Mus musculus
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA92785 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:1) 144 intact-mass and top-down raw LC-MS and LC-MS/MS files (myoblast and myotube, 3 biological replicates, 6 fractions, 2 top-down MS/MS technical replicates and 2 MS1-only technical replicates) from 12% GELFrEE fractions of C2C12 mitochondrial extracts. 2) 12 intact-mass raw LC-MS files from unfractionated C2C12 mitochondrial extracts (myoblast and myotube, 3 biological replicates, 2 MS1-only technical replicates). 3) 12 bottom-up raw LC-MS/MS files from unfractionated C2C12 mitochondrial extracts digested with trypsin (myoblast and myotube, 3 biological replicates, 2 technical replicates).
2018-05-16 | MSV000082366 | MassIVE
Project description:Murine Myoblast C2C12 Cells: Control vs. Mybbp1a Knockdown
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Project description:Gene Expression Profiling of C2C12 Myoblast Differentiation
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Project description:<p>Cells use glycolytic intermediates for anabolism e.g., via the serine synthesis and pentose phosphate pathways. However, we still understand poorly how these metabolic pathways contribute to skeletal muscle cell biomass generation. The first aim of this study was therefore to identify enzymes that limit protein synthesis, myotube size and proliferation in skeletal muscle cells. We inhibited key enzymes of glycolysis, the pentose phosphate pathway and serine synthesis pathway to evaluate their importance in C2C12 myotube protein synthesis. Based on the results of this first screen, we then focused on the serine synthesis pathway enzyme phosphoglycerate dehydrogenase (PHGDH). We used two different PHGDH inhibitors and mouse C2C12 and human primary muscle cells to study the importance and function of the PHGDH. Both myoblasts and myotubes incorporated glucose-derived carbon into proteins, RNA and lipids and we showed that PHGDH is essential in these processes. PHGDH inhibition decreased protein synthesis, myotube size and myoblast proliferation without cytotoxic effects. The decreased protein synthesis in response to PHGDH inhibition appears to occur mainly mTORC1 dependently as was evident from experiments with insulin-like growth factor 1 and rapamycin. Further metabolomics analyses revealed that PHGDH inhibition accelerated glycolysis and altered amino acid, nucleotide and lipid metabolism. Lastly, we found that supplementing an antioxidant and redox modulator N-acetylcysteine partially rescued the decreased protein synthesis and mTORC1 signaling during PHGDH inhibition. The data suggest that PHGDH activity is critical for skeletal muscle cell biomass generation from glucose, and that it regulates protein synthesis and mTORC1 signaling.</p>
2025-03-21 | MTBLS8854 | MetaboLights
Project description:C2C12 murine myoblast cell line and 48 h 10 uM BIO treated C2C12 cellulate
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Project description: Not available
| S-EPMC8784167 | biostudies-literature
Project description:Expression data from C2C12 mouse myoblast with treatment actinomycin D
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Project description: Not available
| S-EPMC11335981 | biostudies-literature
Project description:Wnt/β-catenin signaling is involved in various aspects of skeletal muscle development and regeneration. In addition, Wnt3a and β-catenin are required for muscle-specific gene transcription in embryonic carcinoma cells and satellite-cell proliferation during adult skeletal muscle regeneration. Downstream targets of canonical Wnt signaling are cyclin D1 and c-myc. However, both target genes are suppressed during differentiation of mouse myoblast cells, C2C12. Underlying molecular mechanisms of β-catenin signaling during myogenic differentiation remain unknown. Using C2C12 cells, we examined intracellular signaling and gene transcription during myoblast proliferation and differentiation. We confirmed that several Wnt signaling components, including Wnt9a, Sfrp2 and porcupine, were consistently upregulated in differentiating C2C12 cells. Troponin T-positive myotubes were decreased by Wnt3a overexpression, but not Wnt4. TOP/FOP reporter assays revealed that co-expression with Wnt4 reduced Wnt3a-induced luciferase activity, suggesting that Wnt4 signaling counteracted Wnt3a signaling in myoblasts. FH535, a small-molecule inhibitor of β-catenin/Tcf complex formation, reduced basal β-catenin in cytoplasm and decreased myoblast proliferation. K252a, a protein kinase inhibitor, increased membrane-bound β-catenin and enhanced myoblast fusion. Treatments with K252a or Wnt4 resulted in increased cytoplasmic vesicles containing phosphorylated β-catenin (Tyr654) during myogenic differentiation. These results suggest that various Wnt ligands control subcellular β-catenin localization, which regulate myoblast proliferation and myotube formation. Wnt signaling via β-catenin likely acts as a molecular switch that regulates the transition from cell proliferation to myogenic differentiation.
2011-07-15 | GSE30077 | GEO
Project description:Msx1 ChIP-Seq from C2C12 murine myoblast cells expressing Flag-Msx1 protein
| PRJNA142145 | ENA