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Callipyge sheep exhibit postnatal muscle hypertrophy due to the up-regulation of  DLK1  and/or  RTL1 . The up-regulation of  PARK7  was identified in hypertrophied muscles by microarray analysis and further validated by quantitative PCR. The expression of PARK7 in hypertrophied muscle of callipyge lambs was confirmed to be up-regulated at the protein level. PARK7 was previously identified to positively regulate PI3K/AKT pathway by suppressing the phosphatase activity of PTEN in mouse fibroblasts. The purpose of this study was to investigate the effects of PARK7 in muscle growth and protein accretion in response to IGF1. Primary myoblasts isolated from  Park7  (+/+) and  Park7  (−/−) mice were used to examine the effect of differential expression of  Park7 . The  Park7  (+/+) myotubes had significantly larger diameters and more total sarcomeric myosin expression than  Park7  (−/−) myotubes. IGF1 treatment increased the mRNA abundance of  Myh4, Myh7 and Myh8  between 20-40% in  Park7  (+/+) myotubes relative to  Park7  (− / −). The level of AKT phosphorylation was increased in  Park7  (+/+) myotubes at all levels of IGF1 supplementation. After removal of IGF1, the  Park7  (+/+) myotubes maintained higher AKT phosphorylation through 3 hours. PARK7 positively regulates the PI3K/AKT pathway by inhibition of PTEN phosphatase activity in skeletal muscle. The increased PARK7 expression can increase protein synthesis and result in myotube hypertrophy. These results support the hypothesis that elevated expression of  PARK7  in callipyge muscle would increase levels of AKT activity to cause hypertrophy in response to the normal IGF1 signaling in rapidly growing lambs. Increasing expression of PARK7 could be a novel mechanism to increase protein accretion and muscle growth in livestock or help improve muscle mass with disease or aging.

Park7 Expression Influences Myotube Size and Myosin Expression in Muscle