Key result
Expression of mutated porcine myostatin in transgenic mice increased skeletal muscle mass by up to 53.21% and mean myofiber size by up to 61.30% due to hypertrophy rather than hyperplasia.
Over-expression of cleavage-site mutated porcine myostatin induces skeletal muscle hypertrophy rather than hyperplasia in transgenic mice.
Should not inform human therapies; leaves open myostatin inhibition for muscle-wasting disorders pending clinical trials.
Myostatin, a member of the transforming growth factor beta (TGF-β) superfamily, is a dominant inhibitor that acts to limit skeletal muscle growth and development. In this study, we generated transgenic mice that express porcine myostatin containg mutations at its cleavage site (RSRR) to evaluate its effect on muscle mass. Results showed that the weight of four skeletal muscles including gastrocnemius, rectus femoris, tibialis anterior, and pectoralis increased by 17.83 and 28.39%, 21.76 and 28.70%, 34.31 and 41.62%, 53.21 and 27.54% in transgenic male and female mice, respectively, compared to their corresponding non-transgenic control mice. Measurement of muscle fiber size and number indicated that the mean myofiber size increased by 50.73 and 61.30% in transgenic male and female mice respectively compared to the non-transgenic controls. However, there was no difference in the number of myofiber between transgenic and non-transgenic male mice. These results clearly demonstrated that the increase in skeletal muscle mass in transgenic mice is caused by hypertrophy instead of hyperplasia.
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Qian et al. (2016) studied Skeletal muscle growth. Expression of porcine myostatin mutated at its cleavage site (RSRR) vs. Non-transgenic control mice was evaluated on Skeletal muscle weight and myofiber size/number. Expression of mutated porcine myostatin in transgenic mice increased skeletal muscle mass by up to 53.21% and mean myofiber size by up to 61.30% due to hypertrophy rather than hyperplasia.
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