Development of the excitation-contraction coupling machinery and its relation to myofibrillogenesis in human iPSC-derived skeletal myocytes

Lainé, Jeanne; Skoglund, Gunnar; Fournier, Emmanuel; Tabti, Nacira

doi:10.1186/s13395-017-0147-5

Cited by 27 publications

(26 citation statements)

References 39 publications

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“…Apoptosis was down-regulated with exercise training, as evidenced by reduced cytochrome c release from SS mitochondria and attenuated Bax protein levels in the mKO mice. Proteins of the autophagy pathway, including Parkin, Beclin-1, and LC3-II were significantly upregulated in the WT mice with training, as shown in other models of chronic exercise 45 – 47 . In contrast, training reduced the already elevated levels of these proteins in mKO mice toward levels observed in the WT trained mice.…”

Section: Discussionsupporting

confidence: 56%

The Role of p53 in Determining Mitochondrial Adaptations to Endurance Training in Skeletal Muscle

Beyfuss

Erlich

Triolo

et al. 2018

Sci Rep

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p53 plays an important role in regulating mitochondrial homeostasis. However, it is unknown whether p53 is required for the physiological and mitochondrial adaptations with exercise training. Furthermore, it is also unknown whether impairments in the absence of p53 are a result of its loss in skeletal muscle, or a secondary effect due to its deletion in alternative tissues. Thus, we investigated the role of p53 in regulating mitochondria both basally, and under the influence of exercise, by subjecting C57Bl/6J whole-body (WB) and muscle-specific p53 knockout (mKO) mice to a 6-week training program. Our results confirm that p53 is important for regulating mitochondrial content and function, as well as proteins within the autophagy and apoptosis pathways. Despite an increased proportion of phosphorylated p53 (Ser15) in the mitochondria, p53 is not required for training-induced adaptations in exercise capacity or mitochondrial content and function. In comparing mouse models, similar directional alterations were observed in basal and exercise-induced signaling modifications in WB and mKO mice, however the magnitude of change was less pronounced in the mKO mice. Our data suggest that p53 is required for basal mitochondrial maintenance in skeletal muscle, but is not required for the adaptive responses to exercise training.

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Section: Discussionsupporting

confidence: 56%

The Role of p53 in Determining Mitochondrial Adaptations to Endurance Training in Skeletal Muscle

Beyfuss

Erlich

Triolo

et al. 2018

Sci Rep

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“…Fasting had no effect on the isometric force-frequency relationship at baseline or under any of the tested conditions in the EDL (Fig 2A) or soleus (Fig 2B), indicating reduced carbohydrate pool size did not alter excitation-contraction coupling. Specific force values for both muscles were consistent with those obtained previously [21]. Additionally, we observed characteristic reductions in maximal specific force following the O 2 protocols (and completely impaired force production following the N 2 protocols) in both muscles (Fig 2A and 2B).…”

Section: Plos Onesupporting

confidence: 90%

“…to restrict muscles to stored fuel supplies. The bath solution was a modified Krebs Ringer solution PLOS ONE described previously [21]. All muscles were dissected and mounted within 15 mins of sacrifice.…”

Section: Measurement Of Muscle Mechanical Functionmentioning

confidence: 99%

Effects of fasting on isolated murine skeletal muscle contractile function during acute hypoxia

et al. 2020

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Stored muscle carbohydrate supply and energetic efficiency constrain muscle functional capacity during exercise and are influenced by common physiological variables (e.g. age, diet, and physical activity level). Whether these constraints affect overall functional capacity or the timing of muscle energetic failure during acute hypoxia is not known. We interrogated skeletal muscle contractile properties in two anatomically distinct rodent hindlimb muscles that have well characterized differences in energetic efficiency (locomotory-extensor digitorum longus (EDL) and postural-soleus muscles) following a 24 hour fasting period that resulted in substantially reduced muscle carbohydrate supply. 180 mins of acute hypoxia resulted in complete energetic failure in all muscles tested, indicated by: loss of force production, substantial reductions in total adenosine nucleotide pool intermediates, and increased adenosine nucleotide degradation product-inosine monophosphate (IMP). These changes occurred in the absence of apparent myofiber structural damage assessed histologically by both transverse section and whole mount. Fasting and the associated reduction of the available intracellular carbohydrate pool (~50% decrease in skeletal muscle) did not significantly alter the timing to muscle functional impairment or affect the overall force/work capacities of either muscle type. Fasting resulted in greater passive tension development in both muscle types, which may have implications for the design of pre-clinical studies involving optimal timing of reperfusion or administration of precision therapeutics.

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“…Ca V 1.1 is the voltage sensor for skeletal muscle EC coupling [ 35 ]. Similar to the role of Ca V 1.2 in heart and smooth muscle, Ca V 1.1 senses the depolarization of the muscle cell during bursts of action potentials and leads to a rapid increase of the myoplasmic free calcium concentration, which in turn triggers shortening of the contractile elements and force production.…”

Section: Ca V 11’s Role In Skeletal Muscle Excitamentioning

confidence: 99%

Skeletal muscle CaV1.1 channelopathies

Flucher

2020

Pflugers Arch - Eur J Physiol

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Ca V 1.1 is specifically expressed in skeletal muscle where it functions as voltage sensor of skeletal muscle excitation-contraction (EC) coupling independently of its functions as L-type calcium channel. Consequently, all known Ca V 1.1-related diseases are muscle diseases and the molecular and cellular disease mechanisms relate to the dual functions of Ca V 1.1 in this tissue. To date, four types of muscle diseases are known that can be linked to mutations in the CACNA1S gene or to splicing defects. These are hypo-and normokalemic periodic paralysis, malignant hyperthermia susceptibility, Ca V 1.1-related myopathies, and myotonic dystrophy type 1. In addition, the Ca V 1.1 function in EC coupling is perturbed in Native American myopathy, arising from mutations in the Ca V 1.1-associated protein STAC3. Here, we first address general considerations concerning the possible roles of Ca V 1.1 in disease and then discuss the state of the art regarding the pathophysiology of the Ca V 1.1-related skeletal muscle diseases with an emphasis on molecular disease mechanisms.

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Development of the excitation-contraction coupling machinery and its relation to myofibrillogenesis in human iPSC-derived skeletal myocytes

Cited by 27 publications

References 39 publications

The Role of p53 in Determining Mitochondrial Adaptations to Endurance Training in Skeletal Muscle

The Role of p53 in Determining Mitochondrial Adaptations to Endurance Training in Skeletal Muscle

Effects of fasting on isolated murine skeletal muscle contractile function during acute hypoxia

Skeletal muscle CaV1.1 channelopathies

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