scholarly journals Ku70 regulates Bax-mediated pathogenesis in laminin- 2-deficient human muscle cells and mouse models of congenital muscular dystrophy

2009 ◽  
Vol 18 (23) ◽  
pp. 4467-4477 ◽  
Author(s):  
V. K. Vishnudas ◽  
J. B. Miller
Keyword(s):  
Muscular Dystrophy ◽  
Mouse Models ◽  
Congenital Muscular Dystrophy ◽  
Muscle Cells ◽  
Human Muscle ◽  
Human Muscle Cells

scholarly journals A novel isoform of myosin alkali light chain isolated from human muscle cells

1989 ◽  
Vol 17 (24) ◽  
pp. 10496-10496 ◽  
Author(s):  
Katrin Zimmermann ◽  
Anna Starzinski-Powitz
Keyword(s):  
Light Chain ◽  
Muscle Cells ◽  
Human Muscle ◽  
Human Muscle Cells

scholarly journals Fibroblast growth factor 9 (FGF9) inhibits myogenic differentiation of C2C12 and human muscle cells

Cell Cycle ◽  
2019 ◽  
Vol 18 (24) ◽  
pp. 3562-3580 ◽  
Author(s):  
Jian Huang ◽  
Kun Wang ◽  
Lora A. Shiflett ◽  
Leticia Brotto ◽  
Lynda F. Bonewald ◽  
...  
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Myogenic Differentiation ◽  
Muscle Cells ◽  
Human Muscle ◽  
Fibroblast Growth ◽  
Human Muscle Cells

Insulin and insulinlike growth factor receptors and responses in cultured human muscle cells

1986 ◽  
Vol 251 (5) ◽  
pp. E611-E615 ◽  
Author(s):  
M. Shimizu ◽  
C. Webster ◽  
D. O. Morgan ◽  
H. M. Blau ◽  
R. A. Roth
Keyword(s):  
Insulin Receptor ◽  
Biological Effects ◽  
Muscle Cells ◽  
Model System ◽  
Human Muscle ◽  
Acid Analogue ◽  
Igf I ◽  
Specific Receptors ◽  
Human Muscle Cells ◽  
Biological Actions

Specific receptors for insulinlike growth factors I and II (IGF-I and IGF-II) were found on cultured human myoblasts and myotubes. In contrast, myotubes but not myoblasts specifically bound insulin and were stimulated by nanomolar concentrations of insulin to take up deoxyglucose. In addition, in myoblasts, physiological concentrations of IGF-I and -II and, to a lesser extent, insulin stimulated two- to threefold the uptake of the nonmetabolizable amino acid analogue methylaminoisobutyric acid (MAIB). In myotubes, uptake of MAIB was stimulated preferentially by IGF-I. Monoclonal antibodies that preferentially recognize either the insulin receptor or the IGF-I receptor were utilized to examine which receptors mediated the biological effects of these hormones. The effects of insulin on both myoblasts and myotubes appeared to be mediated in part by the insulin receptor and in part by the IGF-I receptor. In myotubes, the effects of IGF-I and -II both appeared to be mediated through the IGF-I receptor. In myoblasts, the effects of the two IGFs appeared to be in part mediated by the IGF-I receptor and in part mediated by either the IGF-II receptor or another type of IGF-I receptor. The present results suggest that cultured human muscle cells provide a useful model system in which to study the biological actions of insulin and the IGFs.

scholarly journals Regulation of glycogen metabolism in cultured human muscles by the glycogen phosphorylase inhibitor CP-91149

2004 ◽  
Vol 378 (3) ◽  
pp. 1073-1077 ◽  
Author(s):  
Carlos LERÍN ◽  
Eulàlia MONTELL ◽  
Teresa NOLASCO ◽  
Mar GARCÍA-ROCHA ◽  
Joan J. GUINOVART ◽  
...  
Keyword(s):  
Muscle Glycogen ◽  
Glycogen Phosphorylase ◽  
Glycogen Synthase ◽  
Muscle Cells ◽  
Glycogen Metabolism ◽  
Human Muscle ◽  
Insulin Dependent Diabetes ◽  
Type Ii ◽  
Insulin Dependent ◽  
Human Muscle Cells

Pharmacological inhibition of liver GP (glycogen phosphorylase), which is currently being studied as a treatment for Type II (non-insulin-dependent) diabetes, may affect muscle glycogen metabolism. In the present study, we analysed the effects of the GP inhibitor CP-91149 on non-engineered or GP-overexpressing cultured human muscle cells. We found that CP-91149 treatment decreased muscle GP activity by (1) converting the phosphorylated AMP-independent a form into the dephosphorylated AMP-dependent b form and (2) inhibiting GP a activity and AMP-mediated GP b activation. Dephosphorylation of GP was exerted, irrespective of incubation of the cells with glucose, whereas inhibition of its activity was synergic with glucose. As expected, CP-91149 impaired the glycogenolysis induced by glucose deprivation. CP-91149 also promoted the dephosphorylation and activation of GS (glycogen synthase) in non-engineered or GP-overexpressing cultured human muscle cells, but exclusively in glucose-deprived cells. However, this inhibitor did not activate GS in glucose-deprived but glycogen-replete cells overexpressing PTG (protein targeting to glycogen), thus suggesting that glycogen inhibits the CP-91149-mediated activation of GS. Consistently, CP-91149 promoted glycogen resynthesis, but not its overaccumulation. Hence, treatment with CP-91149 impairs muscle glycogen breakdown, but enhances its recovery, which may be useful for the treatment of Type II (insulin-dependent) diabetes.

Developmental regulation of myotonic dystrophy protein kinase in human muscle cells in vitro

Neuroscience ◽  
1998 ◽  
Vol 85 (1) ◽  
pp. 311-322 ◽  
Author(s):  
N Kameda ◽  
H Ueda ◽  
S Ohno ◽  
M Shimokawa ◽  
F Usuki ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Myotonic Dystrophy ◽  
Developmental Regulation ◽  
Muscle Cells ◽  
Human Muscle ◽  
Myotonic Dystrophy Protein Kinase ◽  
Human Muscle Cells
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