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Original

PLATELET INTERACTIONS WITH LIPOSOMES CARRYING RECOMBINANT PLATELET MEMBRANE GLYCOPROTEINS OR FIBRINOGEN: APPROACH TO PLATELET SUBSTITUTES

, , , &
Pages 453-464 | Published online: 11 Jul 2009

Figures & data

Figure 1. Interaction of rGPIa/IIa-Ibα-liposomes with platelets on the collagen surface depends on the shear rate. Images were obtained after a 3-min perfusion of a mixture of liposomes (4.0 × 105/μl) and platelets (1.0 × 105/μl) on the surface at a hematocrit of 37.5%, soluble vWf concentration of 10 μg/ml, 2 mM Mg2+, 37°C, and various shear rates as indicated. Exofacial concentration of rGPIa/IIa and rGPIbα was 1.0 and 0.70 μg/ml, respectively. Values are the mean ± standard deviation, n = 6.

Figure 1. Interaction of rGPIa/IIa-Ibα-liposomes with platelets on the collagen surface depends on the shear rate. Images were obtained after a 3-min perfusion of a mixture of liposomes (4.0 × 105/μl) and platelets (1.0 × 105/μl) on the surface at a hematocrit of 37.5%, soluble vWf concentration of 10 μg/ml, 2 mM Mg2+, 37°C, and various shear rates as indicated. Exofacial concentration of rGPIa/IIa and rGPIbα was 1.0 and 0.70 μg/ml, respectively. Values are the mean ± standard deviation, n = 6.

Figure 2. Inhibition of the interaction of rGPIa/IIa-Ibα-liposomes with platelets on the collagen surface. Experimental conditions were the same as described for . Inhibition studies were performed in the presence of the RGD-peptide (1 mM), RGE-peptide (1 mM), or PGE (1 μM).

Figure 2. Inhibition of the interaction of rGPIa/IIa-Ibα-liposomes with platelets on the collagen surface. Experimental conditions were the same as described for Figure 1. Inhibition studies were performed in the presence of the RGD-peptide (1 mM), RGE-peptide (1 mM), or PGE (1 μM).

Figure 3. Enhancement of platelet aggregation by rGPIa/IIa-Ibα-liposomes assessed by changes in light scattering intensity. PRP at 1 × 104/μl platelets was mixed with various concentrations of rGPIa/IIa-Ibα-liposomes, and 10 μg/ml of collagen was then added to the mixture.

Figure 3. Enhancement of platelet aggregation by rGPIa/IIa-Ibα-liposomes assessed by changes in light scattering intensity. PRP at 1 × 104/μl platelets was mixed with various concentrations of rGPIa/IIa-Ibα-liposomes, and 10 μg/ml of collagen was then added to the mixture.

Figure 4. Interaction of Fbg-liposomes with platelets on the collagen surface depends on the shear rate. Experimental conditions were the same as described for , except that the exofacial concentration of Fbg was 0.74 μg/ml.

Figure 4. Interaction of Fbg-liposomes with platelets on the collagen surface depends on the shear rate. Experimental conditions were the same as described for Figure 1, except that the exofacial concentration of Fbg was 0.74 μg/ml.

Figure 5. Inhibition of the interaction of Fbg-liposomes with platelets on the collagen surface. Experimental conditions were the same as described for .

Figure 5. Inhibition of the interaction of Fbg-liposomes with platelets on the collagen surface. Experimental conditions were the same as described for Figure 2.

Figure 6. Enhancement of platelet aggregation by Fbg-liposomes assessed by changes in light scattering intensity. PRP at 5 × 104/μl platelets was mixed with various concentrations of Fbg-liposomes, and 2 μM ADP was then added to the mixture.

Figure 6. Enhancement of platelet aggregation by Fbg-liposomes assessed by changes in light scattering intensity. PRP at 5 × 104/μl platelets was mixed with various concentrations of Fbg-liposomes, and 2 μM ADP was then added to the mixture.

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