Figure 4.
Figure 4. The impact of deleting RGS10 on Akt phosphorylation. (A-B) Gel-filtered platelets from RGS10−/− mice or matched WT controls were incubated with vehicle, 350 μM AYPGKF, or 20 μM ADP for 5 minutes in the presence or absence of the P2Y1 antagonist MRS2500 (50 µM) or the P2Y12 antagonist cangrelor (100 nM), as indicated. Lysates were probed with anti–p-Akt (S473) and then reprobed with anti-Akt. The p-Akt signal was normalized to the Akt loading control and is represented as signal relative to the maximum for WT controls. Data are mean ± SEM, N = 5. (C-D) Platelets were incubated for 5 minutes with AYPGKF at the concentrations shown, lysed, and immunoblotted for p-Akt and Akt as in panel A. Quantification was performed as in panels A and B. Data are mean ± SEM. N = 3 to 5.

The impact of deleting RGS10 on Akt phosphorylation. (A-B) Gel-filtered platelets from RGS10−/− mice or matched WT controls were incubated with vehicle, 350 μM AYPGKF, or 20 μM ADP for 5 minutes in the presence or absence of the P2Y1 antagonist MRS2500 (50 µM) or the P2Y12 antagonist cangrelor (100 nM), as indicated. Lysates were probed with anti–p-Akt (S473) and then reprobed with anti-Akt. The p-Akt signal was normalized to the Akt loading control and is represented as signal relative to the maximum for WT controls. Data are mean ± SEM, N = 5. (C-D) Platelets were incubated for 5 minutes with AYPGKF at the concentrations shown, lysed, and immunoblotted for p-Akt and Akt as in panel A. Quantification was performed as in panels A and B. Data are mean ± SEM. N = 3 to 5.

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