Myoblast structure affects subsequent skeletal myotube morphology and sarcomere assembly

Berendse, M.; Grounds, Miranda D.; Lloyd, Catriona

doi:10.1016/j.yexcr.2003.07.004

Cited by 43 publications

(33 citation statements)

References 35 publications

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“…45,46 In contrast to that observed in plated cultures, the early cessation of differentiation may have resulted from exposure to mechanical strain or interaction of the cells with extracellular matrix constituents. It was also possible that the observed lack of progression through differentiation was simply the result of spatial restriction imposed by collagen fibrils in the ETCs.…”

Section: Discussionmentioning

confidence: 99%

Cardiac Conduction through Engineered Tissue

Choi

Stamm

Hammer

et al. 2006

The American Journal of Pathology

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In children, interruption of cardiac atrioventricular (AV) electrical conduction can result from congenital defects, surgical interventions, and maternal autoimmune diseases during pregnancy. Complete AV conduction block is typically treated by implanting an electronic pacemaker device, although long-term pacing therapy in pediatric patients has significant complications. As a first step toward developing a substitute treatment, we implanted engineered tissue constructs in rat hearts to create an alternative AV conduction pathway. We found that skeletal muscle-

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Section: Discussionmentioning

confidence: 99%

Cardiac Conduction through Engineered Tissue

Choi

Stamm

Hammer

et al. 2006

The American Journal of Pathology

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“…13). Organelle migration and subcellular partitioning are particularly important during muscle differentiation when dramatic changes in cytoskeletal structure and myofibril organisation occur to convert a simple cell into a highly organised differentiated cell in which accurate spatial orientation of sub-cellular components is a requisite for function (Berendse et al, 2003;Takekura et al, 2001). The abundance of muscle-specific nesprin-2 isoforms also supports a structural role.…”

Section: Discussionmentioning

confidence: 99%

Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle

Zhang

Ragnauth

Skepper³

et al. 2005

Journal of Cell Science

241

294

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Nesprin-2 is a multi-isomeric, modular protein composed of variable numbers of spectrin-repeats linked to a C-terminal transmembrane domain and/or to N-terminal paired calponin homology (CH) domains. The smaller isoforms of nesprin-2 co-localize with and bind lamin A and emerin at the inner nuclear envelope (NE). In SW-13 cells, which lack lamin A/C, nesprin-2 epitopes and emerin were both mislocalized and formed aggregates in the endoplasmic reticulum (ER). The larger isoforms and other CH-domain-containing isoforms co-localize with heterochromatin within the nucleus and are also present at the outer NE and in multiple cytoplasmic compartments. Nesprin-2 isoforms relocalize during in vitro muscle differentiation of C2C12 myoblasts to the sarcomere of myotubes. Immunogold electron microscopy using antibodies specific for three different epitopes detected nesprin-2 isoforms at multiple locations including intranuclear foci, both membranes of the NE, mitochondria, sarcomeric structures and plasma membrane foci. In adult skeletal muscle, confocal immunolocalization studies demonstrated that nesprin-2 epitopes were present at the Z-line and were also associated with the sarcoplasmic reticulum (SR) in close apposition to SERCA2. These data suggest that nesprin-2 isoforms form a linking network between organelles and the actin cytoskeleton and thus may be important for maintaining sub-cellular spatial organisation. Moreover, its association at the NE with lamin and emerin, the genes mutated in Emery-Dreifuss muscular dystrophy, suggests a mechanism to explain how disruption of the NE leads to muscle dysfunction.

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“…During myoblasts differentiation, myoblasts fuse together to form myotube (Berendse et al, 2003) and contractile gene expression, such as β-actin, is up-regulated (Gunning et al, 1987;Spangenburg et al, 2004). Survival, growth and differentiation of myoblasts are systemically regulated by distinct growth factor-regulated signaling pathways.…”

Section: Discussionmentioning

confidence: 99%

SIMVASTATIN REDUCES INSULIN-LIKE GROWTH FACTOR-1 SIGNALING IN DIFFERENTIATING C2C12 MOUSE MYOBLAST CELLS IN AN HMG-CoA REDUCTASE INHIBITION-INDEPENDENT MANNER

Ogura¹,

Tanaka²,

Nakata³

et al. 2007

J. Toxicol. Sci.

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-Inhibitors of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase occasionally cause myopathy characterized by weakness, pain, and elevated serum creatine phosphokinase (CK). In this study, we investigated the effects of simvastatin, an HMG-CoA reductase inhibitor, on the viability and insulin-like growth factor-1 (IGF-1) signaling in differentiating C2C12 mouse myoblast cells. Simvastatin decreased cell viability and CK activity, a marker of myogenesis, in differentiating cells in a dosedependent manner. Although the simvastatin-induced decrease in viability in proliferating and differentiated cells was completely abolished by mevalonate or geranylgeranyl-pyrophosphate, the inhibitory effects of simvastatin in differentiating cells were not abolished by mevalonate or isoprenoid derivatives of mevalonate. Moreover, the sensitivity of differentiating cells to simvastatin regarding cell viability was about 7 times higher than that of proliferating cells. After induction of differentiation in the presence of 1 μM simvastatin for 2 days, IGF-1-induced activation of ERK1/2 and Akt was significantly decreased. Although mRNA expression of the IGF-1 receptor β-chain (IGF-1Rβ) did not change, protein level of the 200 kDa IGF-1Rβ precursor was significantly increased by simvastatin in a dose-dependent manner. Mevalonate did not abolish the effect of simvastatin on IGF-1Rβ expression. These results suggest that simvastatin decreases IGF-1 signaling via a regulation of the post-translational modification of IGF-1Rβ in an HMG-CoA reductase inhibition-independent manner.

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Myoblast structure affects subsequent skeletal myotube morphology and sarcomere assembly

Cited by 43 publications

References 35 publications

Cardiac Conduction through Engineered Tissue

Cardiac Conduction through Engineered Tissue

Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle

SIMVASTATIN REDUCES INSULIN-LIKE GROWTH FACTOR-1 SIGNALING IN DIFFERENTIATING C2C12 MOUSE MYOBLAST CELLS IN AN HMG-CoA REDUCTASE INHIBITION-INDEPENDENT MANNER

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