Abstract:Ingestion of protein is crucial for maintenance of a variety of body functions and within the scope of this review we will specifically focus on the regulation of skeletal muscle mass. A quantitative limitation exists as to how much muscle protein the body can synthesize in response to protein intake. Ingestion of excess protein exerts an unwanted load to the body and therefore, it is important to find the least amount of protein that provides the maximal hypertrophic stimulus. Hence, research has focused on r… Show more
“…Previous studies clearly suggested that fast-digested and slow-digested proteins have synergistic effects on muscle anabolism (Dideriksen et al, 2013;Boirie et al, 1997).…”
While effects of the two classes of proteins found in milk (i.e. soluble proteins, including whey, and casein) on muscle protein synthesis have been well investigated after a single bout of resistance exercise (RE), the combined effects of these two proteins on the muscle responses to resistance training (RT) have not yet been investigated. Therefore, the aim of this study was to examine the effects of protein supplementation varying by the ratio between milk soluble proteins (fast-digested protein) and casein (slow-digested protein) on the muscle to a 9-week RT program. In a double-blind protocol, 31 resistance-trained men, were assigned to 3 groups receiving a drink containing 20g of protein comprising either 100% of fast protein (FP(100), n=10), 50% of fast and 50% of slow proteins (FP(50), n=11) or 20% of fast protein and 80% of casein (FP(20), n=10) at the end of training bouts. Body composition (DXA), and maximal strength in dynamic and isometric were analyzed before and after RT. Moreover, blood plasma aminoacidemia kinetic after RE was measured. The results showed a higher leucine bioavailability after ingestion of FP(100) and FP(50) drinks, when compared with FP (20) (p<0.05). However, the RT-induced changes in lean body mass (p<0.01), dynamic (p<0.01), and isometric muscle strength (p<0.05) increased similarly in all experimental groups. To conclude, compared to the FP(20) group, the higher rise in plasma amino acids following the ingestion of FP(100) and FP(50) did not lead to higher muscle long-term adaptations.
“…Previous studies clearly suggested that fast-digested and slow-digested proteins have synergistic effects on muscle anabolism (Dideriksen et al, 2013;Boirie et al, 1997).…”
While effects of the two classes of proteins found in milk (i.e. soluble proteins, including whey, and casein) on muscle protein synthesis have been well investigated after a single bout of resistance exercise (RE), the combined effects of these two proteins on the muscle responses to resistance training (RT) have not yet been investigated. Therefore, the aim of this study was to examine the effects of protein supplementation varying by the ratio between milk soluble proteins (fast-digested protein) and casein (slow-digested protein) on the muscle to a 9-week RT program. In a double-blind protocol, 31 resistance-trained men, were assigned to 3 groups receiving a drink containing 20g of protein comprising either 100% of fast protein (FP(100), n=10), 50% of fast and 50% of slow proteins (FP(50), n=11) or 20% of fast protein and 80% of casein (FP(20), n=10) at the end of training bouts. Body composition (DXA), and maximal strength in dynamic and isometric were analyzed before and after RT. Moreover, blood plasma aminoacidemia kinetic after RE was measured. The results showed a higher leucine bioavailability after ingestion of FP(100) and FP(50) drinks, when compared with FP (20) (p<0.05). However, the RT-induced changes in lean body mass (p<0.01), dynamic (p<0.01), and isometric muscle strength (p<0.05) increased similarly in all experimental groups. To conclude, compared to the FP(20) group, the higher rise in plasma amino acids following the ingestion of FP(100) and FP(50) did not lead to higher muscle long-term adaptations.
“…[69][70][71][72] Because protein ingestion is crucial for the maintenance of a variety of body functions, the requirements of protein in the elderly are a major factor in maintaining skeletal muscle mass; the amount of protein ingested that induces maximal muscle protein synthesis must be higher in elderly than in young individuals in order to combat anabolic resistance in the elderly. 5,[73][74][75][76][77] Dysregulation of autophagy [78][79][80] contributes notably to aging. Autophagy, a lysosomal process involved in the maintenance of cellular homeostasis, is inhibited by the insulin-amino acid-mTOR signaling pathway that controls both protein synthesis and longevity (see next paragraph).…”
Section: Impact Of Aging On Regulation Of Glutamine Metabolismmentioning
Glutamine, reviewed extensively in the last century, is a key substrate for the splanchnic bed in the whole body and is a nutrient of particular interest in gastrointestinal research. A marked decrease in the plasma glutamine concentration has recently been observed in neonates and adults during acute illness and stress. Although some studies in newborns have shown parenteral and enteral supplementation with glutamine to be of benefit (by decreasing proteolysis and activating the immune system), clinical trials have not demonstrated prolonged advantages such as reductions in mortality or risk of infections in adults. In addition, glutamine is not able to combat the muscle wasting associated with disease or age-related sarcopenia. Oral glutamine supplementation initiated before advanced age in rats increases gut mass and improves the villus height of mucosa, thereby preventing the gut atrophy encountered in advanced age. Enterocytes from very old rats continuously metabolize glutamine into citrulline, which allowed, for the first time, the use of citrulline as a noninvasive marker of intestinal atrophy induced by advanced age.
“…However, while the decrease in the male participants was statistically significant, the decrease in the female participants was not statistically significant. A plausible reason for this decrease in total protein value has been suggested [21][22][23], to be due to increased demand of glucogenic amino acids for the generation of energy leading to increased degradation of proteins. A similar result was obtained for plasma albumin.…”
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