Regulators of protein metabolism are affected by cyclical nutritional treatments with diets varying in protein and energy content
2012
Omezzine, Sourour | Metayer-Coustard, Sonia | Collin, Anne | Rideau, Nicole | Leterrier, Christine | Bouvarel, Isabelle | Seiliez, Iban | Tesseraud, Sophie | Unité de Recherches Avicoles (URA) ; Institut National de la Recherche Agronomique (INRA) | Physiologie de la reproduction et des comportements [Nouzilly] (PRC) ; Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur] (IFCE)-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS) | Institut Technique de l'AVIculture (ITAVI) | Nutrition, Aquaculture et Génomique (NUAGE) ; Institut National de la Recherche Agronomique (INRA)-Université Sciences et Technologies - Bordeaux 1 (UB)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER) | ACTA/MAP/MESR, INRA
There is evidence that the E3 ubiquitin ligases muscle ring finger-1 (MuRF1) and atrogin-1, which mediate the ubiquitination of certain proteins and thereby their proteolysis, are regulated by cyclical nutritional treatments varying in lysine content. In order to explore further the regulatory mechanisms involved in metabolic adaptation to dietary changes, we investigated the effects of daily variations in energy [2800 (E-) followed by 3200 kcal/kg (E+)], protein [230 (P+) followed by 150g/kg (P-)] or both [E-P+ followed by E+P-] on muscle protein metabolism in 2-week-old male broiler chickens. Growth performance was similar for all treatments. Expression of atrogin-1 and MuRF1 was changed by alternation of diets varying in protein (higher expression with P- vs. P+) and energy content (higher expression with E- vs. E+). The expression of atrogin-1 was regulated with mixed diets (increase in E+P- vs. E-P+) but not that of MuRF1. Such regulation may involve the mammalian target of rapamycin (mTOR), which was more phosphorylated with P+ than with P-. Eukaryotic initiation factor 4E binding protein, p70S6 kinase and ribosomal protein S6, which are mTOR targets known to control protein synthesis, were highly activated by increased protein content (P+ vs. P-). The mechanisms coordinating the protein synthesis/proteolysis balance remain to be characterized.
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