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Platelet adhesion and aggregation on human type VI collagen surfaces under
physiological flow conditions
JM Ross, LV McIntire, JL Moake and JH Rand
Cox Laboratory for Biomedical Engineering, Rice University, Houston,
TX77251, USA.
Type VI collagen is a subendothelial constituent that binds von Willebrand
factor (vWF) and platelets. The interaction of platelets with type VI
collagen and the roles of platelet glycoprotein (GP) receptors and vWF were
studied under flow conditions using epi- fluorescent videomicroscopy
coupled with digital image processing. We found that surface coverage was
less than 6% on collagen VI at a relatively high-wall shear rate (1,000
s-1) and was approximately 60% at a low-wall shear rate (100 s-1). The
molecular mechanisms involved in low-shear platelet binding were studied
using monoclonal antibodies to platelet GPIb and GPIIb-IIIa, and polymeric
aurin tricarboxylic acid. Anti-GPIIb-IIIa was the most effective in
eliminating adhesion (surface coverage, 0.8%), followed by anti-GPIb
(4.3%), and ATA (12.6%). Experiments with von Willebrand disease blood
indicate that vWF is involved in platelet adhesion to collagen VI at 100
s-1. In the absence of vWF, there may be direct binding of platelet
GPIIb-IIIa complexes to collagen VI. Adhesion and aggregation on collagen
VI are different in shear rate dependence from collagen I. Our results
suggest a possible role for collagen VI and vWF in platelet adhesion and
aggregation in vascular regions with low shear rates.
Volume 85,
Issue 7,
pp. 1826-1835,
04/01/1995
Copyright © 1995 by The American Society of Hematology
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