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Blood, Vol. 92 No. 10 (November 15), 1998:
pp. 3684-3693
Shear-Dependent Rolling on von Willebrand Factor of Mammalian Cells
Expressing the Platelet Glycoprotein Ib-IX-V Complex
Becky J. Fredrickson,
Jing-Fei Dong,
Larry V. McIntire, and
José A. López
From the Cox Laboratory for Biomedical Engineering, Rice University,
Houston, TX; and the Department of Medicine, Division of
Hematology/Oncology, and the Department of Molecular and Human
Genetics, Baylor College of Medicine and Veterans Affairs Medical
Center, Houston, TX.
Mural thrombi form on exposed arterial subendothelium by a two-step
process of platelet adhesion and aggregation. At high shear stresses
such as are found in stenotic arteries, both steps are mediated by von
Willebrand factor (vWF). Platelets initially adhere on vWF affixed to
the subendothelial matrix through the glycoprotein (GP) Ib-IX-V
complex. To examine the role of the GP Ib-IX-V complex under dynamic
conditions, we modeled initial platelet adhesion at shear stresses
ranging from 2 to 40 dyn/cm2 using vWF-coated glass slides,
mammalian cells expressing full or partial GP Ib-IX-V complexes, and a
parallel plate flow chamber with phase contrast video microscopy and
digital image processing. Mammalian cells expressing the full complex
tethered and rolled on the vWF substrate, whereas control cells did
not. The rolling was completely inhibited by the monoclonal GP Ib
antibody, AK2, or the vWF antibody, 5D2, both shown previously to block
vWF-dependent platelet aggregation. Other GP Ib antibodies, WM23 and
SZ2, did not significantly change the number or mean velocity of
rolling cells. At low levels of GP Ib surface expression, cells
expressing the full complex rolled slower than cells expressing the
complex without GP V, indicating that GP V strengthens the interactions with the vWF surface under these conditions. Preshearing vWF for 5 minutes at 40 dyn/cm2 immediately before introducing cells
into the chamber did not significantly change the number or the mean
velocity of rolling cells. Inhibiting sulfation of the tyrosine
residues within the GP Ib subunit reduced the number but did not
change the mean velocity of the rolling cells. Our results indicate
that, under the conditions of these experiments, bonds between vWF and
GP Ib constantly form and break under fluid shear stress.
Additionally, our results suggest that GP Ib-IX-V complexes behave like
selectin receptors in their ability to mediate smooth rolling while
cells maintain continuous surface contact. Such a mechanism, in vivo, would allow platelets to slow down and eventually arrest on the blood
vessel wall. The system described provides a valuable approach for
investigating the structure-function relationship of individual receptors and ligands in the process of platelet adhesion and thrombosis.
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