None of these factors are capable of bringing about muscle tissue accrual by themselves. Instead these factors complement each other and do so by facilitating the reduction of the breakdown or promotion of the synthesis of muscle protein. Some factors are only capable of positively effecting retainment or uptake of a single crucial amino acid while others have multifaceted roles to play. Most of these factors are not anabolic by themselves. Rather they contribute specific necessities to a central pool that together maximize anabolism. All of these factors modulate amino acids which come from protein.<\/p>\n
The Centerpiece \u2013 Protein<\/h3>\n
Quality<\/span><\/p>\n Infant formulas rely on bovine whey protein to mimic the nutritional content of human milk. Of critical importance in substituting for human milk is the inclusion of the highly nutritious alpha-Lactalbumin protein found in whey. Both bovine and human alpha-Lactalbumin contain very high amounts of the essential amino acids (tryptophan, phenylalanine + tyrosine, leucine, isoleucine, threonine, methionine + cysteine, lysine and valine). Of primary importance are the significant quantities of lysine, cysteine and tryptophan contained in alpha-Lactalbumin1<\/sup>. Unfortunately the processing through which protein undergoes in creating a humanly consumable product harms some of these amino acids. Tryptophan is a particularly unstable amino acid, and the heating of proteins at excessive temperatures will cause major reductions in tryptophan bioavailability 2<\/sup>. In addition the reaction between nitrogenous side chains of the amino acids and reducing sugars usually brings about a deterioration of the nutritional quality of the protein and lysine in particular is often lost. Lysine, tryptophan and methionine residues also react with oxidizing lipids and cause losses in the availability of lysine, tryptophan and sulfur-containing amino acids 3<\/sup>.<\/p>\n The important point is simply if loss of protein bioavailability is unacceptable for infant nutrition it should also be unacceptable to those seeking body transformation.<\/p>\n In the literature there has been considerable interest in the proposition that proteins of different biological quality and digestibility might be more or less efficient at supplying amino acids to muscle after exercise. Recent studies 4,5<\/sup> seem to demonstrate that whey proteins are superior to casein and soy in supplying amino acids for net muscle protein accretion.<\/p>\n Quality protein is the centerpiece around which tissue accrual evolves.<\/p>\n Why is protein the centerpiece?<\/span><\/p>\n <\/p>\n <\/p>\n Normally meals induce a transient increase in muscle protein synthesis (MPS) followed by muscle protein breakdown (MPB). In this manner tissue is maintained but there is no net protein synthesis thus no anabolism.<\/p>\n The authors of the Tipton<\/em> study from which the above quote derives established therein that ingestion of either whey protein or casein protein after exercise led to \u201cincreases in muscle protein net balance, resulting in net muscle protein synthesis despite different patterns of blood amino acid responses\u201d 6<\/sup>.<\/p>\n The general consensus from research in this area is that exercise induces protein degradation as well as protein synthesis. Ingestion of protein during this time period strongly tips the balance of degradation versus synthesis to that of overall protein synthesis.<\/p>\n There really is very little to be gained by spending a lot of time discussing the details of numerous studies which examine such things as:<\/p>\n Making Whey digest slowly<\/span><\/p>\n Most of the variability between the various protein sources lies in the digestion rate. Whey is a fast digesting protein and can be made to behave like the even speedier essential amino acids (EAA) by simply ingesting whey a little earlier. This is an effective pre-workout approach. Like-wise if a slower digestion rate is desired co-ingestion of viscous gels and soluble dietary fibers such as psyllium, pectin, guar gum and ispaghula will slow amino acid release either by increasing the time needed for intestinal absorption or slowing the rate of gastric emptying 7-11<\/sup>. In this manner whey can be made to behave as the slower releasing soy and casein proteins.<\/p>\n So while whey protein can be made to behave more like casein, casein can not be made to behave like whey.<\/p>\n Just ingest it<\/span><\/p>\n Exercise and whey protein are anabolic no matter when ingested. The effect whey protein has on anabolism can be explained through the microscope. A more comfortable approach though is to simply back away from all of the details many of which have yet to be elucidated and focus on a natural discussion of those familiar factors that ultimately influence protein metabolism at the microscopic level. That is the approach we will follow. But since we have the microscope in front of us lets take a quick look.