Immobilization induces anabolic resistance in human myofibrillar protein synthesis with low and high dose amino acid infusion
We tested the hypothesis that increasing blood amino acid (AA) availability would counter the physical inactivity-induced reduction in muscle protein synthesis. We determined how 14 days of unilateral knee immobilization affected quadriceps myofibrillar protein synthesis (MPS) in young healthy subje...
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| Published in | The Journal of physiology Vol. 586; no. 24; pp. 6049 - 6061 |
|---|---|
| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Oxford, UK
The Physiological Society
15.12.2008
Blackwell Publishing Ltd Blackwell Science Inc |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0022-3751 1469-7793 1469-7793 |
| DOI | 10.1113/jphysiol.2008.160333 |
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| Abstract | We tested the hypothesis that increasing blood amino acid (AA) availability would counter the physical inactivity-induced
reduction in muscle protein synthesis. We determined how 14 days of unilateral knee immobilization affected quadriceps myofibrillar
protein synthesis (MPS) in young healthy subjects (10 men, 2 women, 21 ± 1 years; 80.2 ± 4.0 kg, mean ± s.e.m. ) in the post-absorptive state and after infusing AA (10% Primene) at low or high doses (43 and 261 mg kg â1 h â1 ). Muscle cross-sectional area (MRI) and peak isometric torque declined in the immobilized leg (â5.0 ± 1.2% and â25 ± 3%,
respectively, both P < 0.005), but were unchanged (all P > 0.6) in the non-immobilized leg. Immobilization induced a 27% decline in the rate of post-absorptive MPS (immobilized,
0.027 ± 0.003: non-immobilized, 0.037 ± 0.003% h â1 ; P < 0.001). Regardless of dose, AA infusion stimulated a greater rise in MPS in the non-immobilized legs; at 4 h MPS was greater
by +54 ± 12% with low dose and +68 ± 17% with high dose AA infusion (both P < 0.001). There was some evidence of delayed responsiveness of phosphorylation of Akt to high doses of AA and p70S6k at both
doses but no marked differences in that of mTOR, GSK3β or eEF2. Phosphorylation of focal adhesion kinase (Tyr 576/577 ) was reduced ( P < 0.05) with immobilization. We observed no change in polyubiquitinated protein content after immobilization. We confirm
that 14 days of immobilization reduces MPS in the post-absorptive state and this diminution is reduced but not abolished by
increased provision of AA, even at high rates. The immobilization-induced decline in post-absorptive MPS with the âanabolic
resistanceâ to amino acids can account for much of immobilization-induced muscle atrophy. |
|---|---|
| AbstractList | We tested the hypothesis that increasing blood amino acid (AA) availability would counter the physical inactivity‐induced reduction in muscle protein synthesis. We determined how 14 days of unilateral knee immobilization affected quadriceps myofibrillar protein synthesis (MPS) in young healthy subjects (10 men, 2 women, 21 ± 1 years; 80.2 ± 4.0 kg, mean ±
s.e.m.
) in the post‐absorptive state and after infusing AA (10% Primene) at low or high doses (43 and 261 mg kg
−1
h
−1
). Muscle cross‐sectional area (MRI) and peak isometric torque declined in the immobilized leg (−5.0 ± 1.2% and −25 ± 3%, respectively, both
P
< 0.005), but were unchanged (all
P
> 0.6) in the non‐immobilized leg. Immobilization induced a 27% decline in the rate of post‐absorptive MPS (immobilized, 0.027 ± 0.003: non‐immobilized, 0.037 ± 0.003% h
−1
;
P
< 0.001). Regardless of dose, AA infusion stimulated a greater rise in MPS in the non‐immobilized legs; at 4 h MPS was greater by +54 ± 12% with low dose and +68 ± 17% with high dose AA infusion (both
P
< 0.001). There was some evidence of delayed responsiveness of phosphorylation of Akt to high doses of AA and p70S6k at both doses but no marked differences in that of mTOR, GSK3β or eEF2. Phosphorylation of focal adhesion kinase (Tyr
576/577
) was reduced (
P
< 0.05) with immobilization. We observed no change in polyubiquitinated protein content after immobilization. We confirm that 14 days of immobilization reduces MPS in the post‐absorptive state and this diminution is reduced but not abolished by increased provision of AA, even at high rates. The immobilization‐induced decline in post‐absorptive MPS with the ‘anabolic resistance’ to amino acids can account for much of immobilization‐induced muscle atrophy. We tested the hypothesis that increasing blood amino acid (AA) availability would counter the physical inactivity-induced reduction in muscle protein synthesis. We determined how 14 days of unilateral knee immobilization affected quadriceps myofibrillar protein synthesis (MPS) in young healthy subjects (10 men, 2 women, 21 ± 1 years; 80.2 ± 4.0 kg, mean ± s.e.m. ) in the post-absorptive state and after infusing AA (10% Primene) at low or high doses (43 and 261 mg kg â1 h â1 ). Muscle cross-sectional area (MRI) and peak isometric torque declined in the immobilized leg (â5.0 ± 1.2% and â25 ± 3%, respectively, both P < 0.005), but were unchanged (all P > 0.6) in the non-immobilized leg. Immobilization induced a 27% decline in the rate of post-absorptive MPS (immobilized, 0.027 ± 0.003: non-immobilized, 0.037 ± 0.003% h â1 ; P < 0.001). Regardless of dose, AA infusion stimulated a greater rise in MPS in the non-immobilized