AMPK Mediates Muscle Mass Change But Not the Transition of Myosin Heavy Chain Isoforms during Unloading and Reloading of Skeletal Muscles in Mice

• Published in: International journal of molecular sciences 2018-10, Vol.19 (10), p.2954
• Main Authors: Egawa, Tatsuro, Ohno, Yoshitaka, Goto, Ayumi, Yokoyama, Shingo, Hayashi, Tatsuya, Goto, Katsumasa
• Format: Article
• Language: English
• Subjects: AMP-Activated Protein Kinases - genetics; AMP-Activated Protein Kinases - metabolism; Animals; atrophy; fiber-type; heat shock protein; Hindlimb Suspension - adverse effects; HSP72 Heat-Shock Proteins - metabolism; Male; Mice; Mice, Inbred C57BL; Muscle, Skeletal - growth & development; Muscle, Skeletal - metabolism; Muscle, Skeletal - physiopathology; Muscular Atrophy - etiology; Muscular Atrophy - metabolism; Myosin Heavy Chains - metabolism; Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha - metabolism; peroxisome proliferator-activated receptor gamma coactivator 1-α (PGC1α); Protein Isoforms - metabolism; regrowth; sirtuin 1 (SIRT1); Sirtuin 1 - metabolism
• ISSN: 1422-0067; 1422-0067
• DOI: 10.3390/ijms19102954

5'AMP-activated protein kinase (AMPK) plays an important role in the regulation of skeletal muscle mass and fiber-type distribution. However, it is unclear whether AMPK is involved in muscle mass change or transition of myosin heavy chain (MyHC) isoforms in response to unloading or increased loading. Here, we checked whether AMPK controls muscle mass change and transition of MyHC isoforms during unloading and reloading using mice expressing a skeletal-muscle-specific dominant-negative AMPKα1 (AMPK-DN). Fourteen days of hindlimb unloading reduced the soleus muscle weight in wild-type and AMPK-DN mice, but reduction in the muscle mass was partly attenuated in AMPK-DN mice. There was no difference in the regrown muscle weight between the mice after 7 days of reloading, and there was concomitantly reduced AMPKα2 activity, however it was higher in AMPK-DN mice after 14 days reloading. No difference was observed between the mice in relation to the levels of slow-type MyHC I, fast-type MyHC IIa/x, and MyHC IIb isoforms following unloading and reloading. The levels of 72-kDa heat-shock protein, which preserves muscle mass, increased in AMPK-DN-mice. Our results indicate that AMPK mediates the progress of atrophy during unloading and regrowth of atrophied muscles following reloading, but it does not influence the transition of MyHC isoforms.