Effect of Quality and Quantity of Dietary Protein on 4E-BP1 and S6K1 Phosphorylation of Brains in Aged Rats

被引:6
|
作者
Ohsumi, Miho [2 ]
Yoshizawa, Fumiaki [3 ]
Hayase, Kazutoshi [1 ]
Yokogoshi, Hidehiko [2 ]
机构
[1] Aichi Univ Educ, Dept Home Econ, Aichi 4488542, Japan
[2] Univ Shizuoka, Lab Nutr Biochem, Sch Food & Nutr Sci, COE Program 21st Century, Shizuoka 4228526, Japan
[3] Utsunomiya Univ, Dept Anim Sci, Utsunomiya, Tochigi 3218505, Japan
关键词
dietary protein; 4E-BP1; S6K1; protein synthesis; brain; SKELETAL-MUSCLE; GROWTH-HORMONE; ASSOCIATION; TURNOVER; INSULIN; TISSUE; CORTEX; LIVER;
D O I
10.3177/jnsv.56.319
中图分类号
R15 [营养卫生、食品卫生]; TS201 [基础科学];
学科分类号
100403 ;
摘要
We have shown that the rate of brain protein synthesis in aged rats depended on the quality and quantity of dietary protein consumed. The purpose of this study was to determine whether the quality and quantity of dietary protein affected the phosphorylation of eukaryotic initiation factor (elf) 4E-binding protein 1 (4E-BP1) and ribosomal protein S6 kinase (S6K1) and regulated the brain protein synthesis. Two experiments were done on three groups of 24-wk-old male rats given diets containing 20% casein. 20% gluten, or 20% gelatin (Experiment 1), and 20% casein, 5% casein or 0% casein (Experiment 2) for 10 d. The phosphorylation of S6K1 in both the cerebral cortex and cerebellum, and the phosphorylation of 4E-BP1 in the cerebral cortex declined with a decrease of quality and quantity of dietary protein. The phosphorylation of 4E-BP1 in the cerebellum did not differ among groups. The results suggest that the ingestion of a higher quality and quantity of dietary protein stimulates the phosphorylation of 4E-BP1 and S6K1 in the brain and increases the brain protein synthesis in the aged rats.
引用
收藏
页码:319 / 325
页数:7
相关论文
共 50 条
  • [31] Mitotic CDK1 and 4E-BP1 I: Loss of 4E-BP1 serine 82 phosphorylation promotes proliferative polycystic disease and lymphoma in aged or sublethally irradiated mice
    Sun, Rui
    Guo, Siying
    Shuda, Yoko
    Chakka, Anish B.
    Rigatti, Lora H.
    Zhao, Guangyi
    Ali, Mohammed A. E.
    Park, Christopher Y.
    Chandran, Uma
    Yu, Jian
    Bakkenist, Christopher J.
    Shuda, Masahiro
    Moore, Patrick S.
    Chang, Yuan
    PLOS ONE, 2023, 18 (05): : e0282722
  • [32] mTOR controls cell cycle progression through its cell growth effectors S6K1 and 4E-BP1/eukaryotic translation initiation factor 4E
    Fingar, DC
    Richardson, CJ
    Tee, AR
    Cheatham, L
    Tsou, C
    Blenis, J
    MOLECULAR AND CELLULAR BIOLOGY, 2004, 24 (01) : 200 - 216
  • [33] Dissociation of the eukaryotic initiation factor-4E/4E-BP1 complex involves phosphorylation of 4E-BP1 by an mTOR-associated kinase
    Heesom, KJ
    Denton, RM
    FEBS LETTERS, 1999, 457 (03) : 489 - 493
  • [34] The dynamic mechanism of 4E-BP1 recognition and phosphorylation by mTORC1
    Bohm, Raphael
    Imseng, Stefan
    Jakob, Roman P.
    Hall, Michael N.
    Maier, Timm
    Hiller, Sebastian
    MOLECULAR CELL, 2021, 81 (11) : 2403 - +
  • [35] Order Of Phosphorylation Events In Activation Of Ribosomal Protein S6 Kinase 1 (S6K1)
    Keshwani, Malik M.
    Taylor, Susan S.
    FASEB JOURNAL, 2010, 24
  • [36] 4E-BP1 phosphorylation is mediated by the FRAP-p70(s6k) pathway and is independent of mitogen-activated protein kinase
    vonManteuffel, SR
    Gingras, AC
    Ming, XF
    Sonenberg, N
    Thomas, G
    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (09) : 4076 - 4080
  • [37] 4E-BP1, a multifactor regulated multifunctional protein
    Qin, Xiaoyu
    Jiang, Bin
    Zhang, Yanjie
    CELL CYCLE, 2016, 15 (06) : 781 - 786
  • [39] mTORC1 drives HIF-1α and VEGF-A signalling via multiple mechanisms involving 4E-BP1, S6K1 and STAT3
    K M Dodd
    J Yang
    M H Shen
    J R Sampson
    A R Tee
    Oncogene, 2015, 34 : 2239 - 2250
  • [40] mTORC1 drives HIF-1α and VEGF-A signalling via multiple mechanisms involving 4E-BP1, S6K1 and STAT3
    Dodd, K. M.
    Yang, J.
    Shen, M. H.
    Sampson, J. R.
    Tee, A. R.
    ONCOGENE, 2015, 34 (17) : 2239 - 2250