legs; at 4 h MPS was greater by +54 ± 12% with low dose and +68 ± 17% with high dose AA infusion (both P < 0.001). There was some evidence of delayed responsiveness of phosphorylation of Akt to high doses of AA and p70S6k at both doses but no marked differences in that of mTOR, GSK3β or eEF2. Phosphorylation of focal adhesion kinase (Tyr 576/577 ) was reduced ( P < 0.05) with immobilization. We observed no change in polyubiquitinated protein content after immobilization. We confirm that 14 days of immobilization reduces MPS in the post-absorptive state and this diminution is reduced but not abolished by increased provision of AA, even at high rates. The immobilization-induced decline in post-absorptive MPS with the âanabolic resistanceâ to amino acids can account for much of immobilization-induced muscle atrophy. We tested the hypothesis that increasing blood amino acid (AA) availability would counter the physical inactivity-induced reduction in muscle protein synthesis. We determined how 14 days of unilateral knee immobilization affected quadriceps myofibrillar protein synthesis (MPS) in young healthy subjects (10 men, 2 women, 21 +/- 1 years; 80.2 +/- 4.0 kg, mean +/- S.E.M.) in the post-absorptive state and after infusing AA (10% Primene) at low or high doses (43 and 261 mg kg(-1) h(-1)). Muscle cross-sectional area (MRI) and peak isometric torque declined in the immobilized leg (-5.0 +/- 1.2% and -25 +/- 3%, respectively, both P < 0.005), but were unchanged (all P > 0.6) in the non-immobilized leg. Immobilization induced a 27% decline in the rate of post-absorptive MPS (immobilized, 0.027 +/- 0.003: non-immobilized, 0.037 +/- 0.003% h(-1); P < 0.001). Regardless of dose, AA infusion stimulated a greater rise in MPS in the non-immobilized legs; at 4 h MPS was greater by +54 +/- 12% with low dose and +68 +/- 17% with high dose AA infusion (both P < 0.001). There was some evidence of delayed responsiveness of phosphorylation of Akt to high doses of AA and p70S6k at both doses but no marked differences in that of mTOR, GSK3beta or eEF2. Phosphorylation of focal adhesion kinase (Tyr(576/577)) was reduced (P < 0.05) with immobilization. We observed no change in polyubiquitinated protein content after immobilization. We confirm that 14 days of immobilization reduces MPS in the post-absorptive state and this diminution is reduced but not abolished by increased provision of AA, even at high rates. The immobilization-induced decline in post-absorptive MPS with the 'anabolic resistance' to amino acids can account for much of immobilization-induced muscle atrophy. We tested the hypothesis that increasing blood amino acid (AA) availability would counter the physical inactivity-induced reduction in muscle protein synthesis. We determined how 14 days of unilateral knee immobilization affected quadriceps myofibrillar protein synthesis (MPS) in young healthy subjects (10 men, 2 women, 21 +/- 1 years; 80.2 +/- 4.0 kg, mean +/- S.E.M.) in the post-absorptive state and after infusing AA (10% Primene) at low or high doses (43 and 261 mg kg(-1) h(-1)). Muscle cross-sectional area (MRI) and peak isometric torque declined in the immobilized leg (-5.0 +/- 1.2% and -25 +/- 3%, respectively, both P < 0.005), but were unchanged (all P > 0.6) in the non-immobilized leg. Immobilization induced a 27% decline in the rate of post-absorptive MPS (immobilized, 0.027 +/- 0.003: non-immobilized, 0.037 +/- 0.003% h(-1); P < 0.001). Regardless of dose, AA infusion stimulated a greater rise in MPS in the non-immobilized legs; at 4 h MPS was greater by +54 +/- 12% with low dose and +68 +/- 17% with high dose AA infusion (both P < 0.001). There was some evidence of delayed responsiveness of phosphorylation of Akt to high doses of AA and p70S6k at both doses but no marked differences in that of mTOR, GSK3beta or eEF2. Phosphorylation of focal adhesion kinase (Tyr(576/577)) was reduced (P < 0.05) with immobilization. We observed no change in polyubiquitinated protein content after immobilization. We confirm that 14 days of immobilization reduces MPS in the post-absorptive state and this diminution is reduced but not abolished by increased provision of AA, even at high rates. The immobilization-induced decline in post-absorptive MPS with the 'anabolic resistance' to amino acids can account for much of immobilization-induced muscle atrophy.We tested the hypothesis that increasing blood amino acid (AA) availability would counter the physical inactivity-induced reduction in muscle protein synthesis. We determined how 14 days of unilateral knee immobilization affected quadriceps myofibrillar protein synthesis (MPS) in young healthy subjects (10 men, 2 women, 21 +/- 1 years; 80.2 +/- 4.0 kg, mean +/- S.E.M.) in the post-absorptive state and after infusing AA (10% Primene) at low or high doses (43 and 261 mg kg(-1) h(-1)). Muscle cross-sectional area (MRI) and peak isometric torque declined in the immobilized leg (-5.0 +/- 1.2% and -25 +/- 3%, respectively, both P < 0.005), but were unchanged (all P > 0.6) in the non-immobilized leg. Immobilization induced a 27% decline in the rate of post-absorptive MPS (immobilized, 0.027 +/- 0.003: non-immobilized, 0.037 +/- 0.003% h(-1); P < 0.001). Regardless of dose, AA infusion stimulated a greater rise in MPS in the non-immobilized legs; at 4 h MPS was greater by +54 +/- 12% with