| First Author | Guo Y | Year | 2016 |
| Journal | Arch Biochem Biophys | Volume | 600 |
| Pages | 56-60 | PubMed ID | 27136709 |
| Mgi Jnum | J:248763 | Mgi Id | MGI:6093420 |
| Doi | 10.1016/j.abb.2016.04.015 | Citation | Guo Y, et al. (2016) AMP-activated kinase alpha2 deficiency protects mice from denervation-induced skeletal muscle atrophy. Arch Biochem Biophys 600:56-60 |
| abstractText | AMP-activated protein kinase (AMPK) is a master regulator of skeletal muscle metabolic pathways. Recently, AMPK activation by AICAR has been shown to increase myofibrillar protein degradation in C2C12 myotubes via stimulating autophagy and ubiquitin proteasome system. However, the impact of AMPKalpha on denervation induced muscle atrophy has not been tested. In this study, we performed sciatic denervation on hind limb muscles in both wild type (WT) and AMPKalpha2(-/-) mice. We found that AMPKalpha was phosphorylated in atrophic muscles following denervation. In addition, deletion of AMPKalpha2 significantly attenuated denervation induced skeletal muscle wasting and protein degradation, as evidenced by preserved muscle mass and myofiber area, as well as lower levels of ubiquitinated protein, Atrogin-1 and MuRF-1 expression, and LC3-II/I ratio in tibial anterior (TA) muscles. Interestingly, the phosphorylated FoxO3a at Ser253 was significantly decreased in atrophic TA muscles, which was preserved in AMPKalpha2(-/-) mice. Collectively, our data support the notion that the activation of AMPKalpha2 contributes to the atrophic effects of denervation. |
