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Confluent BAEC were stimulated with 5 mM 2-DG for 5 to 120 min, and AMPK activation was measured by monitoring phosphorylation of AMPKα-Thr172.
JNK activation was determined by monitoring phosphorylation of JNK (Thr183 and Tyr185) and c-Jun (Ser63), which is a substrate of JNK.
JNK activation was determined by monitoring phosphorylation of JNK1 and total expression of this protein.
These observations were confirmed at protein level by monitoring phosphorylation of Stat3 and extracellular signal-related kinase (Erk) 1/2.
Arginase activity in cells lysates was measured by colorimetric determination of urea formed from L-arginine as described previously [ 31]. mTORC1 and S6K1 activity were analyzed by monitoring phosphorylation of S6K1 at threonine-389 (S6K1-T389) and its substrate S6 at serine-235/serine-236 (S235/S236), respectively, by Western blotting.
Consequently, we looked at AKT and ERK1/2 activity by monitoring phosphorylation of these molecules and found that ACT1 treatment did not alter AKT or ERK1/2 phosphorylation status (Additional file 1: Figure S2B).
We confirmed this hypothesis by monitoring the phosphorylation of H2AXser139 (γH2AX) and p53ser15, which are important phosphorylation signals in DDR.
The activation of NF-κB can be assessed by monitoring the phosphorylation of the NF-κB inhibitor IκBα by IKK and the degradation of IκBα.
The translation control arm of the UPR was assessed by monitoring the phosphorylation of eukaryotic translation initiation factor 2 subunit alpha (eIF2 α) on serine 51, a commonly used indicator of protein kinase R-like ER kinase activation.
AMPK activation was evaluated by monitoring the phosphorylation of AMPK at Thr172 and ACC at Ser79.
