Effects of dietary amino acid levels and ambient temperature on mixed muscle protein turnover in Pectoralis major during finisher feeding period in two broiler lines

2020 ◽  
Vol 104 (5) ◽  
pp. 1351-1364 ◽  
Author(s):  
Pramir Maharjan ◽  
Garret Mullenix ◽  
Katie Hilton ◽  
Antonio Beitia ◽  
Jordan Weil ◽  
...  
Keyword(s):  
Amino Acid ◽  
Ambient Temperature ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Pectoralis Major ◽  
Feeding Period ◽  
Muscle Protein Turnover ◽  
Dietary Amino Acid ◽  
Amino Acid Levels

Human muscle protein synthesis and breakdown during and after exercise

2009 ◽  
Vol 106 (6) ◽  
pp. 2026-2039 ◽  
Author(s):  
Vinod Kumar ◽  
Philip Atherton ◽  
Kenneth Smith ◽  
Michael J. Rennie
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Protein Turnover ◽  
Acute Exercise ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Mitochondrial Protein ◽  
Human Muscle ◽  
Muscle Protein Turnover ◽  
Amino Acid Availability

Skeletal muscle demonstrates extraordinary mutability in its responses to exercise of different modes, intensity, and duration, which must involve alterations of muscle protein turnover, both acutely and chronically. Here, we bring together information on the alterations in the rates of synthesis and degradation of human muscle protein by different types of exercise and the influences of nutrition, age, and sexual dimorphism. Where possible, we summarize the likely changes in activity of signaling proteins associated with control of protein turnover. Exercise of both the resistance and nonresistance types appears to depress muscle protein synthesis (MPS), whereas muscle protein breakdown (MPB) probably remains unchanged during exercise. However, both MPS and MPB are elevated after exercise in the fasted state, when net muscle protein balance remains negative. Positive net balance is achieved only when amino acid availability is increased, thereby raising MPS markedly. However, postexercise-increased amino acid availability is less important for inhibiting MPB than insulin, the secretion of which is stimulated most by glucose availability, without itself stimulating MPS. Exercise training appears to increase basal muscle protein turnover, with differential responses of the myofibrillar and mitochondrial protein fractions to acute exercise in the trained state. Aging reduces the responses of myofibrillar protein and anabolic signaling to resistance exercise. There appear to be few, if any, differences in the response of young women and young men to acute exercise, although there are indications that, in older women, the responses may be blunted more than in older men.

Increased rates of muscle protein turnover and amino acid transport after resistance exercise in humans

1995 ◽  
Vol 268 (3) ◽  
pp. E514-E520 ◽  
Author(s):  
G. Biolo ◽  
S. P. Maggi ◽  
B. D. Williams ◽  
K. D. Tipton ◽  
R. R. Wolfe
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Resistance Exercise ◽  
Amino Acid Transport ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Acid Transport ◽  
Isotopic Tracers ◽  
Muscle Protein Turnover ◽  
Synthesis And Degradation

The rates of protein synthesis and degradation and of amino acid transport were determined in the leg muscle of untrained postabsorptive normal volunteers at rest and approximately 3 h after a resistance exercise routine. The methodology involved use of stable isotopic tracers of amino acids, arteriovenous catheterization of the femoral vessels, and biopsy of the vastus lateralis muscle. During postexercise recovery, the rate of intramuscular phenylalanine utilization for protein synthesis increased above the basal value by 108 +/- 18%, whereas the rate of release from proteolysis increased by 51 +/- 17%. Muscle protein balance improved (P < 0.05) after exercise but did not become positive (from -15 +/- 12 to -6 +/- 3 nmol phenylalanine.min-1.100 ml leg volume-1). After exercise, rates of inward transport of leucine, lysine, and alanine increased (P < 0.05) above the basal state from 132 +/- 16 to 208 +/- 29, from 122 +/- 8 to 260 +/- 8, and from 384 +/- 71 to 602 +/- 89 nmol.min-1.100 ml leg-1, respectively. Transport of phenylalanine did not change significantly. These results indicate that, during recovery after resistance exercise, muscle protein turnover is increased because of an acceleration of synthesis and degradation. A postexercise acceleration of amino acid transport may contribute to the relatively greater stimulation of protein synthesis.

The effect of systemic hyperinsulinemia with concomitant amino acid infusion on skeletal muscle protein turnover in the human forearm

Metabolism ◽  
1994 ◽  
Vol 43 (1) ◽  
pp. 70-78 ◽  
Author(s):  
Elliot Newman ◽  
Martin J. Heslin ◽  
Ronald F. Wolf ◽  
Peter W.T. Pisters ◽  
Murray F. Brennan
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Skeletal Muscle Protein ◽  
Acid Infusion ◽  
Amino Acid Infusion ◽  
Muscle Protein Turnover ◽  
Human Forearm

Amino acid control of muscle protein turnover in renal disease

2005 ◽  
Vol 15 (1) ◽  
pp. 34-38 ◽  
Author(s):  
Arny A. Ferrando ◽  
Dominic Raj ◽  
Robert R. Wolfe
Keyword(s):  
Amino Acid ◽  
Renal Disease ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Muscle Protein Turnover ◽  
Acid Control
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