메뉴 건너뛰기




Volumn 4, Issue 11, 2012, Pages 1723-1739

Post-meal responses of elongation factor 2 (eEF2) and adenosine monophosphate-activated protein kinase (AMPK) to leucine and carbohydrate supplements for regulating protein synthesis duration and energy homeostasis in rat skeletal muscle

Author keywords

Branched chain amino acids; mTORC1; Translation elongation; Translation initiation; Whey protein

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; CARBOHYDRATE; ELONGATION FACTOR 2; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; INITIATION FACTOR 4E BINDING PROTEIN 1; INSULIN; ISOLEUCINE; LEUCINE; MUSCLE PROTEIN; PROTEIN KINASE B; VALINE;

EID: 84870620874     PISSN: 20726643     EISSN: None     Source Type: Journal    
DOI: 10.3390/nu4111723     Document Type: Article
Times cited : (15)

References (25)
  • 1
    • 64249113497 scopus 로고    scopus 로고
    • Dietary guidelines should reflect new understandings about adult protein needs
    • Layman, D.K. Dietary guidelines should reflect new understandings about adult protein needs. Nutr. Metab. (Lond.) 2009, 6, 12.
    • (2009) Nutr. Metab. (Lond.) , vol.6 , pp. 12
    • Layman, D.K.1
  • 2
    • 0036440779 scopus 로고    scopus 로고
    • Regulation of mammalian translation factors by nutrients
    • Proud, C.G. Regulation of mammalian translation factors by nutrients. Eur. J. Biochem. 2002, 269, 5338-5349.
    • (2002) Eur. J. Biochem , vol.269 , pp. 5338-5349
    • Proud, C.G.1
  • 4
    • 66749157399 scopus 로고    scopus 로고
    • The leucine content of a complete meal directs peak activation but not duration of skeletal muscle protein synthesis and mammalian target of rapamycin signaling in rats
    • Norton, L.E.; Layman, D.K.; Bunpo, P.; Anthony, T.G.; Brana, D.V.; Garlick, P.J. The leucine content of a complete meal directs peak activation but not duration of skeletal muscle protein synthesis and mammalian target of rapamycin signaling in rats. J. Nutr. 2009, 139, 1103-1109.
    • (2009) J. Nutr , vol.139 , pp. 1103-1109
    • Norton, L.E.1    Layman, D.K.2    Bunpo, P.3    Anthony, T.G.4    Brana, D.V.5    Garlick, P.J.6
  • 5
    • 0025292876 scopus 로고
    • Relationship of resting metabolic rate to body composition and protein turnover
    • Welle, S.; Nair, K.S. Relationship of resting metabolic rate to body composition and protein turnover. Am. J. Physiol. 1990, 258, E990-E998.
    • (1990) Am. J. Physiol , vol.258
    • Welle, S.1    Nair, K.S.2
  • 6
    • 0036438894 scopus 로고    scopus 로고
    • Regulation of peptide-chain elongation in mammalian cells
    • Browne, G.J.; Proud, C.G. Regulation of peptide-chain elongation in mammalian cells. Eur. J. Biochem. 2002, 269, 5360-5368.
    • (2002) Eur. J. Biochem , vol.269 , pp. 5360-5368
    • Browne, G.J.1    Proud, C.G.2
  • 7
    • 0037143449 scopus 로고    scopus 로고
    • Activation of amp-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis
    • Horman, S.; Browne, G.; Krause, U.; Patel, J.; Vertommen, D.; Bertrand, L.; Lavoinne, A.; Hue, L.; Proud, C.; Rider, M. Activation of amp-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis. Curr. Biol. 2002, 12, 1419-1423.
    • (2002) Curr. Biol , vol.12 , pp. 1419-1423
    • Horman, S.1    Browne, G.2    Krause, U.3    Patel, J.4    Vertommen, D.5    Bertrand, L.6    Lavoinne, A.7    Hue, L.8    Proud, C.9    Rider, M.10
  • 8
    • 0021068623 scopus 로고
