scholarly journals tk Enzyme expression in differentiating muscle cells is regulated through an internal segment of the cellular tk gene.

1984 ◽  
Vol 4 (9) ◽  
pp. 1777-1784 ◽  
Author(s):  
G F Merrill ◽  
S D Hauschka ◽  
S L McKnight
Keyword(s):  
Skeletal Muscle ◽  
Enzyme Activity ◽  
Thymidine Kinase ◽  
Terminal Differentiation ◽  
Muscle Cells ◽  
Muscle Differentiation ◽  
Skeletal Muscle Cells ◽  
Deficient Mouse ◽  
Enzyme Expression

Thymidine kinase (tk) enzyme expression is shut down when cultured skeletal muscle cells terminally differentiate. This regulation is mediated by a rapid and specific decline in the abundance of cellular tk mRNA. tk-deficient mouse myoblasts were transformed to the tk-positive phenotype by using both the cellular tk gene of the chicken and the herpesvirus tk gene. Myoblasts transformed with the cellular tk gene effectively regulate tk enzyme activity upon terminal differentiation. Conversely, myoblasts transformed with the herpesvirus tk gene continue to express tk enzyme activity in postreplicative muscle cells. A regulated pattern of expression is retained when the promoter of the cellular tk gene is replaced by the promoter of the herpesvirus tk gene. Moreover, the cellular tk gene is appropriately regulated during terminal muscle differentiation when its 3' terminus is removed and replaced by the terminus of the viral tk gene. Thus, the element of the cellular tk gene sufficient to specify its regulation is entirely intragenic.

tk Enzyme expression in differentiating muscle cells is regulated through an internal segment of the cellular tk gene

1984 ◽  
Vol 4 (9) ◽  
pp. 1777-1784
Author(s):  
G F Merrill ◽  
S D Hauschka ◽  
S L McKnight
Keyword(s):  
Skeletal Muscle ◽  
Enzyme Activity ◽  
Thymidine Kinase ◽  
Terminal Differentiation ◽  
Muscle Cells ◽  
Muscle Differentiation ◽  
Skeletal Muscle Cells ◽  
Deficient Mouse ◽  
Enzyme Expression

Thymidine kinase (tk) enzyme expression is shut down when cultured skeletal muscle cells terminally differentiate. This regulation is mediated by a rapid and specific decline in the abundance of cellular tk mRNA. tk-deficient mouse myoblasts were transformed to the tk-positive phenotype by using both the cellular tk gene of the chicken and the herpesvirus tk gene. Myoblasts transformed with the cellular tk gene effectively regulate tk enzyme activity upon terminal differentiation. Conversely, myoblasts transformed with the herpesvirus tk gene continue to express tk enzyme activity in postreplicative muscle cells. A regulated pattern of expression is retained when the promoter of the cellular tk gene is replaced by the promoter of the herpesvirus tk gene. Moreover, the cellular tk gene is appropriately regulated during terminal muscle differentiation when its 3' terminus is removed and replaced by the terminus of the viral tk gene. Thus, the element of the cellular tk gene sufficient to specify its regulation is entirely intragenic.

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.

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 A pRb-independent mechanism preserves the postmitotic state in terminally differentiated skeletal muscle cells

2004 ◽  
Vol 167 (3) ◽  
pp. 417-423 ◽  
Author(s):  
Grazia Camarda ◽  
Francesca Siepi ◽  
Deborah Pajalunga ◽  
Camilla Bernardini ◽  
Rossella Rossi ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Dna Synthesis ◽  
Muscle Cells ◽  
Muscle Differentiation ◽  
Conditional Knockout ◽  
Skeletal Muscle Cells ◽  
Specific Gene ◽  
Pocket Protein ◽  
Independent Mechanism ◽  
Optimal Implementation

In skeletal muscle differentiation, the retinoblastoma protein (pRb) is absolutely necessary to establish definitive mitotic arrest. It is widely assumed that pRb is equally essential to sustain the postmitotic state, but this contention has never been tested. Here, we show that terminal proliferation arrest is maintained in skeletal muscle cells by a pRb-independent mechanism. Acute Rb excision from conditional knockout myotubes caused reexpression of E2F transcriptional activity, cyclin-E and -A kinase activities, PCNA, DNA ligase I, RPA, and MCM2, but did not induce DNA synthesis, showing that pRb is not indispensable to preserve the postmitotic state of these cells. Muscle-specific gene expression was significantly down-regulated, showing that pRb is constantly required for optimal implementation of the muscle differentiation program. Rb-deleted myotubes were efficiently reactivated by forced expression of cyclin D1 and Cdk4, indicating a functionally significant target other than pRb for these molecules. Finally, Rb removal induced no DNA synthesis even in pocket-protein null cells. Thus, the postmitotic state of myotubes is maintained by at least two mechanisms, one of which is pocket-protein independent.

