scholarly journals The effect of four different feeding regimens from rearing period to sexual maturity on breast muscle protein turnover in broiler breeder parent stock

2017 ◽  
Vol 96 (5) ◽  
pp. 1219-1227 ◽  
Author(s):  
Karen Vignale ◽  
Justina V. Caldas ◽  
Judy A. England ◽  
Nirun Boonsinchai ◽  
Phiphob Sodsee ◽  
...  
Keyword(s):  
Protein Turnover ◽  
Sexual Maturity ◽  
Muscle Protein ◽  
Breast Muscle ◽  
Broiler Breeder ◽  
Muscle Protein Turnover ◽  
Parent Stock

Skeletal and cardiac muscle protein turnover during cold acclimation in young rats

2000 ◽  
Vol 278 (3) ◽  
pp. R705-R711 ◽  
Author(s):  
T. A. McAllister ◽  
J. R. Thompson ◽  
S. E. Samuels
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Cardiac Muscle ◽  
Cold Acclimation ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Muscle Protein Turnover ◽  
Protein Mass ◽  
The Absolute

The effect of long-term cold exposure on skeletal and cardiac muscle protein turnover was investigated in young growing animals. Two groups of 36 male 28-day-old rats were maintained at either 5°C (cold) or 25°C (control). Rates of protein synthesis and degradation were measured in vivo on days 5, 10, 15, and 20. Protein mass by day 20 was ∼28% lower in skeletal muscle (gastrocnemius and soleus) and ∼24% higher in heart in cold compared with control rats ( P < 0.05). In skeletal muscle, the fractional rates of protein synthesis ( k syn) and degradation ( k deg) were not significantly different between cold and control rats, although k syn was lower (approximately −26%) in cold rats on day 5; consequent to the lower protein mass, the absolute rates of protein synthesis (approximately −21%; P < 0.05) and degradation (approximately −13%; P < 0.1) were lower in cold compared with control rats. In heart, overall, k syn(approximately +12%; P < 0.1) and k deg(approximately +22%; P < 0.05) were higher in cold compared with control rats; consequently, the absolute rates of synthesis (approximately +44%) and degradation (approximately +54%) were higher in cold compared with control rats ( P < 0.05). Plasma triiodothyronine concentration was higher ( P < 0.05) in cold compared with control rats. These data indicate that long-term cold acclimation in skeletal muscle is associated with the establishment of a new homeostasis in protein turnover with decreased protein mass and normal fractional rates of protein turnover. In heart, unlike skeletal muscle, rates of protein turnover did not appear to immediately return to normal as increased rates of protein turnover were observed beyond day 5. These data also indicate that increased rates of protein turnover in skeletal muscle are unlikely to contribute to increased metabolic heat production during cold acclimation.

scholarly journals Reduction of muscle protein turnover in rats by a high protein diet.

1987 ◽  
Vol 51 (1) ◽  
pp. 261-262
Author(s):  
Ryuhei FUNABUCI ◽  
Kouichi SAITO ◽  
Kazumi YAGASAKI
Keyword(s):  
Protein Turnover ◽  
Muscle Protein ◽  
High Protein Diet ◽  
High Protein ◽  
Protein Diet ◽  
Muscle Protein Turnover

Expression of genes related to the regulation of muscle protein turnover in Angus and Nellore bulls1

2016 ◽  
Vol 94 (4) ◽  
pp. 1472-1481
Author(s):  
K. C. Busato ◽  
R. A. Gomes ◽  
M. M. Ladeira ◽  
M. S. Duarte ◽  
N. C. Freitas ◽  
...  
Keyword(s):  
Protein Turnover ◽  
Muscle Protein ◽  
Muscle Protein Turnover ◽  
Expression Of Genes

Influence of sepsis in rats on muscle protein turnover in vivo and in tissue incubated under different in vitro conditions

Metabolism ◽  
1991 ◽  
Vol 40 (3) ◽  
pp. 247-251 ◽  
Author(s):  
Marianne Hall-Angerås ◽  
Ulf Angerås ◽  
Daniel von Allmen ◽  
Takashi Higashiguchi ◽  
Oded Zamir ◽  
...  
Keyword(s):  
Protein Turnover ◽  
Muscle Protein ◽  
Muscle Protein Turnover

scholarly journals The effect of protein depletion and repletion on muscle-protein turnover in the chick

1981 ◽  
Vol 194 (3) ◽  
pp. 811-819 ◽  
Author(s):  
M L MacDonald ◽  
R W Swick
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Control Diet ◽  
Breast Muscle ◽  
Synthesis Rate ◽  
Protein Depletion ◽  
Protein Mass ◽  
Fractional Rate

Rates of growth and protein turnover in the breast muscle of young chicks were measured in order to assess the roles of protein synthesis and degradation in the regulation of muscle mass. Rates of protein synthesis were measured in vivo by injecting a massive dose of L-[1-14C]valine, and rates of protein degradation were estimated as the difference between the synthesis rate and the growth rate of muscle protein. In chicks fed on a control diet for up to 7 weeks of age, the fractional rate of synthesis decreased from 1 to 2 weeks of age and then changed insignificantly from 2 to 7 weeks of age, whereas DNA activity was constant for 1 to 7 weeks. When 4-week-old chicks were fed on a protein-free diet for 17 days, the total amount of breast-muscle protein synthesized and degraded per day and the amount of protein synthesized per unit of DNA decreased. Protein was lost owing to a greater decrease in the rate of protein synthesis, as a result of the loss of RNA and a lowered RNA activity. When depleted chicks were re-fed the control diet, rapid growth was achieved by a doubling of the fractional synthesis rate by 2 days. Initially, this was a result of increased RNA activity; by 5 days, the RNA/DNA ratio also increased. There was no evidence of a decrease in the fractional degradation rate during re-feeding. These results indicate that dietary-protein depletion and repletion cause changes in breast-muscle protein mass primarily through changes in the rate of protein synthesis.

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.

Genetic studies on the muscle protein turnover rate of coturnix quail

1986 ◽  
Vol 24 (3-4) ◽  
pp. 207-216 ◽  
Author(s):  
Y. Maeda ◽  
K. Hayashi ◽  
T. Hashiguchi ◽  
S. Okamoto
Keyword(s):  
Protein Turnover ◽  
Turnover Rate ◽  
Muscle Protein ◽  
Genetic Studies ◽  
Muscle Protein Turnover ◽  
Coturnix Quail
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