    • Cellular growth of skeletal muscle in weanling rats during dietary restrictions
    • Glore, S.R.; Layman, D.K. Cellular growth of skeletal muscle in weanling rats during dietary restrictions. Growth 1983, 47, 403-410.
    • (1983) Growth , vol.47 , pp. 403-410
    • Glore, S.R.1    Layman, D.K.2
  • 10
    • 0033980371 scopus 로고    scopus 로고
    • Orally administered leucine stimulates protein synthesis in skeletal muscle of postabsorptive rats in association with increased eIF4F formation
    • Anthony, J.C.; Anthony, T.G.; Kimball, S.R.; Vary, T.C.; Jefferson, L.S. Orally administered leucine stimulates protein synthesis in skeletal muscle of postabsorptive rats in association with increased eIF4F formation. J. Nutr. 2000, 130, 139-145.
    • (2000) J. Nutr , vol.130 , pp. 139-145
    • Anthony, J.C.1    Anthony, T.G.2    Kimball, S.R.3    Vary, T.C.4    Jefferson, L.S.5
  • 11
    • 0033006694 scopus 로고    scopus 로고
    • Leucine supplementation enhances skeletal muscle recovery in rats following exercise
    • Anthony, J.C.; Anthony, T.G.; Layman, D.K. Leucine supplementation enhances skeletal muscle recovery in rats following exercise. J. Nutr. 1999, 129, 1102-1106.
    • (1999) J. Nutr , vol.129 , pp. 1102-1106
    • Anthony, J.C.1    Anthony, T.G.2    Layman, D.K.3
  • 12
    • 0035069433 scopus 로고    scopus 로고
    • Oral administration of leucine stimulates ribosomal protein mrna translation but not global rates of protein synthesis in the liver of rats
    • Anthony, T.G.; Anthony, J.C.; Yoshizawa, F.; Kimball, S.R.; Jefferson, L.S. Oral administration of leucine stimulates ribosomal protein mrna translation but not global rates of protein synthesis in the liver of rats. J. Nutr. 2001, 131, 1171-1176.
    • (2001) J. Nutr , vol.131 , pp. 1171-1176
    • Anthony, T.G.1    Anthony, J.C.2    Yoshizawa, F.3    Kimball, S.R.4    Jefferson, L.S.5
  • 13
    • 14944341734 scopus 로고    scopus 로고
    • Oral leucine administration stimulates protein synthesis in rat skeletal muscle
    • Crozier, S.J.; Kimball, S.R.; Emmert, S.W.; Anthony, J.C.; Jefferson, L.S. Oral leucine administration stimulates protein synthesis in rat skeletal muscle. J. Nutr. 2005, 135, 376-382.
    • (2005) J. Nutr , vol.135 , pp. 376-382
    • Crozier, S.J.1    Kimball, S.R.2    Emmert, S.W.3    Anthony, J.C.4    Jefferson, L.S.5
  • 14
    • 0019214262 scopus 로고
    • A rapid and convenient technique for measuring the rate of protein synthesis in tissues by injection of [3H]phenylalanine
    • Garlick, P.J.; McNurlan, M.A.; Preedy, V.R. A rapid and convenient technique for measuring the rate of protein synthesis in tissues by injection of [3H]phenylalanine. Biochem. J. 1980, 192, 719-723.
    • (1980) Biochem. J , vol.192 , pp. 719-723
    • Garlick, P.J.1    McNurlan, M.A.2    Preedy, V.R.3
  • 17
    • 38649094546 scopus 로고    scopus 로고
    • Simultaneous determination of 33 amino acids and dipeptides in spent cell culture media by gas chromatography-flame ionization detection following liquid and solid phase extraction
    • Mohabbat, T.; Drew, B. Simultaneous determination of 33 amino acids and dipeptides in spent cell culture media by gas chromatography-flame ionization detection following liquid and solid phase extraction. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2008, 862, 86-92.
    • (2008) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci , vol.862 , pp. 86-92
