Myostatin inactivation induces a similar muscle molecular signature in double-muscled cattle as in mice

Chelh, Ilham; Picard, Brigitte; Hocquette, Jean-François; Cassar-Malek, Isabelle

doi:10.1017/s1751731110001862

Cited by 26 publications

(14 citation statements)

References 50 publications

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“…The in vitro comparison of myotube size showed Park7 (+/+) myotubes had a bigger size and higher myosin expression than Park7 (−/−) myotubes, but no significant change in the fusion index, which indicates Park7 expression affects myotube hypertrophy (increased myofiber diameter), not hyperplasia (increased myofiber number). These results support the proposed models that elevated PARK7 expression is part of the physiological mechanism for increased muscle growth in callipyge lambs and myostatin null mice and cattle [16], [46], [47].…”

Section: Discussionsupporting

confidence: 89%

“…In addition to callipyge lambs [16], transcriptomic and proteomic analyses in quadriceps muscles in myostatin-null mice, which exhibit a muscle hyperplasia phenotype, found elevated levels of PARK7 and phosphorylation of AKT [46]. Further work by the same group in double-muscled cattle also showed higher PARK7 expression in double-muscled fetuses compared to normal controls [47]. In food animal agriculture, there is a need to identify genes that can increase muscle growth and protein accretion.…”

Section: Introductionmentioning

confidence: 99%

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Park7 Expression Influences Myotube Size and Myosin Expression in Muscle

Waddell

Kuang

et al. 2014

PLoS ONE

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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.

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Section: Discussionsupporting

confidence: 89%

Section: Introductionmentioning

confidence: 99%

Park7 Expression Influences Myotube Size and Myosin Expression in Muscle

Waddell

Kuang

et al. 2014

PLoS ONE

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“…McPherron and Lee [ 17 ] reported the similarity in phenotypes of DM cattle and mice, carrying a targeted deletion of the MSTN gene (MSTN null mice, MSTN knock-out mice), suggesting that MSTN performs the same biological function in these two species. This similarity in biological processes between cattle and mice has been confirmed [ 18 ]. This statement means that MSTN may be a useful target for genetic manipulation in other farm animals.…”

Section: Origin Of Dm Animals: the Unraveling Of The Myostatin Genmentioning

confidence: 67%

Double Muscling in Cattle: Genes, Husbandry, Carcasses and Meat

Fiems¹

2012

Animals

112

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Simple SummarySelection for an increased meatiness in beef cattle has resulted in double-muscled (DM) animals, owing to the inactivation of the myostatin gene. These animals are characterized by an excellent conformation and an extremely high carcass yield, coinciding with a reduced organ mass. As a consequence, voluntary feed intake is reduced, but feed efficiency is considerably improved, although maintenance requirements are not clearly reduced. DM animals are more susceptible to respiratory disease, stress and dystocia, requiring extra attention for accommodation and welfare. Carcasses of DM animals are very lean, and intramuscular fat content is low. The fatty acid profile is different when compared with non-DM animals, containing less saturated fatty acids. Collagen content of the meat is lower, so that meat from double-muscled animals is mostly more tender. However, meat tenderness, color and juiciness are not always improved. A different metabolism as a consequence of faster glycolytic myofibers can be partly responsible for this phenomenon. DM animals are interesting for the producer and butcher, and beneficial for the consumer, if an appropriate nutrition and accommodation, and adequate slaughter conditions are taken into account.AbstractMolecular biology has enabled the identification of the mechanisms whereby inactive myostatin increases skeletal muscle growth in double-muscled (DM) animals. Myostatin is a secreted growth differentiation factor belonging to the transforming growth factor-β superfamily. Mutations make the myostatin gene inactive, resulting in muscle hypertrophy. The relationship between the different characteristics of DM cattle are defined with possible consequences for livestock husbandry. The extremely high carcass yield of DM animals coincides with a reduction in the size of most vital organs. As a consequence, DM animals may be more susceptible to respiratory disease, urolithiasis, lameness, nutritional stress, heat stress and dystocia, resulting in a lower robustness. Their feed intake capacity is reduced, necessitating a diet with a greater nutrient density. The modified myofiber type is responsible for a lower capillary density, and it induces a more glycolytic metabolism. There are associated changes for the living animal and post-mortem metabolism alterations, requiring appropriate slaughter conditions to maintain a high meat quality. Intramuscular fat content is low, and it is characterized by more unsaturated fatty acids, providing healthier meat for the consumer. It may not always be easy to find a balance between the different disciplines underlying the livestock husbandry of DM animals to realize a good performance and health and meat quality.

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“…Furthermore, TCTP has also been shown to be one of several proteins upregulated in the hyper-muscular mouse and bovine myostatin knockout models [40, 41]. This finding is of particular interest because myostatin signaling is known to inhibit muscle growth, in part, via the inhibition of mTOR and protein synthesis [42–44].…”

Section: Introductionmentioning

confidence: 99%

Insights into the role and regulation of TCTP in skeletal muscle

et al. 2016

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The translationally controlled tumor protein (TCTP) is upregulated in a range of cancer cell types, in part, by the activation of the mechanistic target of rapamycin (mTOR). Recently, TCTP has also been proposed to act as an indirect activator of mTOR. While it is known that mTOR plays a major role in the regulation of skeletal muscle mass, very little is known about the role and regulation of TCTP in this post-mitotic tissue. This study shows that muscle TCTP and mTOR signaling are upregulated in a range of mouse models (mdx mouse, mechanical load-induced hypertrophy, and denervation- and immobilization-induced atrophy). Furthermore, the increase in TCTP observed in the hypertrophic and atrophic conditions occurred, in part, via a rapamycin-sensitive mTOR-dependent mechanism. However, the overexpression of TCTP was not sufficient to activate mTOR signaling (or increase protein synthesis) and is thus unlikely to take part in a recently proposed positive feedback loop with mTOR. Nonetheless, TCTP overexpression was sufficient to induce muscle fiber hypertrophy. Finally, TCTP overexpression inhibited the promoter activity of the muscle-specific ubiquitin proteasome E3-ligase, MuRF1, suggesting that TCTP may play a role in inhibiting protein degradation. These findings provide novel data on the role and regulation of TCTP in skeletal muscle in vivo.

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Myostatin inactivation induces a similar muscle molecular signature in double-muscled cattle as in mice

Cited by 26 publications

References 50 publications

Park7 Expression Influences Myotube Size and Myosin Expression in Muscle

Park7 Expression Influences Myotube Size and Myosin Expression in Muscle

Double Muscling in Cattle: Genes, Husbandry, Carcasses and Meat

Insights into the role and regulation of TCTP in skeletal muscle

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