期刊
JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
卷 38, 期 2, 页码 201-214出版社
SPRINGER
DOI: 10.1007/s10974-017-9473-9
关键词
Caffeine; Skeletal muscle; Protein synthesis; Autophagy; Myostatin
类别
资金
- Office of Undergraduate Research at the University of South Carolina
- University of South Carolina Upstate Office of Sponsored Awards and Research Support
- National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health [R15DK106688]
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R15DK106688] Funding Source: NIH RePORTER
Caffeine is a highly catabolic dietary stimulant. High caffeine concentrations (1-10 mM) have previously been shown to inhibit protein synthesis and increase protein degradation in various mammalian cell lines. The purpose of this study was to examine the effect of short-term caffeine exposure on cell signaling pathways that regulate protein metabolism in mammalian skeletal muscle cells. Fully differentiated C2C12 skeletal myotubes either received vehicle (DMSO) or 5 mM caffeine for 6 h. Our analysis revealed that caffeine promoted a 40% increase in autolysosome formation and a 25% increase in autophagic flux. In contrast, caffeine treatment did not significantly increase the expression of the skeletal muscle specific ubiquitin ligases MAFbx and MuRF1 or 20S proteasome activity. Caffeine treatment significantly reduced mTORC1 signaling, total protein synthesis and myotube diameter in a CaMKK beta/AMPK-dependent manner. Further, caffeine promoted a CaMKII-dependent increase in myostatin mRNA expression that did not significantly contribute to the caffeine-dependent reduction in protein synthesis. Our results indicate that short-term caffeine exposure significantly reduced skeletal myotube diameter by increasing autophagic flux and promoting a CaMKK beta/AMPK-dependent reduction in protein synthesis.
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