scholarly journals Erratum to: Ranolazine promotes muscle differentiation and reduces oxidative stress in C2C12 skeletal muscle cells

Endocrine ◽  
2017 ◽  
Vol 58 (1) ◽  
pp. 46-46 ◽  
Author(s):  
Ileana Terruzzi ◽  
Anna Montesano ◽  
Pamela Senesi ◽  
Fernanda Vacante ◽  
Stefano Benedini ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Skeletal Muscle ◽  
Muscle Cells ◽  
Muscle Differentiation ◽  
Skeletal Muscle Cells ◽  
C2c12 Skeletal Muscle Cells

scholarly journals The FGF Receptor–1 Tyrosine Kinase Domain Regulates Myogenesis but Is Not Sufficient to Stimulate Proliferation

1998 ◽  
Vol 142 (1) ◽  
pp. 241-250 ◽  
Author(s):  
Arthur J. Kudla ◽  
Nathan C. Jones ◽  
R. Scott Rosenthal ◽  
Kirstin Arthur ◽  
Kari L. Clase ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Tyrosine Kinase ◽  
Muscle Cells ◽  
Muscle Differentiation ◽  
Kinase Domain ◽  
Skeletal Muscle Cells ◽  
Tyrosine Kinase Domain ◽  
Protein Kinase Activity ◽  
Skeletal Muscle Differentiation ◽  
Chimeric Receptors

Ligand-stimulated activation of FGF receptors (FGFRs) in skeletal muscle cells represses terminal myogenic differentiation. Skeletal muscle cell lines and subsets of primary cells are dependent on FGFs to repress myogenesis and maintain growth. To understand the intracellular events that transduce these signals, MM14 skeletal muscle cells were transfected with expression vectors encoding chimeric receptors. The chimeras are comprised of the PDGF β receptor (PDGFβR) extracellular domain, the FGFR-1 intracellular domain, and either the PDGFβR or FGFR-1 transmembrane domain. The chimeric receptors were autophosphorylated upon PDGF-BB stimulation and are capable of stimulating mitogen-activated protein kinase activity. Activation of the tyrosine kinase domain of either chimera repressed myogenesis, suggesting intracellular responses regulating skeletal muscle differentiation are transduced by activation of the FGFR-1 tyrosine kinase. Unexpectedly, we found that activation of either chimeric receptor failed to stimulate cellular proliferation. Thus, it appears that regulation of skeletal muscle differentiation by FGFs requires only activation of the FGFR tyrosine kinase. In contrast, stimulation of proliferation may require additional, as yet unidentified, signals involving the receptor ectodomain, the FGF ligand, and heparan sulfate either alone, or in combination.

scholarly journals Ranolazine promotes muscle differentiation and reduces oxidative stress in C2C12 skeletal muscle cells

Endocrine ◽  
2016 ◽  
Vol 58 (1) ◽  
pp. 33-45 ◽  
Author(s):  
Terruzzi Ileana ◽  
Montesano Anna ◽  
Senesi Pamela ◽  
Vacante Fernanda ◽  
Benedini Stefano ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Skeletal Muscle ◽  
Muscle Cells ◽  
Muscle Differentiation ◽  
Skeletal Muscle Cells ◽  
C2c12 Skeletal Muscle Cells

Effect of Tea Catechins on Regulation of Antioxidant Enzyme Expression in H2O2-Induced Skeletal Muscle Cells of Goat in Vitro

2011 ◽  
Vol 59 (20) ◽  
pp. 11338-11343 ◽  
Author(s):  
Rong-Zhen Zhong ◽  
Dao-Wei Zhou ◽  
Chuan-Yan Tan ◽  
Zhi-Liang Tan ◽  
Xue-Feng Han ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Antioxidant Enzyme ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Enzyme Expression ◽  
Tea Catechins
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