Involvement of M-cadherin in terminal differentiation of skeletal muscle cells

1995 ◽  
Vol 108 (9) ◽  
pp. 2973-2981 ◽  
Author(s):  
M. Zeschnigk ◽  
D. Kozian ◽  
C. Kuch ◽  
M. Schmoll ◽  
A. Starzinski-Powitz
Keyword(s):  
Cell Cycle ◽  
Skeletal Muscle ◽  
Cell Adhesion ◽  
Troponin T ◽  
Terminal Differentiation ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Myogenic Cells ◽  
Calcium Dependent ◽  
Tissue Organization

Cadherins are a gene family encoding calcium-dependent cell adhesion proteins which are thought to act in the establishment and maintenance of tissue organization. M-cadherin, one member of the family, has been found in myogenic cells of somitic origin during embryogenesis and in the adult. These findings have suggested that M-cadherin is involved in the regulation of morphogenesis of skeletal muscle cells. Therefore, we investigated the function of M-cadherin in the fusion of myoblasts into myotubes (terminal differentiation) in cell culture. Furthermore, we tested whether M-cadherin might influence (a) the expression of troponin T, a typical marker of biochemical differentiation of skeletal muscle cells, and (b) withdrawal of myoblasts from the cell cycle (called terminal commitment). The studies were performed by using antagonistic peptides which correspond to sequences of the putative M-cadherin binding domain. Analogous peptides of N-cadherin have previously been shown to interfere functionally with the N-cadherin-mediated cell adhesion. In the presence of antagonistic M-cadherin peptides, the fusion of myoblasts into myotubes was inhibited. Analysis of troponin T revealed that it was downregulated at the protein level although its mRNA was still detectable. In addition, withdrawal from the cell cycle typical for terminal commitment of muscle cells was not complete in fusion-blocked myogenic cells. Finally, expression of M-cadherin antisense RNA reducing the expression of the endogenous M-cadherin protein interfered with the fusion process of myoblasts. Our data imply that M-cadherin-mediated myoblast interaction plays an important role in terminal differentiation of skeletal muscle cells.

NF-κB activation by depolarization of skeletal muscle cells depends on ryanodine and IP3 receptor-mediated calcium signals

2007 ◽  
Vol 292 (5) ◽  
pp. C1960-C1970 ◽  
Author(s):  
Juan Antonio Valdés ◽  
Jorge Hidalgo ◽  
José Luis Galaz ◽  
Natalia Puentes ◽  
Mónica Silva ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Calcium Release ◽  
Ryanodine Receptors ◽  
Field Potential ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Ip3 Receptor ◽  
Pharmacological Agents ◽  
Calcium Dependent ◽  
Element Binding Protein

Depolarization of skeletal muscle cells by either high external K+ or repetitive extracellular field potential pulses induces calcium release from internal stores. The two components of this release are mediated by either ryanodine receptors or inositol 1,4,5-trisphosphate (IP3) receptors and show differences in kinetics, amplitude, and subcellular localization. We have reported that the transcriptional regulators including ERKs, cAMP/Ca2+-response element binding protein, c- fos, c- jun, and egr-1 are activated by K+-induced depolarization and that their activation requires IP3-dependent calcium release. We presently describe the activation of the nuclear transcription factor NF-κB in response to depolarization by either high K+ (chronic) or electrical pulses (fluctuating). Calcium transients of relative short duration activate an NF-κB reporter gene to an intermediate level, whereas long-lasting calcium increases obtained by prolonged electrical stimulation protocols of various frequencies induce maximal activation of NF-κB. This activation is independent of extracellular calcium, whereas calcium release mediated by either ryanodine or IP3 receptors contribute in all conditions tested. NF-κB activation is mediated by IκBα degradation and p65 translocation to the nucleus. Partial blockade by N-acetyl-l-cysteine, a general antioxidant, suggests the participation of reactive oxygen species. Calcium-dependent signaling pathways such as those linked to calcineurin and PKC also contribute to NF-κB activation by depolarization, as assessed by blockade through pharmacological agents. These results suggest that NF-κB activation in skeletal muscle cells is linked to membrane depolarization and depends on the duration of elevated intracellular calcium. It can be regulated by sequential activation of calcium release mediated by the ryanodine and by IP3 receptors.

scholarly journals Both Membrane Depolarization And IL-6 Induce Calcium-Dependent Hsp70 Expression In Skeletal Muscle Cells

2009 ◽  
Vol 96 (3) ◽  
pp. 121a-122a
Author(s):  
Gonzalo Jorquera ◽  
Nevenka Juretic ◽  
Alejandra Espinosa ◽  
Enrique Jaimovich ◽  
Nora Riveros
Keyword(s):  
Skeletal Muscle ◽  
Muscle Cells ◽  
Membrane Depolarization ◽  
Skeletal Muscle Cells ◽  
Hsp70 Expression ◽  
Calcium Dependent

scholarly journals Oncogenic Ras-Induced Proliferation Requires Autocrine Fibroblast Growth Factor 2 Signaling in Skeletal Muscle Cells

2001 ◽  
Vol 152 (6) ◽  
pp. 1301-1306 ◽  
Author(s):  
Yuri V. Fedorov ◽  
R. Scott Rosenthal ◽  
Bradley B. Olwin
Keyword(s):  
Skeletal Muscle ◽  
Ectopic Expression ◽  
Terminal Differentiation ◽  
Biological Response ◽  
Muscle Cells ◽  
Sodium Chlorate ◽  
Skeletal Muscle Cells ◽  
Specific Gene ◽  
Fibroblast Growth ◽  
Oncogenic Ras