low dose and +68 +/- 17% with high dose AA infusion (both P < 0.001). There was some evidence of delayed responsiveness of phosphorylation of Akt to high doses of AA and p70S6k at both doses but no marked differences in that of mTOR, GSK3beta or eEF2. Phosphorylation of focal adhesion kinase (Tyr(576/577)) was reduced (P < 0.05) with immobilization. We observed no change in polyubiquitinated protein content after immobilization. We confirm that 14 days of immobilization reduces MPS in the post-absorptive state and this diminution is reduced but not abolished by increased provision of AA, even at high rates. The immobilization-induced decline in post-absorptive MPS with the 'anabolic resistance' to amino acids can account for much of immobilization-induced muscle atrophy. We tested the hypothesis that increasing blood amino acid (AA) availability would counter the physical inactivity-induced reduction in muscle protein synthesis. We determined how 14 days of unilateral knee immobilization affected quadriceps myofibrillar protein synthesis (MPS) in young healthy subjects (10 men, 2 women, 21 ± 1 years; 80.2 ± 4.0 kg, mean ± s.e.m. ) in the post-absorptive state and after infusing AA (10% Primene) at low or high doses (43 and 261 mg kg −1 h −1 ). Muscle cross-sectional area (MRI) and peak isometric torque declined in the immobilized leg (−5.0 ± 1.2% and −25 ± 3%, respectively, both P < 0.005), but were unchanged (all P > 0.6) in the non-immobilized leg. Immobilization induced a 27% decline in the rate of post-absorptive MPS (immobilized, 0.027 ± 0.003: non-immobilized, 0.037 ± 0.003% h −1 ; P < 0.001). Regardless of dose, AA infusion stimulated a greater rise in MPS in the non-immobilized legs; at 4 h MPS was greater by +54 ± 12% with low dose and +68 ± 17% with high dose AA infusion (both P < 0.001). There was some evidence of delayed responsiveness of phosphorylation of Akt to high doses of AA and p70S6k at both doses but no marked differences in that of mTOR, GSK3 β or eEF2. Phosphorylation of focal adhesion kinase (Tyr 576/577 ) was reduced ( P < 0.05) with immobilization. We observed no change in polyubiquitinated protein content after immobilization. We confirm that 14 days of immobilization reduces MPS in the post-absorptive state and this diminution is reduced but not abolished by increased provision of AA, even at high rates. The immobilization-induced decline in post-absorptive MPS with the ‘anabolic resistance’ to amino acids can account for much of immobilization-induced muscle atrophy. We tested the hypothesis that increasing blood amino acid (AA) availability would counter the physical inactivity‐induced reduction in muscle protein synthesis. We determined how 14 days of unilateral knee immobilization affected quadriceps myofibrillar protein synthesis (MPS) in young healthy subjects (10 men, 2 women, 21 ± 1 years; 80.2 ± 4.0 kg, mean ±s.e.m.) in the post‐absorptive state and after infusing AA (10% Primene) at low or high doses (43 and 261 mg kg−1 h−1). Muscle cross‐sectional area (MRI) and peak isometric torque declined in the immobilized leg (−5.0 ± 1.2% and −25 ± 3%, respectively, both P < 0.005), but were unchanged (all P > 0.6) in the non‐immobilized leg. Immobilization induced a 27% decline in the rate of post‐absorptive MPS (immobilized, 0.027 ± 0.003: non‐immobilized, 0.037 ± 0.003% h−1; P < 0.001). Regardless of dose, AA infusion stimulated a greater rise in MPS in the non‐immobilized legs; at 4 h MPS was greater by +54 ± 12% with low dose and +68 ± 17% with high dose AA infusion (both P < 0.001). There was some evidence of delayed responsiveness of phosphorylation of Akt to high doses of AA and p70S6k at both doses but no marked differences in that of mTOR, GSK3β or eEF2. Phosphorylation of focal adhesion kinase (Tyr576/577) was reduced (P < 0.05) with immobilization. We observed no change in polyubiquitinated protein content after immobilization. We confirm that 14 days of immobilization reduces MPS in the post‐absorptive state and this diminution is reduced but not abolished by increased provision of AA, even at high rates. The immobilization‐induced decline in post‐absorptive MPS with the ‘anabolic resistance’ to amino acids can account for much of immobilization‐induced muscle atrophy. |
| Author | Elisa I. Glover Jason E. Tang Mark A. Tarnopolsky Stuart M. Phillips Bryan R. Oates Anna Selby Michael J. Rennie Kenneth Smith |
| Author_xml | – sequence: 1 givenname: Elisa I. surname: Glover fullname: Glover, Elisa I. – sequence: 2 givenname: Stuart M. surname: Phillips fullname: Phillips, Stuart M. – sequence: 3 givenname: Bryan R. surname: Oates fullname: Oates, Bryan R. – sequence: 4 givenname: Jason E. surname: Tang fullname: Tang, Jason E. – sequence: 5 givenname: Mark A. surname: Tarnopolsky fullname: Tarnopolsky, Mark A. – sequence: 6 givenname: Anna surname: Selby fullname: Selby, Anna – sequence: 7 givenname: Kenneth surname: Smith fullname: Smith, Kenneth – sequence: 8 givenname: Michael J. surname: Rennie fullname: Rennie, Michael J. