Discovery of a follistatin-derived myostatin inhibitory peptide |
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| Institution: | 1. Department of Bio-science and Engineering, Shibaura Institute of Technology, Japan;2. Department of Health and Nutrition, Tokyo Kasei Gakuin University, Japan;3. Department of Agrobioscience, Graduate School of Agricultural Science, Kobe University, Japan;1. Biopharmaceutical Lab, College of Life Science, Northeast Agricultural University, Harbin, China;2. Key Laboratory of Agricultural Biological Functional Gene, Northeast Agricultural University, Harbin, P.R. China |
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| Abstract: | Follistatin is well known as an inhibitor of transforming growth factor (TGF)-β superfamily ligands including myostatin and activin A. Myostatin, a negative regulator of muscle growth, is a promising target with which to treat muscle atrophic diseases. Here, we focused on the N-terminal domain (ND) of follistatin (Fst) that interacts with the type I receptor binding site of myostatin. Through bioassay of synthetic ND-derived fragment peptides, we identified DF-3, a new myostatin inhibitory 14-mer peptide which effectively inhibits myostatin, but fails to inhibit activin A or TGF-β1, in an in vitro luciferase reporter assay. Injected intramuscularly, DF-3 significantly increases skeletal muscle mass in mice and consequently, it can serve as a platform for development of muscle enhancement based on myostatin inhibition. |
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| Keywords: | Follistatin Myostatin Inhibitor Synthetic peptide Muscle mass enhancer |
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