Platelet adhesion to synthetic surfaces that come in contact with blood is
mediated by the adsorption of adhesive plasma proteins, especially fibrinog
en. However, the roles of other adhesive proteins, such as fibronectin, vit
ronectin: and von Willebrand factor in platelet adhesion are not yet clear.
In this study, the role of fibronectin in platelet adhesion to surfaces wa
s assessed using three approaches. First, platelet adhesion was measured on
Immulon I(R) preadsorbed with fibronectin-depleted plasma or fibronectin-d
epleted plasma replenished with increasing amount of fibronectin. Under the
se conditions, fibronectin adsorbed from plasma did not have any effect on
platelet adhesion, while fibrinogen played a major role in mediating platel
et adhesion. Since fibronectin might play a role in platelet adhesion to su
rfaces which adsorb little or no fibrinogen; we also used two other strateg
ies to assess the potential role of fibronectin. One was to use platelets t
reated with a platelet activation inhibitor, prostaglandin E-1, which preve
nts the activation of platelet fibrinogen receptor GP IIb/IIIa. The adhesio
n of prostaglandin E-1-treated platelets to Immulon IO preadsorbed with pla
sma was greatly decreased compared to that of untreated platelets, but was
increased by the addition of supernormal concentrations of fibronectin to t
he plasma. This suggests that GP Ic/IIa, rather than GP IIb/IIIa, might be
the platelet receptor which is responsible for platelet adhesion to surface
-bound fibronectin. Finally, we studied the effect of fibronectin on platel
et adhesion to surfaces preadsorbed with fibronectin-depleted afibrinogenem
ic plasma. We found that fibronectin re-addition to fibronectin-depleted af
ibrinogenemic plasma increased platelet adhesion. However. our most importa
nt Ending was that fibronectin seems to play little or no role is mediating
platelet adhesion to polystyrene surfaces preadsorbed with normal plasma.