Lysine suppresses protein degradation through autophagic–lysosomal system in C2C12 myotubes

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• 作者：Tomonori Sato (1)
  Yoshiaki Ito (1)
  Taku Nedachi (2)
  Takashi Nagasawa (1)
  
• 关键词：Lysine ; Protein degradation ; Autophagy ; mTOR ; C2C12 myotubes
• 刊名：Molecular and Cellular Biochemistry
• 出版年：2014
• 出版时间：June 2014
• 年：2014
• 卷：391
• 期：1-2
• 页码：37-46
• 全文大小：
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• 作者单位：Tomonori Sato (1)
  Yoshiaki Ito (1)
  Taku Nedachi (2)
  Takashi Nagasawa (1)
  
  1. Department of Biological Chemistry and Food Science, Graduate School of Agriculture, Iwate University, Morioka, Iwate, 020-8550, Japan
  2. Department of Applied Biology, Faculty of Life Sciences, Toyo University, Oura-gun, Gunma, 374-0193, Japan
  
• ISSN：1573-4919

文摘

Muscle mass is determined between protein synthesis and protein degradation. Reduction of muscle mass leads to bedridden condition and attenuation of resistance to diseases. Moreover, bedridden condition leads to additional muscle loss due to disuse muscle atrophy. In our previous study (Sato et al. 2013), we showed that administered lysine (Lys), one of essential amino acid, suppressed protein degradation in skeletal muscle. In this study, we investigated that the mechanism of the suppressive effects of Lys on skeletal muscle proteolysis in C2C12 cell line. C2C12 myotubes were incubated in the serum-free medium containing 10?mM Lys or 20?mM Lys, and myofibrillar protein degradation was determined by the rates of 3-methylhistidine (MeHis) release from the cells. The mammalian target of rapamycin (mTOR) activity from the phosphorylation levels of p70-ribosormal protein S6 kinase 1 and eIF4E-binding protein 1 and the autophagic–lysosomal system activity from the ratio of LC3-II/I in C2C12 myotubes stimulated by 10?mM Lys for 0-?h were measured. The rates of MeHis release were markedly reduced by addition of Lys. The autophagic–lysosomal system activity was inhibited upon 30?min of Lys supplementation. The activity of mTOR was significantly increased upon 30?min of Lys supplementation. The suppressive effect of Lys on the proteolysis by the autophagic–lysosomal system was maintained partially when mTOR activity was inhibited by 100?nM rapamycin, suggesting that some regulator other than mTOR signaling, for example, Akt, might also suppress the autophagic–lysosomal system. From these results, we suggested that Lys suppressed the activity of the autophagic–lysosomal system in part through activation of mTOR and reduced myofibrillar protein degradation in C2C12 myotubes.