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- W46509437 abstract "Ataxia Telangiectasia mutated (ATM) is a kinase that has been shown to be necessary in the phosphorylation of AMPK in fibroblasts stimulated by IGF-1, and we have previously found that the ATM activator chloroquine (CQ) causes an increase in the phosphorylation of AMPK. Based on these findings, we hypothesized that CQ would cause an increase in the phosphorylation of AMPK in C2C12 myotubes in an ATM dependent manner. Myotubes were incubated with 0-750 μM CQ. 750 μM CQ increased phosphorylation of ATM at S1981, a marker for ATM activation (P<0.05). To test whether ATM was necessary for CQ's effect of increasing phosphorylation of AMPK, C2C12 cells were lentivirally transduced with short hairpin RNA (shRNA) against ATM. Cells transduced with shRNA against ATM had an 80% decrease of ATM expression compared to wildtype cells and a cell line transduced with green fluorescent protein (GFP). 500 μM CQ increased phosphorylation of AMPK in cell lines expressing either the shRNA against ATM or GFP (P<0.01, main effect of CQ). A specific ATM inhibitor, KU55933 (KU), was used to discover whether ATM was involved in increasing phosphorylation of a downstream target of AMPK, ACC. Even in the presence of KU, 500 μM CQ caused phosphorylation of ACC to increase (P<0.01, main effect of CQ). Our results suggest that ATM is not required for CQ-related stimulation of AMPK phosphorylation and ACC phosphorylation in C2C12 myotubes." @default.
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- W46509437 date "2010-04-01" @default.
- W46509437 modified "2023-09-26" @default.
- W46509437 title "The ATM activator chloroquine stimulates phosphorylation of AMP activated protein kinase (AMPK) and acetyl CoA‐carboxylase (ACC) independent of ATM" @default.
- W46509437 doi "https://doi.org/10.1096/fasebj.24.1_supplement.lb674" @default.
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