Constitutively activated Ras proteins are associated with a large number of human cancers, including those originating from skeletal muscle tissue. In this study, we show that ectopic expression of oncogenic Ras stimulates proliferation of the MM14 skeletal muscle satellite cell line in the absence of exogenously added fibroblast growth factors (FGFs). MM14 cells express FGF-1, -2, -6, and -7 and produce FGF protein, yet they are dependent on exogenously supplied FGFs to both maintain proliferation and repress terminal differentiation. Thus, the FGFs produced by these cells are either inaccessible or inactive, since the endogenous FGFs elicit no detectable biological response. Oncogenic Ras-induced proliferation is abolished by addition of an anti–FGF-2 blocking antibody, suramin, or treatment with either sodium chlorate or heparitinase, demonstrating an autocrine requirement for FGF-2. Oncogenic Ras does not appear to alter cellular export rates of FGF-2, which does not possess an NH2-terminal or internal signal peptide. However, oncogenic Ras does appear to be involved in releasing or activating inactive, extracellularly sequestered FGF-2. Surprisingly, inhibiting the autocrine FGF-2 required for proliferation has no effect on oncogenic Ras-mediated repression of muscle-specific gene expression. We conclude that oncogenic Ras-induced proliferation of skeletal muscle cells is mediated via a unique and novel mechanism that is distinct from Ras-induced repression of terminal differentiation and involves activation of extracellularly localized, inactive FGF-2.

scholarly journals Proline Isomerase Pin1 Represses Terminal Differentiation and Myocyte Enhancer Factor 2C Function in Skeletal Muscle Cells

2010 ◽  
Vol 285 (45) ◽  
pp. 34518-34527 ◽  
Author(s):  
Alessandro Magli ◽  
Cecilia Angelelli ◽  
Massimo Ganassi ◽  
Fiorenza Baruffaldi ◽  
Vittoria Matafora ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Terminal Differentiation ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Myocyte Enhancer Factor ◽  
Enhancer Factor

scholarly journals Calcium-dependent Regulation of CytochromecGene Expression in Skeletal Muscle Cells

1999 ◽  
Vol 274 (14) ◽  
pp. 9305-9311 ◽  
Author(s):  
Damien Freyssenet ◽  
Martino Di Carlo ◽  
David A. Hood
Keyword(s):  
Skeletal Muscle ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Calcium Dependent

scholarly journals Troponin in embryonic chick skeletal muscle cells in vitro. An immunoelectron microscope study.

1979 ◽  
Vol 81 (1) ◽  
pp. 59-66 ◽  
Author(s):  
T Obinata ◽  
Y Shimada ◽  
R Matsuda
Keyword(s):  
Skeletal Muscle ◽  
Troponin T ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Regulatory Proteins ◽  
Embryonic Chick ◽  
Thin Filaments ◽  
Adult Chicken ◽  
Chicken Muscles

The fine structurel distribution of troponin on thin filaments in developing myofibrils was investigated by the use of immunoelectron microscopy. Embryonic chick skeletal muscle cells grown in vitro were treated with antibodies against each of the troponin components (troponin T, I, and C) from adult chicken muscles. Each antibody was distributed along the thin filaments with a period of 38 nm. It is concluded that these newly synthesized regulatory proteins are assembled at their characteristic position from the initial phases of myofibrillogenesis.

scholarly journals MiR-22-3p Inhibits Proliferation and Promotes Differentiation of Skeletal Muscle Cells by Targeting IGFBP3 in Hu Sheep

Animals ◽  
2022 ◽  
Vol 12 (1) ◽  
pp. 114
Author(s):  
Shan Wang ◽  
Xiukai Cao ◽  
Ling Ge ◽  
Yifei Gu ◽  
Xiaoyang Lv ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Skeletal Muscle ◽  
Growth And Development ◽  
Muscle Cells ◽  
Bioinformatic Analysis ◽  
C2c12 Cells ◽  
Skeletal Muscle Cells ◽  
Luciferase Reporter ◽  
Reporter System ◽  
Hu Sheep

The growth and development of skeletal muscle require a series of regulatory factors. MiRNA is a non-coding RNA with a length of about 22 nt, which can inhibit the expression of mRNA and plays an important role in the growth and development of muscle cells. The role of miR-22-3p in C2C12 cells and porcine skeletal muscle has been reported, but it has not been verified in Hu sheep skeletal muscle. Through qPCR, CCK-8, EdU and cell cycle studies, we found that overexpression of miR-22-3p inhibited proliferation of skeletal muscle cells (p < 0.01). The results of qPCR and immunofluorescence showed that overexpression of miR-22-3p promoted differentiation of skeletal muscle cells (p < 0.01), while the results of inhibiting the expression of miR-22-3p were the opposite. These results suggested that miR-22-3p functions in growth and development of sheep skeletal muscle cells. Bioinformatic analysis with mirDIP, miRTargets, and RNAhybrid software suggested IGFBP3 was the target of miR-22-3p, which was confirmed by dual-luciferase reporter system assay. IGFBP3 is highly expressed in sheep skeletal muscle cells. Overexpression of IGFBP3 was found to promote proliferation of skeletal muscle cells indicated by qPCR, CCK-8, EdU, and cell cycle studies (p < 0.01). The results of qPCR and immunofluorescence experiments proved that overexpression of IGFBP3 inhibited differentiation of skeletal muscle cells (p < 0.01), while the results of interfering IGFBP3 with siRNA were the opposite. These results indicate that miR-22-3p is involved in proliferation and differentiation of skeletal muscle cells by targeting IGFBP3.

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