scholarly journals Supplementation of a suboptimal protein dose with leucine or essential amino acids: effects on myofibrillar protein synthesis at rest and following resistance exercise in men

2012 ◽  
Vol 590 (11) ◽  
pp. 2751-2765 ◽  
Author(s):  
Tyler A. Churchward-Venne ◽  
Nicholas A. Burd ◽  
Cameron J. Mitchell ◽  
Daniel W. D. West ◽  
Andrew Philp ◽  
...  
2018 ◽  
Vol 314 (5) ◽  
pp. E457-E467 ◽  
Author(s):  
Jorn Trommelen ◽  
Imre W. K. Kouw ◽  
Andrew M. Holwerda ◽  
Tim Snijders ◽  
Shona L. Halson ◽  
...  

The purpose of this study was to determine the impact of ingesting 30 g casein protein with and without 2 g free leucine before sleep on myofibrillar protein synthesis rates during postexercise overnight recovery. Thirty-six healthy young men performed a single bout of resistance-type exercise in the evening (1945) after a full day of dietary standardization. Thirty minutes before sleep (2330), subjects ingested 30 g intrinsically l-[1-13C]phenylalanine-labeled protein with (PRO+leu, n = 12) or without (PRO, n = 12) 2 g free leucine, or a noncaloric placebo (PLA, n = 12). Continuous intravenous l-[ ring-2H5]phenylalanine, l-[1-13C]leucine, and l-[ ring-2H2]tyrosine infusions were applied. Blood and muscle tissue samples were collected to assess whole body protein net balance, myofibrillar protein synthesis rates, and overnight incorporation of dietary protein-derived amino acids into myofibrillar protein. Protein ingestion before sleep improved overnight whole body protein net balance ( P < 0.001). Myofibrillar protein synthesis rates did not differ significantly between treatments as assessed by l-[ ring-2H5]phenylalanine (0.057 ± 0.002, 0.055 ± 0.002, and 0.055 ± 0.004%/h for PLA, PRO, and PRO+leu, respectively; means ± SE; P = 0.850) or l-[1-13C]leucine (0.080 ± 0.004, 0.073 ± 0.004, and 0.083 ± 0.006%/h, respectively; P = 0.328). Myofibrillar l-[1-13C]phenylalanine enrichments increased following protein ingestion but did not differ between the PRO and PRO+leu treatments. In conclusion, protein ingestion before sleep improves whole body protein net balance and provides amino acids that are incorporated into myofibrillar protein during sleep. However, the ingestion of 30 g casein protein with or without additional free leucine before sleep does not increase muscle protein synthesis rates during postexercise overnight recovery.


2018 ◽  
Vol 596 (21) ◽  
pp. 5119-5133 ◽  
Author(s):  
Joseph W. Beals ◽  
Sarah K. Skinner ◽  
Colleen F. McKenna ◽  
Elizabeth G. Poozhikunnel ◽  
Samee A. Farooqi ◽  
...  

2012 ◽  
Vol 9 (1) ◽  
pp. 57 ◽  
Author(s):  
Yifan Yang ◽  
Tyler A Churchward-Venne ◽  
Nicholas A Burd ◽  
Leigh Breen ◽  
Mark A Tarnopolsky ◽  
...  

2017 ◽  
Vol 28 (1) ◽  
pp. 116-125 ◽  
Author(s):  
A. Pérez-López ◽  
J. McKendry ◽  
M. Martin-Rincon ◽  
D. Morales-Alamo ◽  
B. Pérez-Köhler ◽  
...  

2012 ◽  
Vol 108 (6) ◽  
pp. 958-962 ◽  
Author(s):  
Nicholas A. Burd ◽  
Yifan Yang ◽  
Daniel R. Moore ◽  
Jason E. Tang ◽  
Mark A. Tarnopolsky ◽  
...  

We aimed to determine the effect of consuming pure isolated micellar casein or pure whey protein isolate on rates of myofibrillar protein synthesis (MPS) at rest and after resistance exercise in elderly men. Healthy elderly men (72 (sem 1) years; BMI 26·4 (sem 0·7) kg/m2) were divided into two groups (n 7 each) who received a primed, constant infusion of l-[ring-13C6]phenylalanine to measure MPS at rest and during 4 h of exercise recovery. Participants performed unilateral leg resistance exercise followed by the consumption of isonitrogenous quantities (20 g) of casein or whey. Blood essential amino acids and leucine concentration peaked 60 min post-drink and were greater in amplitude after whey protein ingestion (both, P < 0·05). MPS in the rested leg was 65 % higher (P = 0·002) after ingestion of whey (0·040 (sem 0·003) %/h) when compared with micellar casein (0·024 (sem 0·002) %/h). Similarly, resistance exercise-stimulated rates of MPS were greater (P < 0·001) after whey ingestion (0·059 (sem 0·005) %/h) v. micellar casein (0·035 (sem 0·002) %/h). We conclude that ingestion of isolated whey protein supports greater rates of MPS than micellar casein both at rest and after resistance exercise in healthy elderly men. This result is probably related to a greater hyperaminoacidaemia or leucinaemia with whey ingestion.


1999 ◽  
Vol 276 (4) ◽  
pp. E628-E634 ◽  
Author(s):  
Kevin D. Tipton ◽  
Arny A. Ferrando ◽  
Stuart M. Phillips ◽  
David Doyle ◽  
Robert R. Wolfe

We examined the response of net muscle protein synthesis to ingestion of amino acids after a bout of resistance exercise. A primed, constant infusion ofl-[ ring-2H5]phenylalanine was used to measure net muscle protein balance in three male and three female volunteers on three occasions. Subjects consumed in random order 1 liter of 1) a mixed amino acid (40 g) solution (MAA), 2) an essential amino acid (40 g) solution (EAA), and 3) a placebo solution (PLA). Arterial amino acid concentrations increased ∼150–640% above baseline during ingestion of MAA and EAA. Net muscle protein balance was significantly increased from negative during PLA ingestion (−50 ± 23 nmol ⋅ min−1 ⋅ 100 ml leg volume−1) to positive during MAA ingestion (17 ± 13 nmol ⋅ min−1 ⋅ 100 ml leg volume−1) and EAA (29 ± 14 nmol ⋅ min−1 ⋅ 100 ml leg volume−1; P < 0.05). Because net balance was similar for MAA and EAA, it does not appear necessary to include nonessential amino acids in a formulation designed to elicit an anabolic response from muscle after exercise. We concluded that ingestion of oral essential amino acids results in a change from net muscle protein degradation to net muscle protein synthesis after heavy resistance exercise in humans similar to that seen when the amino acids were infused.


2018 ◽  
Vol 58 (2) ◽  
pp. 583-595 ◽  
Author(s):  
Søren Reitelseder ◽  
Kasper Dideriksen ◽  
Jakob Agergaard ◽  
Nikolaj M. Malmgaard-Clausen ◽  
Rasmus L. Bechshoeft ◽  
...  

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