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Biochem Biophys Res Commun. 2017 Dec 9;494(1-2):278-284. doi: 10.1016/j.bbrc.2017.10.040. Epub 2017 Oct 9.

Myostatin inhibits eEF2K-eEF2 by regulating AMPK to suppress protein synthesis.

Author information

1
Department of Animal Nutrition and Feed Science, College of Animal Science and Technology, Huazhong Agricultural University, 430070, Wuhan, China; The Cooperative Innovation Center for Sustainable Pig Production, Wuhan, 430070, Hubei, China.
2
Department of Animal Nutrition and Feed Science, College of Animal Science and Technology, Huazhong Agricultural University, 430070, Wuhan, China.
3
Department of Animal Nutrition and Feed Science, College of Animal Science and Technology, Huazhong Agricultural University, 430070, Wuhan, China; The Cooperative Innovation Center for Sustainable Pig Production, Wuhan, 430070, Hubei, China. Electronic address: weihongkui@mail.hzau.edu.cn.

Abstract

Growth of skeletal muscle is dependent on the protein synthesis, and the rate of protein synthesis is mainly regulated in the stage of translation initiation and elongation. Myostatin, a member of the transforming growth factor-β (TGF-β) superfamily, is a negative regulator of protein synthesis. C2C12 myotubes was incubated with 0, 0.01, 0.1, 1, 2, 3 μg/mL myostatin recombinant protein, and then we detected the rates of protein synthesis by the method of SUnSET. We found that high concentrations of myostatin (2 and 3 μg/mL) inhibited protein synthesis by blocking mTOR and eEF2K-eEF2 pathway, while low concentration of myostatin (0.01, 0.1 and 1 μg/mL) regulated eEF2K-eEF2 pathway activity to block protein synthesis without affected mTOR pathway, and myostatin inhibited eEF2K-eEF2 pathway through regulating AMPK pathway to suppress protein synthesis. It provided a new mechanism for myostatin regulating protein synthesis and treating muscle atrophy.

KEYWORDS:

AMPK; Myostatin; Protein synthesis; eEF2K-eEF2

PMID:
29024627
DOI:
10.1016/j.bbrc.2017.10.040
[Indexed for MEDLINE]

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