrombus formation.
Biophys J, July 2002, p. 194-205, Vol. 83, No. 1
© 2002 by the Biophysical Society 0006-3495/02/07/194/12 $2.00
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