Differential regulation of IGF-I and IGF-II gene expression in skeletal muscle cells

2012 ◽  
Vol 373 (1-2) ◽  
pp. 107-113 ◽  
Author(s):  
Shuang Jiao ◽  
Hongxia Ren ◽  
Yun Li ◽  
Jianfeng Zhou ◽  
Cunming Duan ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Muscle Cells ◽  
Differential Regulation ◽  
Skeletal Muscle Cells ◽  
Igf I

scholarly journals Impact of Adenosine A2 Receptor Ligands on BCL2 Expression in Skeletal Muscle Cells

2021 ◽  
Vol 11 (5) ◽  
pp. 2272
Author(s):  
Mansour Haddad
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Adenosine Receptors ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Qrt Pcr ◽  
A2a Receptor ◽  
Adenosine A2a ◽  
Bcl2 Expression ◽  
Bcl2 Gene

Background: Adenosine plays the role of regulating cell differentiation, proliferation, and apoptosis in various kinds of cells through the B-cell lymphoma 2 (BCL2) pathway. Objectives: Since anti-apoptotic (BCL2) expression plays a role in controlling apoptosis in some cell lines, this study was designed to investigate whether adenosine analogue, NECA (non-selective adenosine receptors agonist), selective adenosine A2B receptor antagonist, PSB 603, and a selective adenosine A2A receptor agonist, CG21680, affect BCL2-gene expression in the skeletal muscle cells of rats. The purpose of this investigation was to test the hypothesis that CG21680 treatment would significantly intensify BCL2 gene expression in rat skeletal muscle. Methods: Flasks measuring 25 cm2 were employed in culturing the rat L6 skeletal muscle cells. After treating these differential cells, the relative mRNA expression level for the BCL2 gene, at varying conditions of treatment, was measured using quantitative reverse transcription-polymerase chain reaction (qRT-PCR). Results: From the qRT-PCR analysis results, it was concluded that BCL2 expression was markedly amplified after selective adenosine A2A receptor agonist, CGS21680 (p < 0.01) treatment. More prospective validation for the adenosine receptors’ contribution in modulating apoptosis by NECA was delivered by the outcomes from the combined pre-treatment of the cells with NECA and PSB 603. These outcomes show that when starved skeletal muscle cells are treated with a combination of NECA and 100 nM PSB 603, there was a substantial decrease in comparison to either treatment used on its own. Conclusions: This study’s results showed, for the first time, an increase in BCL2 gene expression within skeletal muscle after CGS21680 treatment. Hence, the prospective escalation in BCL2 protein expression might have a protective role to play against apoptosis and avert damage to the skeletal muscle.

scholarly journals Isolation and validation of human prepubertal skeletal muscle cells: maturation and metabolic effects of IGF-I, IGFBP-3 and TNFα

2005 ◽  
Vol 568 (1) ◽  
pp. 229-242 ◽  
Author(s):  
Malcolm Grohmann ◽  
Emily Foulstone ◽  
Gavin Welsh ◽  
Jeff Holly ◽  
Julian Shield ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Metabolic Effects ◽  
Igf I ◽  
Igfbp 3

scholarly journals Focal adhesion kinase is required for IGF-I-mediated growth of skeletal muscle cells via a TSC2/mTOR/S6K1-associated pathway

2013 ◽  
Vol 305 (2) ◽  
pp. E183-E193 ◽  
Author(s):  
Hannah Crossland ◽  
Abid A. Kazi ◽  
Charles H. Lang ◽  
James A. Timmons ◽  
Philippe Pierre ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cell Growth ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Muscle Hypertrophy ◽  
Kinase Activity ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Cell Phenotype ◽  
Igf I

Focal adhesion kinase (FAK) is an attachment complex protein associated with the regulation of muscle mass through as-of-yet unclear mechanisms. We tested whether FAK is functionally important for muscle hypertrophy, with the hypothesis that FAK knockdown (FAK-KD) would impede cell growth associated with a trophic stimulus. C2C12 skeletal muscle cells harboring FAK-targeted (FAK-KD) or scrambled (SCR) shRNA were created using lentiviral transfection techniques. Both FAK-KD and SCR myotubes were incubated for 24 h with IGF-I (10 ng/ml), and additional SCR cells (±IGF-1) were incubated with a FAK kinase inhibitor before assay of cell growth. Muscle protein synthesis (MPS) and putative FAK signaling mechanisms (immunoblotting and coimmunoprecipitation) were assessed. IGF-I-induced increases in myotube width (+41 ± 7% vs. non-IGF-I-treated) and total protein (+44 ± 6%) were, after 24 h, attenuated in FAK-KD cells, whereas MPS was suppressed in FAK-KD vs. SCR after 4 h. These blunted responses were associated with attenuated IGF-I-induced FAK Tyr397 phosphorylation and markedly suppressed phosphorylation of tuberous sclerosis complex 2 (TSC2) and critical downstream mTOR signaling (ribosomal S6 kinase, eIF4F assembly) in FAK shRNA cells (all P < 0.05 vs. IGF-I-treated SCR cells). However, binding of FAK to TSC2 or its phosphatase Shp-2 was not affected by IGF-I or cell phenotype. Finally, FAK-KD-mediated suppression of cell growth was recapitulated by direct inhibition of FAK kinase activity in SCR cells. We conclude that FAK is required for IGF-I-induced muscle hypertrophy, signaling through a TSC2/mTOR/S6K1-dependent pathway via means requiring the kinase activity of FAK but not altered FAK-TSC2 or FAK-Shp-2 binding.

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