Cross-talk between transcriptional regulation by thyroid hormone and myogenin: new aspects of the Ca2+-dependent expression of the fast-type sarcoplasmic reticulum Ca2+-ATPase

Thelen, Marc; Simonides, Warner S.; Muller, Alice; Hardeveld, C. van

doi:10.1042/bj3290131

Cited by 16 publications

(9 citation statements)

References 51 publications

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“…Using methods of somatic gene transfer, a recent study suggested that myogenin can enhance the oxidative capacities in adult myofibres of adult animals [31]. Moreover, a moderate increase in intracellular Ca 2+ levels, as observed during tonic motor nerve activity, leads to increased myogenin levels in cultured myotubes [116]. This finding suggests a link between intracellular Ca 2+ levels, calcineurin activity and myogenin expression as previously suggested during muscle differentiation [37].…”

Section: Molecular Mechanisms Modulating Muscle Phenotype During Endumentioning

confidence: 76%

Interaction between signalling pathways involved in skeletal muscle responses to endurance exercise

Koulmann

Bigard

2006

Pflugers Arch - Eur J Physiol

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The purpose of this review is to summarise the latest literature on the signalling pathways involved in transcriptional modulations of genes that encode contractile and metabolic proteins in response to endurance exercise. A special attention has been paid to the cooperation between signalling pathways and coordinated expression of protein families that establish myofibre phenotype. Calcium acts as a second messenger in skeletal muscle during exercise, conveying neuromuscular activity into changes in the transcription of specific genes. Three main calcium-triggered regulatory pathways acting through calcineurin, Ca(2+)-calmodulin-dependent protein kinases (CaMK) and Ca(2+)-dependent protein kinase C, transduce alterations in cytosolic calcium concentration to target genes. Calcineurin signalling, the most important of these Ca(2+)-dependent pathways, stimulates the activation of many slow-fibre gene expression, including genes encoding proteins involved in contractile process, Ca(2+) uptake and energy metabolism. It involves the interaction between multiple transcription factors and the collaboration of other Ca(2+)-dependent CaMKs. Although members of mitogen-activated protein kinase (MAPK) pathways are activated during exercise, their integration into other signalling pathways remains largely unknown. The peroxisome proliferator-activated receptor gamma (PPARgamma) coactivator-1alpha (PGC-1alpha) constitutes a pivotal factor of the circuitry which coordinates mitochondrial biogenesis and which couples to the expression of contractile and metabolic genes with prolonged exercise.

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Section: Molecular Mechanisms Modulating Muscle Phenotype During Endumentioning

confidence: 76%

Interaction between signalling pathways involved in skeletal muscle responses to endurance exercise

Koulmann

Bigard

2006

Pflugers Arch - Eur J Physiol

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“…Both cell lines did not react with a significant myotube atrophy after a 3-day treatment, and T 3 receptor analysis excluded receptor deficiency as a cause. Furthermore, in both myogenic cell lines, cross talk between T 3 -induced gene expression and contractile activity determining muscle phenotype has been reported (32,33). In both cell lines, metabolic effects of T 3 have been reported, e.g., upregulation of the sarco(endo)plasmic reticulum Ca 2ϩ -ATPases in C 2 C 12 myotubes and induction of uncoupling protein 3 in L6 myotubes (21,40).…”

Section: Discussionmentioning

confidence: 98%

Quantification of hormone-induced atrophy of large myotubes from C₂C₁₂ and L6 cells: atrophy-inducible and atrophy-resistant C₂C₁₂ myotubes

Sultan¹,

Henkel²,

Terlou³

et al. 2006

American Journal of Physiology-Cell Physiology

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Myofiber atrophy is the final outcome of muscle wasting induced by catabolic factors such as glucocorticoids and thyroid hormones. We set up an in vitro system to define the catabolic reaction based on myotube atrophy. Both mouse C(2)C(12) and rat L6 cells were used. C(2)C(12) myotube formation was improved by replacing horse serum with the serum substitute Ultroser G. A new method was developed to quantify size changes of large (0.5-1 mm) myotubes only, excluding remaining myoblasts and small myotubes. Dexamethasone reduced myotube size by 30% in L6 but not in C(2)C(12) myotubes. Expression of the glucocorticoid receptor was twofold higher in L6 myotubes than in C(2)C(12) myotubes. In both cell lines, 3,3',5-triiodo-l-thyronine (T(3)) did not induce a significant size reduction. Expression of the major T(3) receptor (T(3)Rbeta1) was higher in L6 myotubes. We investigated whether the changes in myotube size are related to changes in atrogin-1 expression, as this enzyme is thought to be a key factor in the initiation of muscle atrophy. Dexamethasone induced a twofold increase of atrogin-1 mRNA; again, only L6 myotubes were susceptible. Interestingly, atrogin-1 expression in Ultroser G-fused C(2)C(12) myotubes was lower than that in horse serum-fused myotubes. Furthermore, dexamethasone treatment increased atrogin-1 expression only in horse serum-fused myotubes but not in Ultroser G-fused myotubes. Ultroser G-induced fusion may result in atrophy-resistant C(2)C(12) myotubes. Therefore, C(2)C(12) myotubes offer an ideal system in which to study skeletal muscle atrophy because, depending on differentiation conditions, C(2)C(12) cells produce atrophy-inducible and atrophy-resistant myotubes.