<\/p>\n The regulation of skeletal muscle protein turnover is complex. It involves the interactions of gene transcription (i.e. obtaining the assembly instructions) and the subsequent translational control of protein synthesis (i.e. the assembly of the protein from its constituent parts, amino acids). The primary translation pathway leading to protein synthesis is mTOR (mammalian target of rapamycin). In order to build proteins, translation needs to occur and this is initiated by many factors and signaling molecules which feed into this complex regulator called mTOR.<\/p>\n mTOR is a key regulator of translational control. Nutrient, hormonal, and contractile stimuli primarily converge at this protein making mTOR an important modulator of protein synthesis. So when we back away from the microscope and discuss hormones such as insulin, IGF-1 and growth hormone and factors such as exercise, blood flow and protein ingestion what we should be vaguely aware of is that these hormones and factors are in part converging on mTOR to activate those positive regulators of mTOR and protein synthesis or deactivate those negative regulators (or inhibitors) of mTOR and subsequent protein synthesis.<\/p>\n There is no need to examine the specifics and so the following image is meant to convey a very general understanding of the complexity inside the cell.<\/p>\n A recent study in humans using muscle biopsies, tissue processing, western immunoblot analysis and maybe a microscope as well concluded that resistance exercise rapidly increases mTOR signaling, and whey protein increases and prolongs the mTOR signaling response to exercise and training 12<\/sup>.<\/p>\n Simply stated whey protein following exercise increases net protein synthesis which leads to anabolism. If you have a microscope you can add \u201cthrough mTOR\u201d.<\/p>\n 1 \u2013 Heine, Willi E.<\/em>, The Importance of alpha-Lactalbumin in Infant Nutrition<\/strong>, J. Nutr. 121: 277-283, 1991<\/span> A complete protein such as SynthePURE\u2122 provides the raw materials (amino acids) for protein synthesis. We understand that anabolism only occurs when protein synthesis exceeds protein degradation\/breakdown. Exercise creates an environment where anabolism is possible if protein is supplied. In that environment protein synthesis will exceed protein breakdown resulting in net tissue accrual.<\/p>\n However ultimate body transformation requires maximum anabolism. This is primarily achieved through the complementary interplay of those hormones that affect the components of protein metabolism. By understanding precisely how each hormone or factor affects the components responsible for the outcome of protein metabolism one can better achieve an anabolic response.<\/p>\n The primary components responsible for determining the outcome of protein metabolism are:<\/p>\n These components will be discussed in relation to the hormones and factors that manipulate them. We will examine the science behind these hormones so that by the end of this section we will understand for instance exactly how insulin and growth hormone relate to one another and how only as an ensemble are they truly anabolic.<\/p>\n The hormones and factors we will examine are:<\/p>\n For each paragraph the relevant science and studies will be briefly discussed and then summarized in bracketed bold<\/span><\/span>. At the end of the section I will provide a handy table indicating in which direction each hormone affects each of the components of protein metabolism.<\/p>\n There is indirect evidence that post-meal hyperinsulinemia [excess levels of circulating insulin] induces protein anabolism, other than through the suppression of whole-body proteolysis [i.e. protein breakdown\/ catabolism], by facilitating the incorporation of dietary amino acids into new proteins. In fact, when post-meal hyperinsulinemia and hyperaminoacidemia [high insulin & high amino acids] are reproduced in normal subjects by a combined intravenous infusion of insulin and amino acids, the estimates of whole-body protein synthesis increase more than after amino acids alone 20<\/sup>.<\/p>\n [Insulin + Amino Acids = greater increase in entire body protein synthesis]<\/span><\/span><\/p>\n The stimulatory effect of hyperinsulinemia on whole-body protein synthesis cannot be demonstrated when insulin alone is infused 20-25<\/sup>. In this case, by reducing the rate of protein breakdown, hyperinsulinemia decreased the intracellular concentrations of most amino acids 26<\/sup>, limiting their utilization for protein synthesis 27<\/sup>.<\/p>\n [In other words the store of amino acids (often called the intracellular amino acid pool) is replenished in two ways: one by eating\/ingestion of protein & the other by the breakdown of protein in muscle (i.e. protein degradation). This latter, protein degradation reduces protein to its constituent parts (amino acids) which will be transported outside the cell & either be further removed or remain in the amino acid pool (which resides between muscle cells) and is available for reuse in muscle for the next round of transport into muscle & new protein synthesis. Insulin reduces protein breakdown so the amino acid pools are not replenished.]<\/span><\/span><\/p>\n Branched-chain amino acids (Leucine, Isoleucine, Valine) are particularly sensitive to hyperinsulinemia 28<\/sup> and it has been shown the insulin-induced suppression of plasma isoleucine concentration 29<\/sup>, i.e. of a single essential amino acid, is sufficient to decrease whole body protein synthesis.