scholarly journals A new platelet-specific alloantigen system, Yuka/Yukb is located on platelet membrane glycoprotein IIIa.

1987 ◽  
Vol 63 (1) ◽  
pp. 36-38 ◽  
Author(s):  
Yoichi SHIBATA ◽  
Hiroshi MORI
Keyword(s):  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Platelet Membrane Glycoprotein ◽  
Glycoprotein Iiia

An additional HpaII polymorphism in exon 2 of the human platelet membrane glycoprotein IIIa gene

1994 ◽  
Vol 93 (3) ◽  
pp. 353-354 ◽  
Author(s):  
Bruno Perichon ◽  
Sylvie Clemenceau ◽  
Alain Romand ◽  
Jacques Elion ◽  
Cecile Kaplan ◽  
...  
Keyword(s):  
Human Platelet ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Exon 2 ◽  
Platelet Membrane Glycoprotein ◽  
Glycoprotein Iiia

scholarly journals Thrombin-induced platelet membrane glycoprotein IIb and IIIa complex formation. An electron microscope study.

1981 ◽  
Vol 154 (4) ◽  
pp. 1058-1068 ◽  
Author(s):  
M J Polley ◽  
L L Leung ◽  
F Y Clark ◽  
R L Nachman
Keyword(s):  
Complex Formation ◽  
Keyhole Limpet Hemocyanin ◽  
Human Platelets ◽  
Platelet Membrane ◽  
Macromolecular Complex ◽  
Membrane Glycoprotein ◽  
Platelet Surface ◽  
Platelet Membrane Glycoprotein ◽  
Normal Platelet ◽  
Glycoprotein Iiia

The topographic relationships of platelet membrane glycoprotein IIb and glycoprotein IIIa have been studied in stimulated and unstimulated human platelets using immunoelectron microscopy. An indirect approach with ferritin-conjugated goat anti-rabbit gamma-globulin was used to localize the rabbit antibody to glycoprotein IIIa. The second ultrastructural label was keyhole limpet hemocyanin conjugated directly to antibody to glycoprotein IIb. Using the double labels, it was demonstrated that glycoprotein IIb and glycoprotein IIIa were distributed randomly in the unstimulated platelet membrane. After platelet stimulation with thrombin, large clusters of glycoprotein IIb-glycoprotein IIIa complexes were formed. No complex formation between glycoprotein Ib and glycoprotein IIb was observed in control experiments. These observations suggest that thrombin stimulation initiates the specific glycoprotein IIb-glycoprotein IIIa macromolecular complex formation on the platelet surface, which may act as the active fibrinogen-binding site required for normal platelet aggregation.

DN-9693: A PHOSPHODIESTERASE INHIBITOR WITH A PLATELET MEMBRANE EFFECT

1987 ◽  
Author(s):  
J Ball ◽  
M Greaves ◽  
C Jackson ◽  
J Peel ◽  
F E Preston
Keyword(s):  
Platelet Rich Plasma ◽  
Phosphodiesterase Inhibitor ◽  
Water Soluble ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Glycoprotein Ib ◽  
Platelet Surface ◽  
Platelet Membrane Glycoprotein ◽  
Plasma Factor ◽  
Glycoprotein Iiia

We have examined the effect of DN-9693 (piperidinyl - imidazo - quinazoline: Daiichi Seiyaku, Japan) a water soluble phosphodiesterase inhibitor on platelet aggregation, secretion and thromboxane B2 (TXB2) production. In platelet rich plasma and at concentrations of 2uM and 5uM the drug significantly inhibited aggregation induced by adenosine diphosphate, collagen and sodium arachidonate. TXB2 production and release of adenosine tri-phosphate and 14C 5-hydroxytryptamine were also significantly inhibited by the drug. Cyclic adenosine mono-phosphate accumulation was enhanced. Inhibition of ristocetin induced platelet agglutination was an unexpected finding and further experiments were undertaken to explore this. These suggested no specific effect against a plasma factor (von Willebrand factor) and reduced expression of the platelet membrane glycoprotein Ib was implicated. To investigate this further we examined the effect of DN-9693 on the binding of a monoclonal antibody (McAb) to platelet membrane glycoprotein lb (AN51). This was assessed by a FACS IV flow cytofluorimeter utilising a goat anti-mouse fluorescein isothiocyanate (FITC) labelled secondary antibody. Similar experiments were also performed with McAbs to the membrane glycoprotein complex IIb/IIIa (M148) and also to glycoprotein IIIa (C17). In platelet rich plasma, at concentrations which have been shown to inhibit aggregation, DN-9693 significantly reduced the mean fluorescence intensity of the cells coated with McAb AN51 in a dose related manner. This strongly suggested a drug effect against the glycoprotein Ib receptor site. Also, the drug appeared to enhance the binding of McAb C17 to glycoprotein IIIa. This study indicates that in addition to potent phosphodiesterase inhibitor activity, DN-9693 causes a platelet surface membrane change which is associated with reduced expression of membrane glycoprotein Ib.

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