Akt phosphorylation in response to PAR4 stimulation in mouse platelets is secretion- and αIIbβ3-dependent.

(A) Aggregation of normal and Tp deficient mouse washed platelets induced by 160 µM of the PAR4 agonist peptide AYPGKF. Aggregation of Tp deficient mouse platelets induced by 160 µM of the PAR4 agonist peptide AYPGKF with and without 10 U/ml of apyrase, ± 250 µg/ml of Fg, ± 10 µg/ml of mAb 1B5. (B) Akt Ser473 phosphorylation of normal and Tp deficient mouse platelets treated with and without 10 U/ml of apyrase, ± 250 µg/ml of Fg, ± 10 µg/ml of mAb 1B5. (C) Aggregation of normal and β3 deficient mouse washed platelets induced by 160 µM of peptide AYPGKF. (D) Akt Ser473 phosphorylation of normal and β3 deficient mouse washed platelets induced by 160 µM of peptide AYPGKF. The experiments were repeated for three times.