Effects of Glycine on Protein Synthesis and Degradation in C2C12 Muscle Cells
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Glycine is an amino acid that is used for the synthesis of muscle proteins. In the present study, we conducted an experiment to determine the optimal amount of glycine for C2C12 cells to be synthesized and prevent degradation. The experiment required the cells to be cultured in medium of radioactive phenylalanine 3H-labeled phenylalanine (*Phe) and one of 5 concentrations of glycine (10, 100, 250, 500, or 1000 µM). By counting the radioactivity of *Phe in protein, we were able to determine protein synthesis in these cells, and determined what concentration of glycine worked best. Our findings show that 100 to 1000 µM of glycine stimulated protein synthesis in C2C12 cells in a dose-dependent manner (P<0.05). C2C12 cells were also used to determine protein degradation in the presence of 0 to 1000 µM glycine. Specifically, the cells were cultured in *Phe and 0, 100, 250, 500 0r 1000 µM glycine. After culturing for 24 h, the release of *Phe from the prelabeled protein was determined as an indicator of protein degradation. Glycine (0-1000 µM) reduced protein degradation in a dose-dependent manner. These results indicate that glycine is an anabolic amino acid to enhance protein accretion in muscle cells. Supported by USDA-NIFA grants and Texas A&M University.
SubjectmL Milliliter µL Microliter mM Millimolar Gly Glycine [3H]-Phe Tritium treated Phenylalanine TCA Trichloroacetic acid DMEM/F-12 Dulbeco’s Modified Eagle Medium NaOH Sodium Hydroxide mTORC1 mammalian target of rapamycin complex 1
Long, David William (2018). Effects of Glycine on Protein Synthesis and Degradation in C2C12 Muscle Cells. Undergraduate Research Scholars Program. Available electronically from