Quantitative Proteome Analysis in Response to Glucose Concentration in C2C12 Myotubes
Glucose is important for the maintenance of muscle function; however, it is still unclear how changes in glucose concentration affect muscle. Here, we analyzed the effect of glucose concentration on protein expression under different glucose concentration media in C2C12 myotubes. First, we performed...
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2022-01-01
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author | Ayano Kato Iori Sakakibara Taku Fukushima Kosuke Sugiura Tomoya Fukawa Takeshi Nikawa Takayuki Uchida |
author_facet | Ayano Kato Iori Sakakibara Taku Fukushima Kosuke Sugiura Tomoya Fukawa Takeshi Nikawa Takayuki Uchida |
author_sort | Ayano Kato |
collection | DOAJ |
description | Glucose is important for the maintenance of muscle function; however, it is still unclear how changes in glucose concentration affect muscle. Here, we analyzed the effect of glucose concentration on protein expression under different glucose concentration media in C2C12 myotubes. First, we performed proteome analysis in C2C12 myotubes cultured in Low (1.0 g/L), Medium (2.0 g/L), and High (4.5 g/L) glucose media. Proteome analysis revealed 113 proteins were significantly changed in group cultured in Low or Medium glucose media compared to group cultured in High glucose media. Furthermore, glycolysis, oxidative phosphorylation, and fatty acid metabolism were increased in the Medium and Low groups. Among these pathways, HK2, PFKP, NDUFA11, and FABP3 were especially upregulated proteins in Low and Medium groups. In this context, ATP production in C2C12 myotubes cultured in Low and Medium glucose media was increased. There was no significant change in myotubes morphology and myogenic differentiation factors in all groups. Finally, we examined the effect on glucose concentration in culture media on myosin isoforms expression by qRT-PCR. As a result, <i>Myh2</i> and <i>Myh4</i> were significantly increased in Low and Medium conditions. Altogether, Low and Medium glucose conditions induced <i>Myh</i> expression probably via enhancement glucose utilization. |
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spelling | doaj.art-5f7714659cac4a36a9513293d4950b002023-11-23T15:59:30ZengMDPI AGApplied Sciences2076-34172022-01-01123155310.3390/app12031553Quantitative Proteome Analysis in Response to Glucose Concentration in C2C12 MyotubesAyano Kato0Iori Sakakibara1Taku Fukushima2Kosuke Sugiura3Tomoya Fukawa4Takeshi Nikawa5Takayuki Uchida6Department of Nutritional Physiology, Institute of Medical Nutrition, Tokushima University Graduate School, 3-18-15 Kuramoto-cho, Tokushima 770-8503, JapanDepartment of Nutritional Physiology, Institute of Medical Nutrition, Tokushima University Graduate School, 3-18-15 Kuramoto-cho, Tokushima 770-8503, JapanDepartment of Nutritional Physiology, Institute of Medical Nutrition, Tokushima University Graduate School, 3-18-15 Kuramoto-cho, Tokushima 770-8503, JapanDepartment of Orthopedics, Institute of Medical Biosciences, Tokushima University Graduate School, Tokushima 770-8503, JapanDepartment of Urology, Tokushima University Graduate School of Biomedical Sciences, Tokushima 770-8503, JapanDepartment of Nutritional Physiology, Institute of Medical Nutrition, Tokushima University Graduate School, 3-18-15 Kuramoto-cho, Tokushima 770-8503, JapanDepartment of Nutritional Physiology, Institute of Medical Nutrition, Tokushima University Graduate School, 3-18-15 Kuramoto-cho, Tokushima 770-8503, JapanGlucose is important for the maintenance of muscle function; however, it is still unclear how changes in glucose concentration affect muscle. Here, we analyzed the effect of glucose concentration on protein expression under different glucose concentration media in C2C12 myotubes. First, we performed proteome analysis in C2C12 myotubes cultured in Low (1.0 g/L), Medium (2.0 g/L), and High (4.5 g/L) glucose media. Proteome analysis revealed 113 proteins were significantly changed in group cultured in Low or Medium glucose media compared to group cultured in High glucose media. Furthermore, glycolysis, oxidative phosphorylation, and fatty acid metabolism were increased in the Medium and Low groups. Among these pathways, HK2, PFKP, NDUFA11, and FABP3 were especially upregulated proteins in Low and Medium groups. In this context, ATP production in C2C12 myotubes cultured in Low and Medium glucose media was increased. There was no significant change in myotubes morphology and myogenic differentiation factors in all groups. Finally, we examined the effect on glucose concentration in culture media on myosin isoforms expression by qRT-PCR. As a result, <i>Myh2</i> and <i>Myh4</i> were significantly increased in Low and Medium conditions. Altogether, Low and Medium glucose conditions induced <i>Myh</i> expression probably via enhancement glucose utilization.https://www.mdpi.com/2076-3417/12/3/1553low glucoseskeletal muscleproteomeenergy metabolism |
spellingShingle | Ayano Kato Iori Sakakibara Taku Fukushima Kosuke Sugiura Tomoya Fukawa Takeshi Nikawa Takayuki Uchida Quantitative Proteome Analysis in Response to Glucose Concentration in C2C12 Myotubes Applied Sciences low glucose skeletal muscle proteome energy metabolism |
title | Quantitative Proteome Analysis in Response to Glucose Concentration in C2C12 Myotubes |
title_full | Quantitative Proteome Analysis in Response to Glucose Concentration in C2C12 Myotubes |
title_fullStr | Quantitative Proteome Analysis in Response to Glucose Concentration in C2C12 Myotubes |
title_full_unstemmed | Quantitative Proteome Analysis in Response to Glucose Concentration in C2C12 Myotubes |
title_short | Quantitative Proteome Analysis in Response to Glucose Concentration in C2C12 Myotubes |
title_sort | quantitative proteome analysis in response to glucose concentration in c2c12 myotubes |
topic | low glucose skeletal muscle proteome energy metabolism |
url | https://www.mdpi.com/2076-3417/12/3/1553 |
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