<\/p>\n [So in essence protein synthesis requires all the essential amino acids. If one is missing no protein synthesis will occur.]<\/span><\/span><\/p>\n The results of several studies demonstrate that the overall effect of insulin on the rate of change in whole-body proteins comes from the combined results of the differential effects of the hormone on the rates of protein breakdown and synthesis of individual proteins. For instance, despite the rate of whole-body proteolysis [breakdown] being decreased by insulin 20-25<\/sup>, the rate of muscle protein proteolysis is not affected by local hyperinsulinemia 30<\/sup>. Such a differential effect can be explained by the fact that insulin decreases the proteolytic activity of lysosomes [which are a degradation pathway acting throughout the body] but does not control the ubiquitin system [which is active in muscle breakdown] 31<\/sup> that is responsible for the bulk of muscle proteolysis 31<\/sup>.<\/p>\n [So insulin decreases protein breakdown\/degradation throughout the entire body but does not inhibit protein breakdown specifically in muscle.]<\/span><\/span><\/p>\n Insulin increases the amount of protein deposited in muscle by directly increasing the rate of protein synthesis (40-60% as measured by lysine & phenylalanine disappearance from intracellular pools). For the most part (two exceptions) Insulin does not increase (or regulate) transmember amino acid transport. Therefore transportation of amino acids is not a primary mediator of insulin anabolic actions in muscle 40<\/sup>.<\/p>\n [So Insulin\u2019s primary modes of action are reduction of whole-body protein breakdown as discussed already & in muscle an increase in the rate of protein synthesis. Insulin draws on the intracellular pool of amino acids to affect this increased synthesis. It is possible to run out of amino acids from that pool. Insulin can suck the reservoir dry so to speak. In addition insulin in general (there is an exception) does not increase the rate of transportation of amino acids across the cell membrane into the cell. That remains normal. But the benefit of insulin in muscle is that it increases protein synthesis. However other things are needed besides insulin to affect overall anabolism.]<\/span><\/span><\/p>\n Insulin draws on an existing intracellular pool of amino acids. When amino acid concentrations are maintained at levels higher than normal during systemic insulin administration insulin increased muscle protein synthesis 40<\/sup>.<\/p>\n [So anabolism occurs when both insulin increased protein synthesis occurs and amino acid levels are maintained higher then normal. The primary way to effect this is to increase amino acid\/protein ingestion.]<\/span><\/span><\/p>\n Insulin does not significantly modify protein breakdown in muscle. It has been shown that, during adequate amino acid supply, the most important degradative system in muscle is an ATP-independent system that requires the presence of a specialized protein, termed ubiquitin. This system is not sensitive to insulin. Concerning protein breakdown insulin apparently plays a role only in the regulation of the lysosome activity. These intracellular organelles are not involved in the myofibrillar protein degradation in normal conditions, but only in the presence of low insulin levels or decreased amino acid availability) 31<\/sup> .<\/p>\n [So again insulin will increase protein synthesis in muscle but will not inhibit protein breakdown. So in general anabolism will occur if more protein synthesis then protein breakdown occurs.]<\/span><\/span><\/p>\n Following protein degradation, the amino acids from the degradation event are either transported outward (or in the case of leucine oxidized) or are redirected back into protein synthesis. Phenylalanine & leucine have been shown to be redirected back into protein synthesis while lysine may not 30<\/sup> .<\/p>\n Insulin induces hyperpolarization in the skeletal muscle cells by directly activating the sodium ion (Na+) and potassium ion (K+) -ATPase pump. Those amino acids which are strongly \u201cattracted\u201d to the electrochemical characteristics of the cell membrane are more readily taken up into muscle from the intracellular pool of amino acids. Alanine & lysine are two amino acids that have this attraction and are more readily drawn into muscle by insulin 30<\/sup> .<\/p>\n [When protein in muscle is broken down and its constituents removed back to the amino acid pool, those amino acids may be removed from muscle pools entirely, may be reused for new synthesis or for some amino acids oxidized or used for energy. It would not benefit anabolism to lose the important amino acid leucine to oxidation. Insulin which in general doesn\u2019t increase transport of amino acids from the pool into cells, does so for a few amino acids which use NA+ & K+ channels, namely alanine & lysine.]