Fig. 4.
Fig. 4. Effect of RhoA inactivation by C3 exoenzyme on agonist-induced affinity modulation of platelet αIIbβ3. Washed platelets were incubated with vehicle buffer (“No C3”) or C3 exoenzyme as in Fig 3. Cells were then diluted with incubation buffer and the affinity state of αIIbβ3 was assessed by flow cytometry using FITC-PAC1. PAC1 binding was expressed as a percentage, 100% being arbitrarily assigned to the maximal response for the “No C3” control sample that had been paired with the experimental sample containing 200 μg/mL of C3 exoenzyme. Data represent the means ± SEM of three experiments.

Effect of RhoA inactivation by C3 exoenzyme on agonist-induced affinity modulation of platelet αIIbβ3. Washed platelets were incubated with vehicle buffer (“No C3”) or C3 exoenzyme as in Fig 3. Cells were then diluted with incubation buffer and the affinity state of αIIbβ3 was assessed by flow cytometry using FITC-PAC1. PAC1 binding was expressed as a percentage, 100% being arbitrarily assigned to the maximal response for the “No C3” control sample that had been paired with the experimental sample containing 200 μg/mL of C3 exoenzyme. Data represent the means ± SEM of three experiments.

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