    • Mohabbat, T.1    Drew, B.2
  • 18
    • 0030759493 scopus 로고    scopus 로고
    • Determination of free amino acids in pig plasma by precolumn derivatization with 6-N-aminoquinolyl-N-hydroxysuccinimidyl carbamate and high-performance liquid chromatography
    • Reverter, M.; Lundh, T.; Lindberg, J.E. Determination of free amino acids in pig plasma by precolumn derivatization with 6-N-aminoquinolyl-N-hydroxysuccinimidyl carbamate and high-performance liquid chromatography. J. Chromatogr. B Biomed. Sci. Appl. 1997, 696, 1-8.
    • (1997) J. Chromatogr. B Biomed. Sci. Appl , vol.696 , pp. 1-8
    • Reverter, M.1    Lundh, T.2    Lindberg, J.E.3
  • 20
    • 34247241597 scopus 로고    scopus 로고
    • Leucine stimulates mammalian target of rapamycin signaling in C2C12 myoblasts in part through inhibition of adenosine monophosphate-activated protein kinase
    • Du, M.; Shen, Q.W.; Zhu, M.J.; Ford, S.P. Leucine stimulates mammalian target of rapamycin signaling in C2C12 myoblasts in part through inhibition of adenosine monophosphate-activated protein kinase. J. Anim. Sci. 2007, 85, 919-927.
    • (2007) J. Anim. Sci , vol.85 , pp. 919-927
    • Du, M.1    Shen, Q.W.2    Zhu, M.J.3    Ford, S.P.4
  • 21
    • 32444435321 scopus 로고    scopus 로고
    • Leucine regulates translation initiation of protein synthesis in skeletal muscle after exercise
    • Norton, L.E.; Layman, D.K. Leucine regulates translation initiation of protein synthesis in skeletal muscle after exercise. J. Nutr. 2006, 136, 533S-537S.
    • (2006) J. Nutr , vol.136
    • Norton, L.E.1    Layman, D.K.2
  • 22
    • 31544455222 scopus 로고    scopus 로고
    • Branched-chain amino acids as fuels and anabolic signals in human muscle
    • Rennie, M.J.; Bohe, J.; Smith, K.; Wackerhage, H.; Greenhaff, P. Branched-chain amino acids as fuels and anabolic signals in human muscle. J. Nutr. 2006, 136, 264S-268S.
    • (2006) J. Nutr , vol.136
    • Rennie, M.J.1    Bohe, J.2    Smith, K.3    Wackerhage, H.4    Greenhaff, P.5
  • 23
    • 68149162719 scopus 로고    scopus 로고
    • Leucine modulation of mitochondrial mass and oxygen consumption in skeletal muscle cells and adipocytes
    • Sun, X.; Zemel, M.B. Leucine modulation of mitochondrial mass and oxygen consumption in skeletal muscle cells and adipocytes. Nutr. Metab. (Lond.) 2009, 6, 26.
    • (2009) Nutr. Metab. (Lond.) , vol.6 , pp. 26
    • Sun, X.1    Zemel, M.B.2
  • 24
    • 34247579321 scopus 로고    scopus 로고
    • Leucine and calcium regulate fat metabolism and energy partitioning in murine adipocytes and muscle cells
    • Sun, X.; Zemel, M.B. Leucine and calcium regulate fat metabolism and energy partitioning in murine adipocytes and muscle cells. Lipids 2007, 42, 297-305.
    • (2007) Lipids , vol.42 , pp. 297-305
    • Sun, X.1    Zemel, M.B.2
  • 25
    • 84870584380 scopus 로고    scopus 로고
    • Long-term consumption of leucine-rich meals is associated with mitochondrial changes in skeletal muscle of rats
    • Moulton, C.J.; Norton, L.E.; Wilson, G.J.; Layman, D.K. Long-term consumption of leucine-rich meals is associated with mitochondrial changes in skeletal muscle of rats. FASEB J. 2011, 25, 774.15.
    • (2011) FASEB J , vol.25 , Issue.774 , pp. 15
    • Moulton, C.J.1    Norton, L.E.2    Wilson, G.J.3    Layman, D.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.