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/18955382$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1152/jappl.2001.90.3.1174 10.1152/japplphysiol.90558.2008 10.1152/japplphysiol.00560.2007 10.1152/ajpendo.00582.2007 10.1152/ajpendo.00415.2005 10.1152/japplphysiol.00247.2005 10.1007/s004210100467 10.1210/jc.2003-032159 10.1038/emboj.2008.39 10.1093/ajcn/82.5.941 10.1038/sj.onc.1209887 10.1128/MCB.01512-07 10.1152/japplphysiol.01346.2007 10.1093/jn/135.7.1824S 10.1111/j.1530-0277.2007.00548.x 10.1073/pnas.251541198 10.1093/ajcn/85.4.1031 10.1152/ajpcell.1999.277.1.C152 10.1152/ajpregu.00292.2007 10.1146/annurev.physiol.66.052102.134444 10.1111/j.1365-201X.2004.01293.x 10.1152/ajpendo.90411.2008 10.1093/ajcn/84.3.475 10.1111/j.1469-7793.2001.0575f.x 10.1042/cs0720503 10.1152/ajpregu.00761.2007 10.1093/jn/136.1.227S 10.1042/BJ20070024 10.1152/ajpendo.00430.2003 10.1016/j.nut.2004.04.009 10.1113/jphysiol.2006.118042 10.1042/bst0290541 10.1152/physiol.00024.2006 10.1152/japplphysiol.00221.2002 10.1113/jphysiol.2003.050674 10.1096/fj.03-0610com 10.1139/H07-076 10.1113/jphysiol.2007.134593 10.1210/jc.2004-1702 10.1152/ajpendo.00141.2006 10.1096/fj.06-6604com 10.1139/h06-028 10.1113/jphysiol.2007.142828 10.1152/ajpendo.00387.2004 10.1113/jphysiol.2004.066365 10.1152/ajpendo.1996.270.4.E627 10.1210/jc.2006-0651 10.1152/japplphysiol.00180.2006 10.1113/jphysiol.2006.113175 10.1152/japplphysiol.00346.2003 10.1152/jappl.1989.67.1.19 10.1681/ASN.2006010083 10.1096/fj.04-2640fje 10.1128/MCB.25.7.2558-2572.2005 |
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| References | 2007; 103 2004; 287 2004; 66 2007; 585 2004; 20 2006; 31 2001; 90 1987; 72 2005; 135 2007; 582 2008; 105 2006; 291 2008; 32 2006; 290 2007; 32 2003; 95 2003; 552 2001; 85 2006; 576 2006; 136 2005; 25 2007; 579 2007; 293 2006; 21 2006; 25 2008; 27 2008; 28 2002; 93 2007; 21 2001; 532 2001; 98 2006; 91 1989; 67 2006; 50 2007; 403 2004; 181 2002; 9 2005; 90 2006; 17 2004; 89 2005; 82 2001; 29 2005; 19 2006; 84 2004; 18 2005; 288 1996; 270 2005; 10 1999; 277 2007; 85 2004; 558 2008; 295 2006; 101 2005; 99 2008; 294 e_1_2_5_27_1 e_1_2_5_25_1 e_1_2_5_48_1 e_1_2_5_23_1 e_1_2_5_46_1 e_1_2_5_21_1 e_1_2_5_44_1 e_1_2_5_29_1 Anastasi G (e_1_2_5_4_1) 2006; 50 Rennie MJ (e_1_2_5_40_1) 2005; 10 e_1_2_5_42_1 e_1_2_5_15_1 e_1_2_5_38_1 e_1_2_5_17_1 e_1_2_5_36_1 e_1_2_5_9_1 e_1_2_5_11_1 e_1_2_5_34_1 e_1_2_5_57_1 e_1_2_5_7_1 e_1_2_5_13_1 e_1_2_5_32_1 e_1_2_5_55_1 e_1_2_5_5_1 e_1_2_5_3_1 e_1_2_5_19_1 e_1_2_5_30_1 e_1_2_5_53_1 e_1_2_5_51_1 e_1_2_5_28_1 e_1_2_5_49_1 e_1_2_5_26_1 e_1_2_5_47_1 e_1_2_5_24_1 e_1_2_5_45_1 e_1_2_5_22_1 e_1_2_5_43_1 e_1_2_5_20_1 e_1_2_5_41_1 e_1_2_5_14_1 e_1_2_5_39_1 e_1_2_5_16_1 e_1_2_5_37_1 e_1_2_5_58_1 e_1_2_5_8_1 e_1_2_5_35_1 e_1_2_5_56_1 e_1_2_5_6_1 e_1_2_5_12_1 e_1_2_5_33_1 e_1_2_5_54_1 e_1_2_5_2_1 e_1_2_5_18_1 e_1_2_5_31_1 e_1_2_5_52_1 e_1_2_5_50_1 Carrithers JA (e_1_2_5_10_1) 2002; 9 15196095 - Acta Physiol Scand. 2004 Jul;181(3):345-57 16365087 - J Nutr. 2006 Jan;136(1 Suppl):227S-31S 18577697 - Am J Physiol Endocrinol Metab. 2008 Sep;295(3):E595-604 14600160 - J Appl Physiol (1985). 2003 Dec;95(6):2185-201 16960159 - Am J Clin Nutr. 2006 Sep;84(3):475-82 15212752 - Nutrition. 2004 Jul-Aug;20(7-8):689-95 17478528 - J Physiol. 2007 Jul 15;582(Pt 2):813-23 2435445 - Clin Sci (Lond). 1987 Apr;72(4):503-9 17218363 - J Physiol. 2007 Mar 15;579(Pt 3):877-92 17641219 - J Appl Physiol (1985). 2007 Oct;103(4):1242-50 16835402 - Am J Physiol Endocrinol Metab. 2006 Dec;291(6):E1197-205 8928769 - Am J Physiol. 1996 Apr;270(4 Pt 1):E627-33 16873412 - J Physiol. 2006 Oct 15;576(Pt 2):613-24 18483167 - J Appl Physiol (1985). 2008 Jul;105(1):241-8 11606016 - Eur J Appl Physiol. 2001 Sep;85(5):466-71 11306673 - J Physiol. 2001 Apr 15;532(Pt 2):575-9 15987873 - J Nutr. 2005 Jul;135(7):1824S-1828S 15356032 - J Clin Endocrinol Metab. 2004 Sep;89(9):4351-8 14977422 - Annu Rev Physiol. 2004;66:799-828 17041627 - Oncogene. 2006 Oct 16;25(48):6423-35 12183515 - J Appl Physiol (1985). 2002 Sep;93(3):1168-80 18059587 - Appl Physiol Nutr Metab. 2007 Dec;32(6):1132-8 17037086 - Ann Transplant. 2005;10(4):31-4 18337751 - EMBO J. 2008 Apr 9;27(7):1005-16 18056791 - Am J Physiol Endocrinol Metab. 2008 Feb;294(2):E392-400 18160716 - Mol Cell Biol. 2008 Mar;28(5):1429-42 16280423 - Am J Clin Nutr. 2005 Nov;82(5):941-8 15131238 - J Physiol. 2004 Jul 15;558(Pt 2):381-8 17376031 - Biochem J. 2007 Apr 15;403(2):217-34 14998784 - Am J Physiol Endocrinol Metab. 2004 Jul;287(1):E1-7 17901116 - J Physiol. 2007 Nov 15;585(Pt 1):241-51 2668254 - J Appl Physiol (1985). 1989 Jul;67(1):19-23 17413102 - Am J Clin Nutr. 2007 Apr;85(4):1031-40 18028527 - Alcohol Clin Exp Res. 2008 Jan;32(1):128-37 15860685 - J Appl Physiol (1985). 2005 Sep;99(3):1085-92 18094071 - Am J Physiol Regul Integr Comp Physiol. 2008 Mar;294(3):R939-47 11717410 - Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14440-5 17213042 - Eur J Histochem. 2006 Oct-Dec;50(4):327-36 16263770 - Am J Physiol Endocrinol Metab. 2006 Apr;290(4):E731-8 16763108 - J Appl Physiol (1985). 2006 Oct;101(4):1136-48 17670860 - Am J Physiol Regul Integr Comp Physiol. 2007 Oct;293(4):R1722-7 12909668 - J Physiol. 2003 Oct 1;552(Pt 1):315-24 11498025 - Biochem Soc Trans. 2001 Aug;29(Pt 4):541-7 15596483 - FASEB J. 2005 Mar;19(3):422-4 11181634 - J Appl Physiol (1985). 2001 Mar;90(3):1174-83; discussion 1165 16990457 - Physiology (Bethesda). 2006 Oct;21:362-9 14718385 - FASEB J. 2004 Jan;18(1):39-51 15598679 - J Clin Endocrinol Metab. 2005 Mar;90(3):1453-9 15002527 - J Gravit Physiol. 2002 Jul;9(1):P155-6 17116744 - FASEB J. 2007 Jan;21(1):140-55 16984982 - J Clin Endocrinol Metab. 2006 Dec;91(12):4836-41 16738015 - J Am Soc Nephrol. 2006 Jul;17(7):1807-19 15572656 - Am J Physiol Endocrinol Metab. 2005 Jun;288(6):E1153-9 17111006 - Appl Physiol Nutr Metab. 2006 Oct;31(5):518-29 15767663 - Mol Cell Biol. 2005 Apr;25(7):2558-72 18535133 - J Appl Physiol (1985). 2008 Sep;105(3):902-6 10409118 - Am J Physiol. 1999 Jul;277(1 Pt 1):C152-62 |
