Knockdown of optineurin controls C2C12 myoblast differentiation via regulating myogenin and MyoD expressions

2021 ◽  
Author(s):  
Kenichi Ishikawa ◽  
Mutsuko Araki ◽  
Yoshito Nagano ◽  
Atsuko Motoda ◽  
Takeo Shishido ◽  
...  
Keyword(s):  
Myoblast Differentiation ◽  
C2c12 Myoblast

PGC-1α is associated with C2C12 Myoblast differentiation

2014 ◽  
Vol 9 (11) ◽  
pp. 1030-1036 ◽  
Author(s):  
Yaqiu Lin ◽  
Yanying Zhao ◽  
Ruiwen Li ◽  
Jiaqi Gong ◽  
Yucai Zheng ◽  
...  
Keyword(s):  
Mrna Level ◽  
Biological Significance ◽  
C2c12 Cells ◽  
Myoblast Differentiation ◽  
C2c12 Myoblast ◽  
Mrna Levels ◽  
Transfected Cells ◽  
Myosin Heavy Chain Isoform ◽  
Important Mediator

AbstractPGC-1α has been implicated as an important mediator of functional capacity of skeletal muscle. However, the role of PGC-1α in myoblast differentiation remains unexplored. In the present study, we observed a significant up-regulation of PGC-1α expression during the differentiation of murine C2C12 myoblast. To understand the biological significance of PGC-1α up-regulation in myoblast differentiation, C2C12 cells were transfected with murine PGC-1α cDNA and siRNA targeting PGC-1α, respectively. PGC-1α over-expressing clones fused to form typical myotubes with higher mRNA level of myosin heavy chain isoform I (MyHCI) and lower MyHCIIX. No obvious differentiation was observed in PGC-1α-targeted siRNA-transfected cells with marked decrement of mRNA levels of MyHCI and MyHCIIX. Furthermore, PGC-1α increased the expression of MyoD and MyoG in C2C12 cells, which controlled the commitment of precursor cells to myotubes. These results indicate that PGC-1α is associated with myoblast differentiation and elevates MyoD and MyoG expression levels in C2C12 cells.

scholarly journals MicroRNAs Regulate Cellular ATP Levels by Targeting Mitochondrial Energy Metabolism Genes during C2C12 Myoblast Differentiation

PLoS ONE ◽  
2015 ◽  
Vol 10 (5) ◽  
pp. e0127850 ◽  
Author(s):  
Puntita Siengdee ◽  
Nares Trakooljul ◽  
Eduard Murani ◽  
Manfred Schwerin ◽  
Klaus Wimmers ◽  
...  
Keyword(s):  
Energy Metabolism ◽  
Myoblast Differentiation ◽  
C2c12 Myoblast ◽  
Mitochondrial Energy Metabolism ◽  
Atp Levels

scholarly journals Proteomics-based investigation in C2C12 myoblast differentiation

2009 ◽  
Vol 53 (4) ◽  
pp. 31 ◽  
Author(s):  
L. Casadei ◽  
L. Vallorani ◽  
A.M. Gioacchini ◽  
M. Guescini ◽  
S. Burattini ◽  
...  
Keyword(s):  
Myoblast Differentiation ◽  
C2c12 Myoblast

scholarly journals Myoferlin Regulates Wnt/β-Catenin Signaling-Mediated Skeletal Muscle Development by Stabilizing Dishevelled-2 Against Autophagy

2019 ◽  
Vol 20 (20) ◽  
pp. 5130 ◽  
Author(s):  
Shunshun Han ◽  
Can Cui ◽  
Haorong He ◽  
Xiaoxu Shen ◽  
Yuqi Chen ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Atrophy ◽  
Muscle Development ◽  
Skeletal Muscle Atrophy ◽  
Myoblast Differentiation ◽  
C2c12 Myoblast ◽  
Skeletal Muscle Development ◽  
Muscle Tissues ◽  
Underlying Mechanisms ◽  
Canonical Wnt

Myoferlin (MyoF), which is a calcium/phospholipid-binding protein expressed in cardiac and muscle tissues, belongs to the ferlin family. While MyoF promotes myoblast differentiation, the underlying mechanisms remain poorly understood. Here, we found that MyoF not only promotes C2C12 myoblast differentiation, but also inhibits muscle atrophy and autophagy. In the present study, we found that myoblasts fail to develop into mature myotubes due to defective differentiation in the absence of MyoF. Meanwhile, MyoF regulates the expression of atrophy-related genes (Atrogin-1 and MuRF1) to rescue muscle atrophy. Furthermore, MyoF interacts with Dishevelled-2 (Dvl-2) to activate canonical Wnt signaling. MyoF facilitates Dvl-2 ubiquitination resistance by reducing LC3-labeled Dvl-2 levels and antagonizing the autophagy system. In conclusion, we found that MyoF plays an important role in myoblast differentiation during skeletal muscle atrophy. At the molecular level, MyoF protects Dvl-2 against autophagy-mediated degradation, thus promoting activation of the Wnt/β-catenin signaling pathway. Together, our findings suggest that MyoF, through stabilizing Dvl-2 and preventing autophagy, regulates Wnt/β-catenin signaling-mediated skeletal muscle development.

