Figure 6
Figure 6. Role of AMPKα2 in the threonine phosphorylation of Fyn. (A) Effect of SKF inhibition (PP2, 30nM) on the thrombin-induced phosphorylation (p-Tyr747) of β3 integrin in washed human platelets. (B) In vitro kinase assays showing 32P incorporation into Fyn (left panel) and its threonine phosphorylation (p-Thr; right panel) in the presence of AMPK. Experiments were performed in the absence and presence of PP2 iodotubercidin (Iodo) and compound C (CC). (C) Thrombin-induced phosphorylation of Fyn on Thr12 in platelets from AMPKα2+/+ and α2−/− mice. The bar graphs summarize data from 6 different experiments; *P < .05 and **P < .01 vs solvent (Sol)-treated platelets in the absence of thrombin.

Role of AMPKα2 in the threonine phosphorylation of Fyn. (A) Effect of SKF inhibition (PP2, 30nM) on the thrombin-induced phosphorylation (p-Tyr747) of β3 integrin in washed human platelets. (B) In vitro kinase assays showing 32P incorporation into Fyn (left panel) and its threonine phosphorylation (p-Thr; right panel) in the presence of AMPK. Experiments were performed in the absence and presence of PP2 iodotubercidin (Iodo) and compound C (CC). (C) Thrombin-induced phosphorylation of Fyn on Thr12 in platelets from AMPKα2+/+ and α2−/− mice. The bar graphs summarize data from 6 different experiments; *P < .05 and **P < .01 vs solvent (Sol)-treated platelets in the absence of thrombin.

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