| References_xml | – volume: 25 start-page: 2558 year: 2005 end-page: 2572 article-title: Distinct signaling events downstream of mTOR cooperate to mediate the effects of amino acids and insulin on initiation factor 4E‐binding proteins publication-title: Mol Cell Biol – volume: 552 start-page: 315 year: 2003 end-page: 324 article-title: Human muscle protein synthesis is modulated by extracellular, not intramuscular amino acid availability: a dose–response study publication-title: J Physiol – volume: 90 start-page: 1453 year: 2005 end-page: 1459 article-title: The catabolic effects of prolonged inactivity and acute hypercortisolemia are offset by dietary supplementation publication-title: J Clin Endocrinol Metab – volume: 98 start-page: 14440 year: 2001 end-page: 14445 article-title: Atrogin‐1, a muscle‐specific F‐box protein highly expressed during muscle atrophy publication-title: Proc Natl Acad Sci U S A – volume: 90 start-page: 1174 year: 2001 end-page: 1183 article-title: Selected contribution: Skeletal muscle focal adhesion kinase, paxillin, and serum response factor are loading dependent publication-title: J Appl Physiol – volume: 89 start-page: 4351 year: 2004 end-page: 4358 article-title: Essential amino acid and carbohydrate supplementation ameliorates muscle protein loss in humans during 28 days bedrest publication-title: J Clin Endocrinol Metab – volume: 82 start-page: 941 year: 2005 end-page: 948 article-title: Factors influencing variation in basal metabolic rate include fat‐free mass, fat mass, age, and circulating thyroxine but not sex, circulating leptin, or triiodothyronine publication-title: Am J Clin Nutr – volume: 290 start-page: E731 year: 2006 end-page: E738 article-title: Anabolic signalling and protein synthesis in human skeletal muscle after dynamic shortening or lengthening exercise publication-title: Am J Physiol Endocrinol Metab – volume: 27 start-page: 1005 year: 2008 end-page: 1016 article-title: cdc2‐cyclin B regulates eEF2 kinase activity in a cell cycle‐ and amino acid‐dependent manner publication-title: EMBO J – volume: 103 start-page: 1242 year: 2007 end-page: 1250 article-title: Single muscle fiber function with concurrent exercise or nutrition countermeasures during 60 days of bed rest in women publication-title: J Appl Physiol – volume: 85 start-page: 466 year: 2001 end-page: 471 article-title: Adaptation to chronic eccentric exercise in humans: the influence of contraction velocity publication-title: Eur J Appl Physiol – volume: 18 start-page: 39 year: 2004 end-page: 51 article-title: Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression publication-title: FASEB J – volume: 288 start-page: E1153 year: 2005 end-page: E1159 article-title: Myofibrillar and collagen protein synthesis in human skeletal muscle in young men after maximal shortening and lengthening contractions publication-title: Am J Physiol Endocrinol Metab – volume: 293 start-page: R1722 year: 2007 end-page: R1727 article-title: Contractile and connective tissue protein content of human skeletal muscle: Effects of 35 and 90 days of simulated microgravity and exercise countermeasures publication-title: Am J Physiol Regul Integr Comp Physiol – volume: 32 start-page: 128 year: 2008 end-page: 137 article-title: Alcohol accelerates loss of muscle and impairs recovery of muscle mass resulting from disuse atrophy publication-title: Alcohol Clin Exp Res – volume: 576 start-page: 613 year: 2006 end-page: 624 article-title: Resistance exercise increases AMPK activity and reduces 4E‐BP1 phosphorylation and protein synthesis in human skeletal muscle publication-title: J Physiol – volume: 9 start-page: 155 year: 2002 end-page: 156 article-title: Skeletal muscle protein composition following 5 weeks of ULLS and resistance exercise countermeasures publication-title: J Gravit Physiol – volume: 585 start-page: 241 year: 2007 end-page: 251 article-title: The temporal responses of protein synthesis, gene expression and cell signalling in human quadriceps muscle and patellar tendon to disuse publication-title: J Physiol – volume: 20 start-page: 689 year: 2004 end-page: 695 article-title: Protein requirements and supplementation in strength sports publication-title: Nutrition – volume: 67 start-page: 19 year: 1989 end-page: 23 article-title: Insulin action in human thighs after one‐legged immobilization publication-title: J Appl Physiol – volume: 101 start-page: 1136 year: 2006 end-page: 1148 article-title: Analysis of human skeletal muscle after 48 h immobilization reveals alterations in mRNA and protein for extracellular matrix components publication-title: J Appl Physiol – volume: 294 start-page: E392 year: 2008 end-page: E400 article-title: Leucine‐enriched essential amino acid and carbohydrate ingestion following resistance exercise enhances mTOR signaling and protein synthesis in human muscle publication-title: Am J Physiol Endocrinol Metab – volume: 105 start-page: 902 year: 2008 end-page: 906 article-title: Skeletal muscle proteolysis in response to short‐term