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.

Regulation of inducible nitric oxide synthase expression in L6 rat skeletal muscle cells

1997 ◽  
Vol 272 (1) ◽  
pp. C35-C40 ◽  
Author(s):  
S. Okuda ◽  
F. Kanda ◽  
Y. Kawahara ◽  
K. Chihara
Keyword(s):  
Nitric Oxide ◽  
Skeletal Muscle ◽  
Protein Kinase ◽  
Nitric Oxide Synthase ◽  
Tyrosine Kinase ◽  
Muscle Cells ◽  
Inos Expression ◽  
Skeletal Muscle Cells ◽  
Rat Skeletal Muscle ◽  
Oxide Synthase

Cytokine-stimulated expression of inducible type of nitric oxide synthase (iNOS) seems to be regulated by various signal pathways in a cell-specific manner. In this study, we examined how it was regulated in L6 rat skeletal muscle cells. In L6 cells, the combination of interleukin-1 beta and interferon-gamma induced a marked accumulation of nitrite, a stable metabolite of nitric oxide. In parallel with this reaction, iNOS mRNA expression was achieved at a maximum between 3 and 6 h, and iNOS protein was detectable at 6 h and peaked at 24 h after stimulation. Tyrosine kinase inhibitors, herbimycin A, and genistein suppressed cytokine-induced iNOS expression and nitrite production. Forskolin, an adenosine 3',5'-cyclic monophosphate-dependent protein kinase (PKA) activator, and phorbol 12-myristate 13-acetate, a protein kinase C (PKC)-activating phorbol ester, enhanced these cytokine-induced reactions. These results indicate that iNOS expression by cytokines is mediated via a protein tyrosine kinase-dependent pathway and is positively modulated by both PKA- and PKC-dependent pathways in this cell type.

scholarly journals Involvement of Tyrosine Kinase Activity in 1α,25(OH)2-vitamin D3Signal Transduction in Skeletal Muscle Cells

2000 ◽  
Vol 275 (46) ◽  
pp. 36021-36028 ◽  
Author(s):  
Susana Morelli ◽  
Claudia Buitrago ◽  
Guillermo Vazquez ◽  
Ana R. De Boland ◽  
Ricardo Boland
Keyword(s):  
Skeletal Muscle ◽  
Tyrosine Kinase ◽  
Kinase Activity ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Tyrosine Kinase Activity

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 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

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.

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