Skeletal muscle development in normal and double‐muscled cattle

Martyn, Julie; Bass, J. J.; Oldham, Jenny M.

doi:10.1002/ar.a.20140

Cited by 19 publications

(13 citation statements)

References 34 publications

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“…Considering the fetal programming of skeletal muscle development [9], [12], these findings are consistent with generally medium to high heritabilities reported for postnatal myofibre size and muscle mass in mammals, including bovine [18], [19], [24], [50], [51]. Since myotubes are immature myofibres that decrease in size as myogenesis progresses [52], both the predominant contribution of the paternal genome to variation in fast myotube cross sectional area (CSA), and the predominant contribution of the maternal genome to variation in fast myofibre CSA ( Figure 2 ), indicate specific roles of maternal and paternal genomes in myofibre differentiation and maturation.…”

Section: Discussionsupporting

confidence: 85%

Maternal and Paternal Genomes Differentially Affect Myofibre Characteristics and Muscle Weights of Bovine Fetuses at Midgestation

et al. 2013

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Postnatal myofibre characteristics and muscle mass are largely determined during fetal development and may be significantly affected by epigenetic parent-of-origin effects. However, data on such effects in prenatal muscle development that could help understand unexplained variation in postnatal muscle traits are lacking. In a bovine model we studied effects of distinct maternal and paternal genomes, fetal sex, and non-genetic maternal effects on fetal myofibre characteristics and muscle mass. Data from 73 fetuses (Day153, 54% term) of four genetic groups with purebred and reciprocal cross Angus and Brahman genetics were analyzed using general linear models. Parental genomes explained the greatest proportion of variation in myofibre size of Musculus semitendinosus (80–96%) and in absolute and relative weights of M. supraspinatus, M. longissimus dorsi, M. quadriceps femoris and M. semimembranosus (82–89% and 56–93%, respectively). Paternal genome in interaction with maternal genome (P<0.05) explained most genetic variation in cross sectional area (CSA) of fast myotubes (68%), while maternal genome alone explained most genetic variation in CSA of fast myofibres (93%, P<0.01). Furthermore, maternal genome independently (M. semimembranosus, 88%, P<0.0001) or in combination (M. supraspinatus, 82%; M. longissimus dorsi, 93%; M. quadriceps femoris, 86%) with nested maternal weight effect (5–6%, P<0.05), was the predominant source of variation for absolute muscle weights. Effects of paternal genome on muscle mass decreased from thoracic to pelvic limb and accounted for all (M. supraspinatus, 97%, P<0.0001) or most (M. longissimus dorsi, 69%, P<0.0001; M. quadriceps femoris, 54%, P<0.001) genetic variation in relative weights. An interaction between maternal and paternal genomes (P<0.01) and effects of maternal weight (P<0.05) on expression of H19, a master regulator of an imprinted gene network, and negative correlations between H19 expression and fetal muscle mass (P<0.001), suggested imprinted genes and miRNA interference as mechanisms for differential effects of maternal and paternal genomes on fetal muscle.

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Section: Discussionsupporting

confidence: 85%

Maternal and Paternal Genomes Differentially Affect Myofibre Characteristics and Muscle Weights of Bovine Fetuses at Midgestation

et al. 2013

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“…On the other hand, Girgenrath et al (2005) showed that MSTN deficiency in mouse caused up-regulation of faster MyHC isoforms and down-regulation of MyHCslow in both fast-(extensor digitorum longus) and slow-type (soleus) muscles. Moreover, percentages of slow-type muscle fibers of the vastus latelaris and vastus medialis muscles of prenatal calves are lower in the DM than in the NM (Martyn et al 2004). Moreover, percentages of slow-type muscle fibers of the vastus latelaris and vastus medialis muscles of prenatal calves are lower in the DM than in the NM (Martyn et al 2004).…”

Section: Discussionmentioning

confidence: 89%

Muscle type‐specific effect of myostatin deficiency on myogenic regulatory factor expression in adult double‐muscled Japanese Shorthorn cattle

Muroya

Watanabe

Hayashi

et al. 2009

Animal Science Journal

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To clarify muscle type-specific effect of myostatin on myogenic regulatory factors (MRFs), we examined mRNA expression of MRFs in five skeletal muscles of normal (NM) and myostatin-deficient double-muscled (DM) adult Japanese Shorthorn cattle by quantitative reverse-transcribed PCR. Among the four MRFs, namely, Myf5, MyoD, myogenin, and MRF4, MyoD expression was different among the muscles of the DM cattle (P < 0.01) but not of the NM cattle. Meanwhile, MyoD expression was significantly elevated only in masseter (MS) muscle in the DM cattle due to the myostatin deficiency (P < 0.05). Myf5 and MRF4 expression in semitendinosus (ST) was higher in the DM than in the NM cattle (P < 0.05). According to analysis of myosin heavy chain (MyHC) isoform expression, more MyHC-2x and -2a and less -slow isoforms were expressed in the longissimus and ST muscles compared to the MS muscle in both cattle (P < 0.05), but no significant difference in MyHC expression was observed between the NM and DM cattle. Taken together, myostatin has influences on Myf5 and MRF4 expression in faster-type muscles and on MyoD expression in slower-type muscles, suggesting a possible muscle type-specific effect of myostatin in skeletal muscle growth and maintenance.

