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

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