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Platelet adhesion to fibronectin in flow: dependence on surface
concentration and shear rate, role of platelet membrane glycoproteins GP
IIb/IIIa and VLA-5, and inhibition by heparin
S Beumer, MJ IJsseldijk, PG de Groot and JJ Sixma
Department of Haematology, University Hospital, Utrecht, The Netherlands.
Platelet adhesion to purified surface-immobilized fibronectin under flow
conditions was investigated. Fibronectin was found to support attachment
and spreading of platelets. The extent of platelet spreading depended on
the amount of immobilized fibronectin. An antiglycoprotein (anti-GP)
IIb/IIIa antibody and an Arg-Gly-Asp (RGD)-containing peptide inhibited
adhesion almost completely, whereas antibodies directed against platelet GP
Ic/IIa (very late antigen 5) inhibited by 50%. Similar results with the
antibodies and the peptide were found in a static system. A comparison of
different anticoagulants showed no difference in adhesion using citrate or
hirudin. However, unfractionated heparin (UFH) or low-molecular-weight
heparin (LMWH) as the only anticoagulant or in combination with citrate
maximally inhibited adhesion by 80% and 60%, respectively. Preincubation of
the immobilized fibronectin with UFH resulted in a maximal inhibition of
90%, whereas preincubation with LMWH had no effect. When we preincubated
the surface with heparins of different size, we observed 40% inhibition of
adhesion with heparins with an average MW of up to 18 kD, whereas a heparin
with an average MW of 21 kD almost completely blocked adhesion. These
results indicate that platelet adhesion to fibronectin in flow involves
several receptors, is highly RGD-mediated, does not require physiologic
levels of divalent cations, and can be inhibited by direct binding of
heparin to the fibronectin surface.
Volume 84,
Issue 11,
pp. 3724-3733,
12/01/1994
Copyright © 1994 by The American Society of Hematology
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