Functional verification of a porcine myostatin propeptide mutant
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Myostatin is a member of TGF-β superfamily that acts as a key negative regulator in development and growth of embryonic and postnatal muscles. In this study, the inhibitory activities of recombinant porcine myostatin propeptide and its mutated form (at the cleavage site of metalloproteinases of BMP-1/TLD family) against murine myostatin was evaluated in vivo by intraperitoneal injection into mice. Results showed that both wild type and mutated form of porcine propeptide significantly inhibited myostatin activity in vivo. The average body weight of mice receiving wild type propeptide or its mutated form increased by 12.5 % and 24.14 %, respectively, compared to mice injected with PBS, implying that the in vivo efficacy of porcine propeptide mutant is greater than its wild type propeptide. Transgenic mice expressing porcine myostatin propeptide mutant were generated to further verify the results obtained from mice injected with recombinant porcine propeptide mutant. Compared with wild type (non-transgenic) mice, relative weight of gastrocnemius, rectusfemoris, and tibialis anterior increased by 22.14 %, 34.13 %, 25.37 %, respectively, in transgenic male mice, and by 19.90 %, 42.47 %, 45.61 %, respectively, in transgenic female mice. Our data also demonstrated that the mechanism by which muscle growth enhancement is achieved by these propeptides is due to an increase in fiber sizes, not by an increase in number of fiber cells.
KeywordsMyostatin Propeptide Mutation Muscle mass Transgenic mice
This study was support by the National Natural Science Foundation of China (Grant No. 30901022) and by the Agricultural Science and Technology Innovation Program (ASTIP-IAS05). We thank Chengyi Song for providing plasmids for “Sleeping Beauty” transposon (pT2-HB) carrier and SB100 transposase. We also thank for Jinan Jiao for editing the manuscript and valuable comments and suggestions on the manuscript.
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Conflict of interest
The authors have declared that no competing interest exists.
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