Platelet endothelial aggregation receptor-1 (PEAR1) is involved in C2C12 myoblast differentiation

2018 ◽  
Vol 366 (2) ◽  
pp. 199-204 ◽  
Author(s):  
Ya Feng Cui ◽  
Yun Qin Yan ◽  
Dan Liu ◽  
Yu Sheng Pang ◽  
Jiang Wu ◽  
...  
Keyword(s):  
Myoblast Differentiation ◽  
C2c12 Myoblast

scholarly journals p57Kip2 Stabilizes the MyoD Protein by Inhibiting Cyclin E-Cdk2 Kinase Activity in Growing Myoblasts

1999 ◽  
Vol 19 (11) ◽  
pp. 7621-7629 ◽  
Author(s):  
Emmanuel G. Reynaud ◽  
Karine Pelpel ◽  
Martine Guillier ◽  
Marie Pierre Leibovitch ◽  
Serge A. Leibovitch
Keyword(s):  
Cyclin E ◽  
Tight Binding ◽  
Dominant Negative ◽  
Myoblast Differentiation ◽  
C2c12 Myoblast ◽  
Cdk Inhibitors ◽  
Cyclin Dependent Kinase ◽  
Muscle Creatine Kinase ◽  
Mouse Muscle ◽  
Cdk2 Activity

ABSTRACT We show that expression of p57Kip2, a potent tight-binding inhibitor of several G1cyclin–cyclin-dependent kinase (Cdk) complexes, increases markedly during C2C12 myoblast differentiation. We examined the effect of p57Kip2 on the activity of the transcription factor MyoD. In transient transfection assays, transcriptional transactivation of the mouse muscle creatine kinase promoter by MyoD was enhanced by the Cdk inhibitors. In addition, p57Kip2, p21Cip1, and p27Kip1 but not p16Ink4a induced an increased level of MyoD protein, and we show that MyoD, an unstable nuclear protein, was stabilized by p57Kip2. Forced expression of p57Kip2 correlated with hypophosphorylation of MyoD in C2C12 myoblasts. A dominant-negative Cdk2 mutant arrested cells at the G1 phase transition and induced hypophosphorylation of MyoD. Furthermore, phosphorylation of MyoD by purified cyclin E-Cdk2 complexes was inhibited by p57Kip2. In addition, the NH2 domain of p57Kip2 necessary for inhibition of cyclin E-Cdk2 activity was sufficient to inhibit MyoD phosphorylation and to stabilize it, leading to its accumulation in proliferative myoblasts. Taken together, our data suggest that repression of cyclin E-Cdk2-mediated phosphorylation of MyoD by p57Kip2 could play an important role in the accumulation of MyoD at the onset of myoblast differentiation.

scholarly journals ADP-Ribosylation Factor 6 Regulates Mammalian Myoblast Fusion through Phospholipase D1 and Phosphatidylinositol 4,5-Bisphosphate Signaling Pathways

2010 ◽  
Vol 21 (14) ◽  
pp. 2412-2424 ◽  
Author(s):  
Anne-Sophie Bach ◽  
Sandrine Enjalbert ◽  
Franck Comunale ◽  
Stéphane Bodin ◽  
Nicolas Vitale ◽  
...  
Keyword(s):  
Myoblast Fusion ◽  
Myoblast Differentiation ◽  
C2c12 Myoblast ◽  
Nucleotide Exchange ◽  
Adp Ribosylation ◽  
Rac1 Activity ◽  
Phospholipase D1 ◽  
Rac1 Gtpase ◽  
Gtpase Activation ◽  
Adp Ribosylation Factor

Myoblast fusion is an essential step during myoblast differentiation that remains poorly understood. M-cadherin–dependent pathways that signal through Rac1 GTPase activation via the Rho-guanine nucleotide exchange factor (GEF) Trio are important for myoblast fusion. The ADP-ribosylation factor (ARF)6 GTPase has been shown to bind to Trio and to regulate Rac1 activity. Moreover, Loner/GEP100/BRAG2, a GEF of ARF6, has been involved in mammalian and Drosophila myoblast fusion, but the specific role of ARF6 has been not fully analyzed. Here, we show that ARF6 activity is increased at the time of myoblast fusion and is required for its implementation in mouse C2C12 myoblasts. Specifically, at the onset of myoblast fusion, ARF6 is associated with the multiproteic complex that contains M-cadherin, Trio, and Rac1 and accumulates at sites of myoblast fusion. ARF6 silencing inhibits the association of Trio and Rac1 with M-cadherin. Moreover, we demonstrate that ARF6 regulates myoblast fusion through phospholipase D (PLD) activation and phosphatidylinositol 4,5-bis-phosphate production. Together, these data indicate that ARF6 is a critical regulator of C2C12 myoblast fusion and participates in the regulation of PLD activities that trigger both phospholipids production and actin cytoskeleton reorganization at fusion sites.

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