Effects of short-term fasting on the Akt-mediated pathway involved in protein metabolism in chicken skeletal muscle

被引:9
|
作者
Saneyasu, T. [1 ]
Tsuchii, N. [1 ]
Nakano, Y. [1 ]
Kitashiro, A. [1 ]
Tsuchihashi, T. [1 ]
Shindo, H. [1 ]
Honda, K. [1 ]
Kamisoyama, H. [1 ]
机构
[1] Kobe Univ, Grad Sch Agr Sci, Kobe, Hyogo 6578501, Japan
关键词
Chicken; Fasting; Protein synthesis; Proteolysis; Skeletal muscle; UBIQUITIN-PROTEASOME; SIGNALING PATHWAYS; EXPRESSION; ATROPHY; PROTEOLYSIS; INSULIN; MDM2; 3-METHYLHISTIDINE; PHOSPHORYLATION; HYPERTROPHY;
D O I
10.1016/j.domaniend.2017.06.002
中图分类号
S8 [畜牧、 动物医学、狩猎、蚕、蜂];
学科分类号
0905 ;
摘要
In the present study, we show that short-term (4 h) fasting significantly decreased the levels of protein synthesis-related factors such as the plasma insulin concentration, skeletal muscle pAkt, and pS6 levels in 2-wk-old chickens (P < 0.05). An intravenous injection of insulin significantly elevated the contents of pAkt and p-S6 in the skeletal muscle (P < 0.01). These findings suggest that decreasing the plasma insulin causes the down regulation of the Akt/S6 pathway in chicken skeletal muscle under short-term fasting conditions. However, protein synthesis was not significantly affected by short-term fasting. In addition, no significant change was observed in the levels of proteolysis-related factors such as plasma N-tau-methylhistidine, phosphorylated forkhead box class 0, and muscle ring finger-1 during, 4-h fasting, indicating that short-term fasting does not induce skeletal muscle proteolysis in chickens. Interestingly, atrogin-1 expression significantly increased after 2-h fasting (P < 0.05), and insulin injection significantly reversed the fasting-induced atrogin-1 expression in chicken skeletal muscle (P < 0.01). Collectively, these findings suggest that short-term fasting downregulates the insulin-stimulated Alct/S6 pathway but does not significantly affect protein synthesis and proteolysis in chicken skeletal muscle, and that atrogin-1 expression is upregulated in a FOX01-independent manners. (C) 2017 Elsevier Inc. All rights reserved.
引用
收藏
页码:54 / 61
页数:8
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