unloading in humans publication-title: J Appl Physiol – volume: 95 start-page: 2185 year: 2003 end-page: 2201 article-title: Skeletal muscle unweighting: spaceflight and ground‐based models publication-title: J Appl Physiol – volume: 579 start-page: 877 year: 2007 end-page: 892 article-title: Alterations in mRNA expression and protein products following spinal cord injury in humans publication-title: J Physiol – volume: 29 start-page: 541 year: 2001 end-page: 547 article-title: Interplay between insulin and nutrients in the regulation of translation factors publication-title: Biochem Soc Trans – volume: 135 start-page: 1824S year: 2005 end-page: 1828S article-title: Metabolic consequences of muscle disuse atrophy publication-title: J Nutr – volume: 270 start-page: E627 year: 1996 end-page: E633 article-title: Prolonged bed rest decreases skeletal muscle and whole body protein synthesis publication-title: Am J Physiol – volume: 93 start-page: 1168 year: 2002 end-page: 1180 article-title: Role of insulin in translational control of protein synthesis in skeletal muscle by amino acids or exercise publication-title: J Appl Physiol – volume: 532 start-page: 575 year: 2001 end-page: 579 article-title: Latency and duration of stimulation of human muscle protein synthesis during continuous infusion of amino acids publication-title: J Physiol – volume: 294 start-page: R939 year: 2008 end-page: R947 article-title: Human soleus single muscle fiber function with exercise or nutrition countermeasures during 60 days of bed rest publication-title: Am J Physiol Regul Integr Comp Physiol – volume: 84 start-page: 475 year: 2006 end-page: 482 article-title: The underappreciated role of muscle in health and disease publication-title: Am J Clin Nutr – volume: 136 start-page: 227S year: 2006 end-page: 231S article-title: Signaling pathways and molecular mechanisms through which branched‐chain amino acids mediate translational control of protein synthesis publication-title: J Nutr – volume: 91 start-page: 4836 year: 2006 end-page: 4841 article-title: Atrophy and impaired muscle protein synthesis during prolonged inactivity and stress publication-title: J Clin Endocrinol Metab – volume: 21 start-page: 140 year: 2007 end-page: 155 article-title: Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases publication-title: FASEB J – volume: 66 start-page: 799 year: 2004 end-page: 828 article-title: Control of the size of the human muscle mass publication-title: Annu Rev Physiol – volume: 10 start-page: 31 year: 2005 end-page: 34 article-title: Maintenance of the musculoskeletal mass by control of protein turnover: the concept of anabolic resistance and its relevance to the transplant recipient publication-title: Ann Transplant – volume: 291 start-page: E1197 year: 2006 end-page: E1205 article-title: Maximal lengthening contractions increase p70, S6 kinase phosphorylation in human skeletal muscle in the absence of nutritional supply publication-title: Am J Physiol Endocrinol Metab – volume: 28 start-page: 1429 year: 2008 end-page: 1442 article-title: A novel mechanism for the control of translation initiation by amino acids, mediated by phosphorylation of eukaryotic initiation factor 2B publication-title: Mol Cell Biol – volume: 287 start-page: E1 year: 2004 end-page: E7 article-title: Branched‐chain amino acids increase p70S6k phosphorylation in human skeletal muscle after resistance exercise publication-title: Am J Physiol Endocrinol Metab – volume: 25 start-page: 6423 year: 2006 end-page: 6435 article-title: When translation meets transformation: the mTOR story publication-title: Oncogene – volume: 558 start-page: 381 year: 2004 end-page: 388 article-title: Short‐term bed rest impairs amino acid‐induced protein anabolism in humans publication-title: J Physiol – volume: 105 start-page: 241 year: 2008 end-page: 248 article-title: Resistance training and timed essential amino acids protect against the loss of muscle mass and strength during 28 days of bed rest and energy deficit publication-title: J Appl Physiol – volume: 403 start-page: 217 year: 2007 end-page: 234 article-title: Signalling to translation: how signal transduction pathways control the protein synthetic machinery publication-title: Biochem J – volume: 72 start-page: 503 year: 1987 end-page: 509 article-title: Decrease in human quadriceps muscle protein turnover consequent upon leg immobilization publication-title: Clin Sci (Lond) – volume: 99 start-page: 1085 year: 2005 end-page: 1092 article-title: Sex‐based differences in skeletal muscle function and morphology with short‐term limb immobilization publication-title: J Appl Physiol – volume: 31 start-page: 518 year: 2006 end-page: 529 article-title: Addition of glutamine to essential amino acids and carbohydrate does not enhance anabolism in young human males following exercise publication-title: Appl Physiol Nutr Metab – volume: 277 start-page: C152 year: 1999 end-page: C162 article-title: Focal adhesion proteins FAK and paxillin increase in hypertrophied skeletal muscle publication-title: Am J Physiol Endocrinol Metab – volume: 21 start-page: 362 year: 2006 end-page: 369 article-title: The mTOR pathway in the control of protein synthesis publication-title: Physiology (Bethesda) – volume: 181 start-page: 345 year: 2004 end-page: 357 article-title: Efficacy of a gravity‐independent resistance exercise