The small intestine acts as interface and regulator between the gut lumen and the rest of the body and controls the degree and rate of transport of amino acids coming from dietary protein via the portal vein to the liver and the systemic circulation. To measure protein absorption, kinetics multicatheter animal (pig) models in combination with amino acid tracer technology are available. Dietary factors infuence the absorption rates from the lumen to the gut, metabolism of dietary component in the gut, and the release of amino acids to the portal circulation from digested protein. In a balanced-protein meal, the gut dietary amino acid utilization (30–50%) for gut protein synthesis will result in a labile protein pool in the gut that can be benefcial during the postabsorptive state. To enhance gut retention, amount and quality of protein and the presence of carbohydrate are major factors. Besides this the use of a slowly digestible protein or the presence of fber in the meal can increase retention further. During the absorption of low-quality protein meals, fewer amino acids are utilized by the gut, resulting in higher amounts of amino acid release to the portal circulation. Malnutrition or starvation, protein depletion, defciencies of specifc nutrients, or illness such as sepsis all inhibit the growth and change protein turnover of the intestinal mucosa and therefore affect absorption kinetics. Therefore, the kind of protein meal that has the most optimal absorption kinetics (the most benefcial) for gut and for the rest of the body depends on these (patho)physiological circumstances. Despite the absence of different absorption kinetics between protein, peptides, and amino acids, they could be benefcial in specifc circumstances.
Search Results
Absorption Kinetics of Amino Acids, Peptides, and Intact Proteins
Gabriella A.M. Ten Have, Marielle P.K.J. Engelen, Yvette C. Luiking, and Nicolaas E.P. Deutz
Bone Broth Unlikely to Provide Reliable Concentrations of Collagen Precursors Compared With Supplemental Sources of Collagen Used in Collagen Research
Rebekah D. Alcock, Gregory C. Shaw, and Louise M. Burke
Collagen is the most abundant body protein, constituting around one third of total protein stores. Within the extracellular matrix of musculoskeletal and connective tissues, collagen contributes to force transmission and joint stability, providing resistance to forces and sudden directional changes
Protein and Amino Acid Needs of the Strength Athlete
Peter W.R. Lemon
The debate regarding optimal protein/amino acid needs of strength athletes is an old one. Recent evidence indicates that actual requirements are higher than those of more sedentaty individuals, although this is not widely recognized. Some data even suggest that high protein/amino acid diets can enhance the development of muscle mass and strength when combined with heavy resistance exercise training. Novices may have higher needs than experienced strength athletes, and substantial interindividual variability exists. Perhaps the most important single factor determining absolute protein/amino acid need is the adequacy of energy intake. Present data indicate that strength athletes should consume approximately 12-15% of their daily total energy intake as protein, or about 1.5-2.0 g protein/
Nutrition for Ultramarathon Running: Trail, Track, and Road
Ricardo J.S. Costa, Beat Knechtle, Mark Tarnopolsky, and Martin D. Hoffman
consumption of sufficient protein to meet daily nitrogen balance (i.e., 1.2–2.0 g·kg −1 ·day −1 ), to support tissue recovery and adaptations ( Phillips & van Loon, 2011 ; Tarnopolsky et al., 1988 ). Habitual dietary protein needs for elite endurance athletes are estimated to be 1.6–1.8 g·kg −1 ·day −1
Exploring the Association Between Physical Activity, Sedentary Behavior, and High-Sensitivity C-Reactive Protein Among Stroke Survivors
Mike Pryzbek, Julie Richardson, Lehana Thabane, and Ada Tang
-reactive protein (hs-CRP), which is elevated in the presence of cardiovascular disease ( Rost et al., 2001 ). While systemic biomarker levels cannot pinpoint the specific location of inflammation, elevated hs-CRP is a reliable predictor of cardiovascular events ( Rost et al., 2001 ) and is an established risk
Muscle Protein Metabolism and the Sarcopenia of Aging
Kevin R. Short and K. Sreekumaran Nair
Loss of muscle mass, strength, and oxidative capacity accompanies normal aging in humans. The mechanisms responsible for these changes remain to be clearly defined. Muscle protein mass and function depend on protein turnover. Synthesis rate of the major muscle contractile protein, myosin heavy chain (MHC), and transcript levels of fast MHC isoforms decrease in association with strength reductions, while mitochondrial protein synthesis rate declines in parallel with activities of mitochondrial enzymes and maximal oxidative capacity (V̇O2max). Resistance exercise training increases the synthesis rate of MHC and transcript levels of the slow MHC isoform in older humans, along with increasing muscle strength. The relationship between the synthesis of muscle proteins, and muscle size and function, with aging and exercise training are discussed in this review.
