Functional verification of a porcine myostatin propeptide mutant

文献类型： 外文期刊

第一作者： Ma, Dezun

作者： Ma, Dezun;Jiang, Shengwang;Gao, Pengfei;Wang, Qingqing;Xiao, Gaojun;Cui, Wentao;Qian, Lili;Cai, Chunbo;Yang, Jinzeng

作者机构：

关键词： Myostatin;Propeptide;Mutation;Muscle mass;Transgenic mice

期刊名称：TRANSGENIC RESEARCH （ 影响因子：2.788； 五年影响因子：2.377 ）

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收录情况： SCI

摘要： Myostatin is a member of TGF-beta 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.

分类号： R394

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