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“…Several lines of evidence have implicated myogenin in the fast-to-slow fiber-type shift (7,15,26,37,47). In cultured myotubes, a moderate increase in [Ca 2ϩ ] i induced a fast-to-slow fiber-type shift and enhanced the protein expression level of myogenin but not other myogenic factors (45). In the fast-twitch muscle of hypothyroid rats, shifting to a slow direction by CLFS increased the expression of myogenin with unaltered MyoD levels (37).…”

Section: Discussionmentioning

confidence: 99%

Continuous mild heat stress induces differentiation of mammalian myoblasts, shifting fiber type from fast to slow

Yamaguchi

Suzuki²,

Arai

et al. 2010

American Journal of Physiology-Cell Physiology

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Yamaguchi T, Suzuki T, Arai H, Tanabe S, Atomi Y. Continuous mild heat stress induces differentiation of mammalian myoblasts, shifting fiber type from fast to slow. Am J Physiol Cell Physiol 298: C140 -C148, 2010. First published July 15, 2009; doi:10.1152/ajpcell.00050.2009.-Local hyperthermia has been widely used as physical therapy for a number of diseases such as inflammatory osteoarticular disorders, tendinitis, and muscle injury. Local hyperthermia is clinically applied to improve blood and lymphatic flow to decrease swelling of tissues (e.g., skeletal muscle). As for muscle repair following injury, the mechanisms underlying the beneficial effects of hyperthermia-induced muscle repair are unknown. In this study, we investigated the direct effects of continuous heat stress on the differentiation of cultured mammalian myoblasts. Compared with control cultures grown at 37°C, incubation at 39°C (continuous mild heat stress; CMHS) enhanced myotube diameter, whereas myotubes were poorly formed at 41°C by primary human skeletal muscle culture cells, human skeletal muscle myoblasts (HSMMs), and C2C12 mouse myoblasts. In HSMMs and C2C12 cells exposed to CMHS, mRNA and protein levels of myosin heavy chain (MyHC) type I were increased compared with the control cultures. The mRNA level of MyHC IIx was unaltered in HSMMs and decreased in C2C12 cells, compared with cells that were not exposed to heat stress. These results indicated a fast-to-slow fiber-type shift in myoblasts. We also examined upstream signals that might be responsible for the fast-to-slow shift of fiber types. CMHS enhanced the mRNA and protein levels of peroxisome proliferator-activated receptor-␥ coactivator (PGC)-1␣ in HSMMS and C2C12 cells but not the activities of MAPKs (ERK1/2 and p38 MAPK) in HSMMs and C2C12 cells. These data suggest that CMHS induces a fast-to-slow fiber-type shift of mammalian myoblasts through PGC-1␣.

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Cross-talk between transcriptional regulation by thyroid hormone and myogenin: new aspects of the Ca2+-dependent expression of the fast-type sarcoplasmic reticulum Ca2+-ATPase

Cited by 16 publications

References 51 publications

Interaction between signalling pathways involved in skeletal muscle responses to endurance exercise

Interaction between signalling pathways involved in skeletal muscle responses to endurance exercise

Quantification of hormone-induced atrophy of large myotubes from C₂C₁₂ and L6 cells: atrophy-inducible and atrophy-resistant C₂C₁₂ myotubes

Continuous mild heat stress induces differentiation of mammalian myoblasts, shifting fiber type from fast to slow

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Cross-talk between transcriptional regulation by thyroid hormone and myogenin: new aspects of the Ca2+-dependent expression of the fast-type sarcoplasmic reticulum Ca2+-ATPase

Cited by 16 publications

References 51 publications

Interaction between signalling pathways involved in skeletal muscle responses to endurance exercise

Interaction between signalling pathways involved in skeletal muscle responses to endurance exercise

Quantification of hormone-induced atrophy of large myotubes from C2C12 and L6 cells: atrophy-inducible and atrophy-resistant C2C12 myotubes

Continuous mild heat stress induces differentiation of mammalian myoblasts, shifting fiber type from fast to slow

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Quantification of hormone-induced atrophy of large myotubes from C₂C₁₂ and L6 cells: atrophy-inducible and atrophy-resistant C₂C₁₂ myotubes