device as a countermeasure to muscle atrophy during 29‐day bed rest publication-title: Acta Physiol Scand – volume: 50 start-page: 327 year: 2006 end-page: 336 article-title: Integrins, muscle agrin and sarcoglycans during muscular inactivity conditions: an immunohistochemical study publication-title: Eur J Histochem – volume: 32 start-page: 1132 year: 2007 end-page: 1138 article-title: Minimal whey protein with carbohydrate stimulates muscle protein synthesis following resistance exercise in trained young men publication-title: Appl Physiol Nutr Metab – volume: 17 start-page: 1807 year: 2006 end-page: 1819 article-title: Protein degradation by the ubiquitin‐proteasome pathway in normal and disease states publication-title: J Am Soc Nephrol – volume: 19 start-page: 422 year: 2005 end-page: 424 article-title: Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle publication-title: FASEB J – volume: 582 start-page: 813 year: 2007 end-page: 823 article-title: Nutrient signalling in the regulation of human muscle protein synthesis publication-title: J Physiol – volume: 295 start-page: E595 year: 2008 end-page: E604 article-title: Disassociation between the effects of amino acids and insulin on signalling, ubiquitin‐ligases and protein turnover in human muscle publication-title: Am J Physiol Endocrinol Metab – volume: 85 start-page: 1031 year: 2007 end-page: 1040 article-title: Consumption of fluid skim milk promotes greater muscle protein accretion following resistance exercise than an isonitrogenous and isoenergetic soy protein beverage publication-title: Am J Clin Nutr – ident: e_1_2_5_22_1 doi: 10.1152/jappl.2001.90.3.1174 – ident: e_1_2_5_46_1 doi: 10.1152/japplphysiol.90558.2008 – ident: e_1_2_5_48_1 doi: 10.1152/japplphysiol.00560.2007 – ident: e_1_2_5_14_1 doi: 10.1152/ajpendo.00582.2007 – ident: e_1_2_5_11_1 doi: 10.1152/ajpendo.00415.2005 – ident: e_1_2_5_58_1 doi: 10.1152/japplphysiol.00247.2005 – ident: e_1_2_5_32_1 doi: 10.1007/s004210100467 – ident: e_1_2_5_35_1 doi: 10.1210/jc.2003-032159 – ident: e_1_2_5_43_1 doi: 10.1038/emboj.2008.39 – ident: e_1_2_5_25_1 doi: 10.1093/ajcn/82.5.941 – ident: e_1_2_5_5_1 doi: 10.1038/sj.onc.1209887 – ident: e_1_2_5_54_1 doi: 10.1128/MCB.01512-07 – ident: e_1_2_5_9_1 doi: 10.1152/japplphysiol.01346.2007 – ident: e_1_2_5_44_1 doi: 10.1093/jn/135.7.1824S – ident: e_1_2_5_51_1 doi: 10.1111/j.1530-0277.2007.00548.x – ident: e_1_2_5_21_1 doi: 10.1073/pnas.251541198 – ident: e_1_2_5_56_1 doi: 10.1093/ajcn/85.4.1031 – ident: e_1_2_5_18_1 doi: 10.1152/ajpcell.1999.277.1.C152 – ident: e_1_2_5_24_1 doi: 10.1152/ajpregu.00292.2007 – ident: e_1_2_5_39_1 doi: 10.1146/annurev.physiol.66.052102.134444 – ident: e_1_2_5_3_1 doi: 10.1111/j.1365-201X.2004.01293.x – ident: e_1_2_5_23_1 doi: 10.1152/ajpendo.90411.2008 – ident: e_1_2_5_57_1 doi: 10.1093/ajcn/84.3.475 – ident: e_1_2_5_7_1 doi: 10.1111/j.1469-7793.2001.0575f.x – ident: e_1_2_5_20_1 doi: 10.1042/cs0720503 – ident: e_1_2_5_47_1 doi: 10.1152/ajpregu.00761.2007 – volume: 50 start-page: 327 year: 2006 ident: e_1_2_5_4_1 article-title: Integrins, muscle agrin and sarcoglycans during muscular inactivity conditions: an immunohistochemical study publication-title: Eur J Histochem – ident: e_1_2_5_28_1 doi: 10.1093/jn/136.1.227S – ident: e_1_2_5_37_1 doi: 10.1042/BJ20070024 – ident: e_1_2_5_26_1 doi: 10.1152/ajpendo.00430.2003 – ident: e_1_2_5_36_1 doi: 10.1016/j.nut.2004.04.009 – ident: e_1_2_5_49_1 doi: 10.1113/jphysiol.2006.118042 – ident: e_1_2_5_38_1 doi: 10.1042/bst0290541 – ident: e_1_2_5_53_1 doi: 10.1152/physiol.00024.2006 – ident: e_1_2_5_27_1 doi: 10.1152/japplphysiol.00221.2002 – ident: e_1_2_5_8_1 doi: 10.1113/jphysiol.2003.050674 – ident: e_1_2_5_30_1 doi: 10.1096/fj.03-0610com – volume: 9 start-page: 155 year: 2002 ident: e_1_2_5_10_1 article-title: Skeletal muscle protein composition following 5 weeks of ULLS and resistance exercise countermeasures publication-title: J Gravit Physiol – ident: e_1_2_5_45_1 doi: 10.1139/H07-076 – ident: e_1_2_5_19_1 doi: 10.1113/jphysiol.2007.134593 – ident: e_1_2_5_34_1 doi: 10.1210/jc.2004-1702 – ident: e_1_2_5_16_1 doi: 10.1152/ajpendo.00141.2006 – ident: e_1_2_5_42_1 doi: 10.1096/fj.06-6604com – ident: e_1_2_5_55_1 doi: 10.1139/h06-028 – ident: e_1_2_5_13_1 doi: 10.1113/jphysiol.2007.142828 – ident: e_1_2_5_31_1 doi: 10.1152/ajpendo.00387.2004 – volume: 10 start-page: 31 year: 2005 ident: e_1_2_5_40_1 article-title: Maintenance of the musculoskeletal mass by control of protein turnover: the concept of anabolic resistance and its relevance to the transplant recipient publication-title: Ann Transplant – ident: e_1_2_5_6_1 doi: 10.1113/jphysiol.2004.066365 – ident: e_1_2_5_17_1 doi: 10.1152/ajpendo.1996.270.4.E627 – ident: e_1_2_5_33_1 doi: 10.1210/jc.2006-0651 – ident: e_1_2_5_50_1 doi: 10.1152/japplphysiol.00180.2006 – ident: e_1_2_5_15_1 doi: 10.1113/jphysiol.2006.113175 – ident: e_1_2_5_2_1 doi: 10.1152/japplphysiol.00346.2003 – ident: e_1_2_5_41_1 doi: 10.1152/jappl.1989.67.1.19 – ident: e_1_2_5_29_1 doi: 10.1681/ASN.2006010083 – ident: e_1_2_5_12_1 doi: 10.1096/fj.04-2640fje – ident: e_1_2_5_52_1 doi: 10.1128/MCB.25.7.2558-2572.2005 – reference: 17213042 - Eur J Histochem. 2006 Oct-Dec;50(4):327-36 – reference: 16984982 - J Clin Endocrinol Metab. 2006 Dec;91(12):4836-41 – reference: 17901116 - J Physiol. 2007 Nov 15;585(Pt 1):241-51 – reference: 14977422 - Annu Rev Physiol. 