Effect of an Amino Acid, Protein, and Carbohydrate Mixture on Net Muscle Protein Balance after Resistance Exercise
Elisabet Børsheim, Asle Aarsland, and Robert R. Wolfe
This study tests the hypotheses that (a) a mixture of whey protein, amino acids (AA), and carbohydrates (CHO) stimulates net muscle protein synthesis to a greater extent than isoenergetic CHO alone after resistance exercise; and (b) that the stimulatory effect of a protein, AA, and CHO mixture will last beyond the 1 st hour after intake. Eight subjects participated in 2 trials. In one (PAAC), they ingested 77.4 g CHO, 17.5 g whey protein, and 4.9 g AA 1 hr after resistance exercise. In the other (CON), 100 g CHO was ingested instead. They received a primed constant infusion of L-[2H5]-phenylalanine, and samples from femoral artery and vein, and biopsies from vastus lateralis were obtained. The area under the curve for net uptake of phenylalanine into muscle above pre-drink value was 128 ±42 mg • leg-1 (PAAC) versus 32 ± 10 mg - leg-1 (CON) for the 3 hr after the drink (p = .04). The net protein balance response to the mixture consisted of two components, one rapid immediate response, and a smaller delayed response about 90 min after drink, whereas in CON only a small delayed response was seen. We conclude that after resistance exercise, a mixture of whey protein, AA, and CHO stimulated muscle protein synthesis to a greater extent than isoenergetic CHO alone. Further, compared to previously reported findings, the addition of protein to an AA + CHO mixture seems to extend the anabolic effect.
Protein Metabolism and Age: Influence of Insulin and Resistance Exercise
Peter A. Farrell
Skeletal muscle proteins are constantly being synthesized and degraded, and the net balance between synthesis and degradation determines the resultant muscle mass. Biochemical pathways that control protein synthesis are complex, and the following must be considered: gene transcription, mRNA splicing, and transport to the cytoplasm; specific amino acyl-tRNA, messenger (mRNA), ribosomal (rRNA) availability; amino acid availability within the cell; the hormonal milieu; rates of mRNA translation; packaging in vesicles for some types of proteins; and post-translational processing such as glycation and phosphorylation/dephosphorylation. Each of these processes is responsive to the need for greater or lesser production of new proteins, and many states such as sepsis, uncontrolled diabetes, prolonged bed-rest, aging, chronic alcohol treatment, and starvation cause marked reductions in rates of skeletal muscle protein synthesis. In contrast, acute and chronic resistance exercise cause elevations in rates of muscle protein synthesis above rates found in nondiseased rested organisms, which are normally fed. Resistance exercise may be unique in this capacity. This chapter focuses on studies that have used exercise to elucidate mechanisms that explain elevations in rates of protein synthesis. Very few studies have investigated the effects of aging on these mechanisms; however, the literature that is available is reviewed.
mTOR-Dependent Control of Skeletal Muscle Protein Synthesis
John C. Lawrence Jr.
Muscle mass is influenced by many factors including genetically programmed changes, hormonal state, level of activity, and disease processes. Ultimately, whether or not a muscle hypertrophies or atrophies is determined by a simple relationship between the rates of protein synthesis and degradation. When synthesis exceeds degradation, the muscle hypertrophies, and vice versa. In contrast to this simple relationship, the processes that control muscle protein synthesis and degradation are complex. Recently, significant progress has been made in understanding the biochemical mechanisms that control the rate of translation initiation, which is generally the limiting phase in protein synthesis.
Control of Muscle Protein Synthesis as a Result of Contractile Activity and Amino Acid Availability: Implications for Protein Requirements
Michael J. Rennie
The major anabolic influences on muscle are feeding and contractile activity. As a result of feeding, anabolism occurs chiefly by increases in protein synthesis with minor changes in protein breakdown. Insulin has a permissive role in increasing synthesis, but the availability of amino acids is crucial for net anabolism. We have investigated the role of amino acids in stimulating muscle protein synthesis, the synergy between exercise and amino acid availability, and some of the signaling elements involved. The results suggest that muscle is acutely sensitive to amino acids, that exercise probably increases the anabolic effects of amino acids by a separate pathway, and that for this reason it is unlikely that accustomed physical exercise increases protein requirements.
