M. Roger et al., THE MEMBRANE GLYCOPROTEIN IIB IIIA COMPLEX MEDIATES DEPOSITION OF THROMBIN-STIMULATED BLOOD-PLATELETS ON POLYSTYRENE PLASTIC UNDER STATIC CONDITIONS/, Platelets, 5(2), 1994, pp. 96-104
A major challenge in the use of artificial materials for implant devic
es, artificial organs, and extra-corporeal circulation systems, is the
adhesion of platelets and the subsequent formation of platelet aggreg
ates on the non-biological surface. The mechanism of platelet attachme
nt to artificial surfaces is not completely understood. Using an enzym
e immunoassay, we examined platelet deposition to the polystyrene plas
tic of microtiter plate wells under static conditions. Following throm
bin stimulation, platelets adhered to the wells. This adhesion process
was suppressible by the use of different substances known to interfer
e with the function of the platelet surface glycoprotein IIb/IIIa comp
lex (GPIIb/IIIa). The substances we used were: ethylenediaminetetraace
tic acid (EDTA), tetrapeptide RGDS (Arg-Gly-Asp-Ser), and a monoclonal
antibody directed against the ma moiety of the GPIIb/IIIa complex. Ou
r results indicate that the GPIIb/IIIa complex is the platelet recepto
r which mediates platelet adhesion to polystyrene plastic under such s
tatic conditions. The GPIIb/IIIa complex should consequently be regard
ed as a multifunctional platelet regulator which, depending on the cir
cumstances, may support platelet adhesion as well as platelet aggregat
ion. By contrast, a monoclonal antibody directed against the platelet
surface glycoprotein complex Ib/IX (GPIb/IX) did not under the same st
atic conditions inhibit platelet deposition to the polystyrene plastic
. In the microtiter wells, platelet alpha-granular proteins were detec
ted either on the surface of adherent platelets or, when platelet depo
sition was inhibited by EDTA directly on the polystyrene plastic. In t
he latter case, fibrinogen and thrombospondin were definitely the domi
nating proteins. The presence of platelet-derived proteins in the micr
otiter wells significantly enhanced the adhesion of thrombin-stimulate
d platelets but not of non-stimulated platelets.