2004;66:799-828 – reference: 14718385 - FASEB J. 2004 Jan;18(1):39-51 – reference: 16280423 - Am J Clin Nutr. 2005 Nov;82(5):941-8 – reference: 17037086 - Ann Transplant. 2005;10(4):31-4 – reference: 2668254 - J Appl Physiol (1985). 1989 Jul;67(1):19-23 – reference: 17413102 - Am J Clin Nutr. 2007 Apr;85(4):1031-40 – reference: 14600160 - J Appl Physiol (1985). 2003 Dec;95(6):2185-201 – reference: 15572656 - Am J Physiol Endocrinol Metab. 2005 Jun;288(6):E1153-9 – reference: 18535133 - J Appl Physiol (1985). 2008 Sep;105(3):902-6 – reference: 17218363 - J Physiol. 2007 Mar 15;579(Pt 3):877-92 – reference: 16835402 - Am J Physiol Endocrinol Metab. 2006 Dec;291(6):E1197-205 – reference: 15356032 - J Clin Endocrinol Metab. 2004 Sep;89(9):4351-8 – reference: 17670860 - Am J Physiol Regul Integr Comp Physiol. 2007 Oct;293(4):R1722-7 – reference: 18483167 - J Appl Physiol (1985). 2008 Jul;105(1):241-8 – reference: 17116744 - FASEB J. 2007 Jan;21(1):140-55 – reference: 11717410 - Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14440-5 – reference: 12183515 - J Appl Physiol (1985). 2002 Sep;93(3):1168-80 – reference: 18160716 - Mol Cell Biol. 2008 Mar;28(5):1429-42 – reference: 18056791 - Am J Physiol Endocrinol Metab. 2008 Feb;294(2):E392-400 – reference: 16960159 - Am J Clin Nutr. 2006 Sep;84(3):475-82 – reference: 15598679 - J Clin Endocrinol Metab. 2005 Mar;90(3):1453-9 – reference: 15196095 - Acta Physiol Scand. 2004 Jul;181(3):345-57 – reference: 11306673 - J Physiol. 2001 Apr 15;532(Pt 2):575-9 – reference: 15212752 - Nutrition. 2004 Jul-Aug;20(7-8):689-95 – reference: 18577697 - Am J Physiol Endocrinol Metab. 2008 Sep;295(3):E595-604 – reference: 11498025 - Biochem Soc Trans. 2001 Aug;29(Pt 4):541-7 – reference: 11606016 - Eur J Appl Physiol. 2001 Sep;85(5):466-71 – reference: 16263770 - Am J Physiol Endocrinol Metab. 2006 Apr;290(4):E731-8 – reference: 17376031 - Biochem J. 2007 Apr 15;403(2):217-34 – reference: 15987873 - J Nutr. 2005 Jul;135(7):1824S-1828S – reference: 15767663 - Mol Cell Biol. 2005 Apr;25(7):2558-72 – reference: 18059587 - Appl Physiol Nutr Metab. 2007 Dec;32(6):1132-8 – reference: 17641219 - J Appl Physiol (1985). 2007 Oct;103(4):1242-50 – reference: 16763108 - J Appl Physiol (1985). 2006 Oct;101(4):1136-48 – reference: 18094071 - Am J Physiol Regul Integr Comp Physiol. 2008 Mar;294(3):R939-47 – reference: 10409118 - Am J Physiol. 1999 Jul;277(1 Pt 1):C152-62 – reference: 18337751 - EMBO J. 2008 Apr 9;27(7):1005-16 – reference: 15002527 - J Gravit Physiol. 2002 Jul;9(1):P155-6 – reference: 16365087 - J Nutr. 2006 Jan;136(1 Suppl):227S-31S – reference: 2435445 - Clin Sci (Lond). 1987 Apr;72(4):503-9 – reference: 17478528 - J Physiol. 2007 Jul 15;582(Pt 2):813-23 – reference: 11181634 - J Appl Physiol (1985). 2001 Mar;90(3):1174-83; discussion 1165 – reference: 17041627 - Oncogene. 2006 Oct 16;25(48):6423-35 – reference: 14998784 - Am J Physiol Endocrinol Metab. 2004 Jul;287(1):E1-7 – reference: 16990457 - Physiology (Bethesda). 2006 Oct;21:362-9 – reference: 15131238 - J Physiol. 2004 Jul 15;558(Pt 2):381-8 – reference: 16738015 - J Am Soc Nephrol. 2006 Jul;17(7):1807-19 – reference: 8928769 - Am J Physiol. 1996 Apr;270(4 Pt 1):E627-33 – reference: 12909668 - J Physiol. 2003 Oct 1;552(Pt 1):315-24 – reference: 18028527 - Alcohol Clin Exp Res. 2008 Jan;32(1):128-37 – reference: 17111006 - Appl Physiol Nutr Metab. 2006 Oct;31(5):518-29 – reference: 16873412 - J Physiol. 2006 Oct 15;576(Pt 2):613-24 – reference: 15596483 - FASEB J. 2005 Mar;19(3):422-4 – reference: 15860685 - J Appl Physiol (1985). 2005 Sep;99(3):1085-92 |
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| Snippet | We tested the hypothesis that increasing blood amino acid (AA) availability would counter the physical inactivity-induced
reduction in muscle protein... We tested the hypothesis that increasing blood amino acid (AA) availability would counter the physical inactivity‐induced reduction in muscle protein... We tested the hypothesis that increasing blood amino acid (AA) availability would counter the physical inactivity-induced reduction in muscle protein... |
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| SubjectTerms | Adult Amino Acids - administration & dosage Amino Acids - metabolism Amino Acids - pharmacology Amino Acids, Essential - blood Amino Acids, Essential - metabolism Dose-Response Relationship, Drug Elongation Factor 2 Kinase - metabolism Female Focal Adhesion Protein-Tyrosine Kinases - metabolism Glycogen Synthase Kinase 3 - metabolism Glycogen Synthase Kinase 3 beta Humans Immobilization - methods Infusions, Intravenous Insulin - blood Male Muscle Proteins - biosynthesis Muscle Strength - drug effects Muscle Strength - physiology Myofibrils - drug effects Myofibrils - metabolism Myofibrils - physiology Phosphorylation - drug effects Protein Kinases - metabolism Proto-Oncogene Proteins c-akt - metabolism Quadriceps Muscle - drug effects Quadriceps Muscle - metabolism Quadriceps Muscle - physiology Ribosomal Protein S6 Kinases, 70-kDa - metabolism Skeletal Muscle and Exercise TOR Serine-Threonine Kinases Ubiquitination - drug effects Young Adult |
| Title | Immobilization induces anabolic resistance in human myofibrillar protein synthesis with low and high dose amino acid infusion |
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