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“…It is, however, remarkable that myostatin-null mice and cattle have a lower fat mass than the wild types (13,14). Similarly, a human child with an inactivating mutation in the myostatin gene was strikingly lean (56).…”

Section: Discussionmentioning

confidence: 99%

The Effects of Myostatin on Adipogenic Differentiation of Human Bone Marrow-derived Mesenchymal Stem Cells Are Mediated through Cross-communication between Smad3 and Wnt/β-Catenin Signaling Pathways

Guo

Flanagan

Jasuja

et al. 2008

Journal of Biological Chemistry

101

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The effects of myostatin on adipogenic differentiation are poorly understood, and the underlying mechanisms are unknown. We determined the effects of human recombinant myostatin protein on adipogenesis of bone marrow-derived human mesenchymal stem cells (hMSCs) and adipose tissuederived preadipocytes. For both progenitor cell types, differentiation in the presence of myostatin caused a dose-dependent reduction of lipid accumulation and diminished incorporation of exogenous fatty acid into cellular lipids. Myostatin significantly down-regulated the expression of adipocyte markers PPAR␥, C/EBP␣, leptin, and aP2, but not C/EBP␤. Overexpression of PPAR␥, but not C/EBP␤, blocked the inhibitory effects of myostatin on adipogenesis. Myostatin induced phosphorylation of Smad3 in hMSCs; knockdown of Smad3 by RNAi or inhibition of its upstream kinase by an Alk5 inhibitor blocked the inhibitory effect of myostatin on adipogenesis in hMSCs, implying an important role of Smad3 activation in this event. Furthermore, myostatin enhanced nuclear translocation of ␤-catenin and formation of the Smad3-␤-catenin-TCF4 complex, together with the altered expression of a number of Wnt/␤-catenin pathway genes in hMSCs. The inhibitory effects of myostatin on adipogenesis were blocked by RNAi silencing of ␤-catenin and diminished by overexpression of dominant-negative TCF4. The conclusion is that myostatin inhibited adipogenesis in human bone marrow-derived mesenchymal stem cells and preadipocytes. These effects were mediated, in part, by activation of Smad3 and cross-communication of the TGF␤/Smad signal to Wnt/␤-catenin/TCF4 pathway, leading to down-regulation of PPAR␥.Whereas the role of myostatin in the regulation of skeletal muscle mass in animals has been widely recognized (1-8), its effects on adipogenesis are poorly understood. Inactivating mutations of the myostatin gene in a number of mammalian species are associated with hypermuscularity and decreased fat mass (9 -13). Similarly, myostatin knockout mice are characterized by a lower fat mass than wild-type controls (14, 15). These in vivo observations have led to speculation that myostatin promotes adipogenesis. However, the data on the effects of myostatin on fat mass and metabolism are conflicting. Transgenic mice that hyperexpress myostatin protein either systemically or in the skeletal muscle have increased fat mass (5), whereas adipose-specific hyperexpression of myostatin leads to reduced fat mass and improved insulin sensitivity (16). Mice bearing tumor cells that hyperexpress myostatin experience loss of lean as well as fat mass (17); it is unclear whether the loss of fat mass is a consequence of myostatin hyperexpression or the tumor-associated cachexia.In vitro studies using various cell lines also have yielded inconsistent results. Some studies have reported that myostatin inhibits adipogenic differentiation of adipocyte precursor cell lines of murine, bovine, and human origins (16,18,19), whereas others have reported promotion of adipogenic differentiation by recombin...

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Skeletal muscle development in normal and double‐muscled cattle

Cited by 19 publications

References 34 publications

Maternal and Paternal Genomes Differentially Affect Myofibre Characteristics and Muscle Weights of Bovine Fetuses at Midgestation

Maternal and Paternal Genomes Differentially Affect Myofibre Characteristics and Muscle Weights of Bovine Fetuses at Midgestation

Muscle type‐specific effect of myostatin deficiency on myogenic regulatory factor expression in adult double‐muscled Japanese Shorthorn cattle

The Effects of Myostatin on Adipogenic Differentiation of Human Bone Marrow-derived Mesenchymal Stem Cells Are Mediated through Cross-communication between Smad3 and Wnt/β-Catenin Signaling Pathways

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