scholarly journals A prostaglandin alpha F2 analog protects from statin-induced myopathic changes in primary human muscle cells

2018 ◽  
Author(s):  
Stefanie Anke Grunwald ◽  
Oliver Popp ◽  
Stefanie Haafke ◽  
Nicole Jedraszczak ◽  
Ulrike Grieben ◽  
...  
Keyword(s):  
Side Effects ◽  
Muscle Cell ◽  
Cholesterol Metabolism ◽  
Plasma Cholesterol ◽  
Cholesterol Biosynthesis ◽  
Muscle Cells ◽  
Human Muscle ◽  
Proliferation And Differentiation ◽  
Pathway Analyses ◽  
Human Muscle Cells

AbstractStatin-related muscle side effects are a constant healthcare problem since patient compliance is dependent on side effects. Statins reduce plasma cholesterol levels and can prevent secondary cardiovascular disease. Although statin-induced muscle damage has been studied, preventive or curative therapies are yet to be reported.We exposed primary human muscle cell populations (n=25) to a lipophilic (simvastatin) and a hydrophilic (rosuvastatin) statin and analyzed their expressome. Data and pathway analyses included GOrilla, Reactome and DAVID. We measured mevalonate intracellularly and analyzed eicosanoid profiles secreted by human muscle cells. Functional assays included proliferation and differentiation quantification.More than 1800 transcripts and 900 proteins were differentially expressed after exposure to statins. Simvastatin had a stronger effect on the expressome than rosuvastatin, but both statins influenced cholesterol biosynthesis, fatty acid metabolism, eicosanoid synthesis, proliferation, and differentiation of human muscle cells. Cultured human muscle cells secreted ω-3 and ω-6 derived eicosanoids and prostaglandins. The ω-6 derived metabolites were found at higher levels secreted from simvastatin-treated primary human muscle cells. Eicosanoids rescued muscle cell differentiation.Our data suggest a new aspect on the role of skeletal muscle in cholesterol metabolism. For clinical practice, the addition of omega-n fatty acids could be suitable to prevent or treat statin-myopathy.

Glucose uptake in human and animal muscle cells in culture

1990 ◽  
Vol 68 (2) ◽  
pp. 536-542 ◽  
Author(s):  
Vivian Sarabia ◽  
Toolsie Ramlal ◽  
Amira Klip
Keyword(s):  
Glucose Uptake ◽  
Muscle Cell ◽  
Muscle Cells ◽  
Human Muscle ◽  
Human Cells ◽  
Mouse Muscle ◽  
Cells In Culture ◽  
Maximal Stimulation ◽  
Hexose Uptake ◽  
Human Muscle Cells

Human muscle cells were grown in culture from satellite cells present in muscle biopsies and fusion-competent clones were identified. Hexose uptake was studied in fused myotubes of human muscle cells in culture and compared with hexose uptake in myotubes of the rat L6 and mouse C2C12 muscle cell lines. Uptake of 2-deoxyglucose was saturable and showed an apparent Km of about 1.5 mM in myotubes of all three cell types. The Vmax of uptake was about 6000 pmol/(min∙mg protein) in human cells, 4000 pmol/(min∙mg protein) in mouse C2C12 muscle cells, and 500 pmol/(min∙mg protein) in L6 cells. Hexose uptake was inhibited ~90% by cytochalasin B in human, rat, and mouse muscle cell cultures. Insulin stimulated 2-deoxyglucose uptake in all three cultures. The hormone also stimulated transport of 3-O-methylglucose. The sensitivity to insulin was higher in human and C2C12 mouse myotubes (half-maximal stimulation observed at 3.5 × 10−9 M) than in rat L6 myotubes (half-maximal stimulation observed at 2.5 × 10−8 M). However, insulin (10−6 M) stimulated hexose uptake to a larger extent (2.37-fold) in L6 than in either human (1.58-fold) or mouse (1.39-fold) myotubes. It is concluded that human muscle cells grown in culture display carrier-mediated glucose uptake, with qualitatively similar characteristics to those of other muscle cells, and that insulin stimulates hexose uptake in human cells. These cultures will be instrumental in the study of human insulin resistance and in investigations on the mechanism of action of antidiabetic drugs.Key words: glucose uptake, insulin action, primary muscle cultures, L6 cells, C2 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

Stimulation of actin synthesis by cytochalasin D is specific for the isoactins normally expressed in muscle or non-muscle cells

1986 ◽  
Vol 84 (1) ◽  
pp. 253-262
Author(s):  
J. Tannenbaum ◽  
A.F. Miranda
Keyword(s):  
Muscle Cell ◽  
Cell Cultures ◽  
Muscle Cells ◽  
Cytochalasin D ◽  
Human Muscle ◽  
The State ◽  
Cytoskeletal Proteins ◽  
Developmentally Regulated ◽  
Alpha Actin ◽  
Stimulation Of

Treatment of human muscle myotube cultures with 2 microM-cytochalasin D (CD) for 6 h stimulated synthesis of both the (muscle-specific) alpha-actin and the (non-muscle) beta and gamma-actins usually expressed by these cells. In non-muscle (HEp-2) cell cultures, CD enhanced synthesis of beta and gamma-actin, but did not induce synthesis of alpha-actin, which is not normally present in these cells. Thus, synthesis of both muscle and non-muscle actins can be increased by CD, but enhancement of actin synthesis results from increases in the isoactins usually present, rather than induction of new isotypes. Comparison of CD-treated (fused) myotube cultures with (unfused) myoblast cultures indicated that beta and gamma-actin synthesis was similarly enhanced in both cultures, but that alpha-actin synthesis was stimulated to a greater extent in the myoblast cultures. Desmin synthesis was also stimulated in the myoblasts but not the myotubes, suggesting that the effect of CD on synthesis of these developmentally regulated cytoskeletal proteins (alpha-actin, desmin) might be modulated by fusion or the state of differentiation of the muscle cell.

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

scholarly journals Effects of Modulation of Glycerol Kinase Expression on Lipid and Carbohydrate Metabolism in Human Muscle Cells

2001 ◽  
Vol 277 (4) ◽  
pp. 2682-2686 ◽  
Author(s):  
Eulàlia Montell ◽  
Carlos Lerı́n ◽  
Christopher B. Newgard ◽  
Anna M. Gómez-Foix
Keyword(s):  
Carbohydrate Metabolism ◽  
Muscle Cells ◽  
Glycerol Kinase ◽  
Human Muscle ◽  
Kinase Expression ◽  
Human Muscle Cells
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