<\/span><\/span><\/p>\n The branched-chain amino acids (leucine, valine, and isoleucine) and the aromatic (phenylalanine and tyrosine) are preferably transported through system L . This sodium-independent system is unable to generate high transmembrane gradients for its substrates. It has been shown that the kinetic characteristics of system L are not influenced by insulin 30<\/sup>.<\/p>\n [So insulin which has no effect on this mode of transport does not increase the uptake of some very important amino acids.]<\/span><\/span><\/p>\n Blood flow has been found to increase local amino acid delivery to muscle and secondarily increase amino acid transport. This effect may be responsible for increase in leucine uptake.<\/p>\n [This is an extremely important way in which amino acids are drawn to muscle and into cells. This important amino acid leucine has been shown to make its way into cells via increase in blood flow.]<\/span><\/span><\/p>\n Alanine synthesis (which is a function of pyruvate) also increases in the presence of insulin because insulin increases glucose uptake & intracellular pyruvate in muscle 30<\/sup> .<\/p>\n [Certain amino acids can be synthesized from the breakdown of other amino acids. Alanine is one of them. Alanine is often used for energy and so protein synthesis rate or anabolism may depend on the availability of alanine not yet oxidized. The fact that insulin increases alanine synthesis is a desirable effect.]<\/span><\/span><\/p>\n The anabolic effect of insulin on muscle may have become self-limited because of an intracellular depletion of precursor amino acids for protein synthesis, unless amino acid transport is independently stimulated by other factors, i.e., amino acid administration 30<\/sup> .<\/p>\n [Again an external source of amino acids is needed to make insulin anabolic in muscle.]<\/span><\/span><\/p>\n 20 \u2013 Castellino P, Luzi L, Simonson DC. Haymond M. DeFronzo RA.<\/em> Effect of insulin and plasma amino acid concentrations of leucine metabolism in man: role of substrate availability on estimates of whole body protein synthesis.<\/strong> J Clin Invest 1987: 80:1784-9 3<\/span> Growth hormone (GH) promotes protein anabolism with mechanisms different from insulin. It does not affect the rates of whole-body proteolysis [breakdown] but decreases those of amino acid oxidation 41,42<\/sup> The sparing effect on amino acid oxidation results in a greater rate of their incorporation into proteins 41,42,47<\/sup>, with a net protein anabolic effect.<\/p>\n [So Growth Hormone decreases amino acid oxidation (or break down for energy). This should have the effect of preserving key amino acids in that very important amino acid pool. This means that muscle protein synthesis or even increased muscle protein synthesis induced by insulin will be prolonged because there will be a larger pool of raw material (aminos) to draw from.]<\/span><\/span><\/p>\n In the Copeland<\/em> study 41<\/sup> the specific effects of GH on protein metabolism were examined in isolation from insulin and IGF-1. Although in reality since GH leads to creation of IGF-1 six or so hours after release or administration it is not possible for a person to experience only those effects specific to GH.<\/p>\n From Copeland<\/em>, \u201cthe most impressive finding of our study is that an acute infusion of growth hormone (GH) is associated with a prompt inhibition in leucine oxidation, a metabolic action independent of other hormonal changes. This observation, in the context of our study design, is of particular importance since previous studies examining the protein anabolic actions of GH may not have controlled for anabolic effects mediated by a secondary increase in insulin secretion. In our study, insulin levels were identical in control and GH treatment groups 41<\/sup>.<\/p>\n [Growth Hormone strongly inhibits the loss of leucine to oxidation leaving it available for protein synthesis.]<\/span><\/span><\/p>\n GH infusion was also associated with an increase in whole body protein synthesis 41<\/sup>. This observation of an acute increase in the rate of whole body protein synthesis supports the findings of Horber and Haymond<\/em> 42<\/sup>, who also observed a stimulation of whole body protein synthesis in normal subjects and corticosteroid-treated subjects given GH chronically.<\/p>\n [Growth Hormone increases whole body protein synthesis.]<\/span><\/span><\/p>\n \u201cOur data also suggest that the acute GH-induced increase in whole body protein synthesis occurs primarily in nonskeletal muscle tissues, as indicated by the directional changes in leucine and phenylalanine disappearance rates across the leg. GH treatment resulted in an hourly net accretion of 32 mg whole body protein but an hourly loss of 77 mg skeletal muscle protein (relative to baseline values). Assuming continued unperturbed biological action of GH (including confounding effects by IGF-I or insulin), this would translate to an average loss of 1.8 g skeletal muscle protein each day. It is well known, however, that GH treatment invariably is followed some 6-8 h later by a significant increase in blood IGF-I which may stimulate skeletal muscle protein anabolism.\u201d 41<\/sup><\/p>\n \u201cBy contrast Fryburg et al<\/em> 43<\/sup> demonstrated that GH infused directly into the brachial artery stimulates protein synthesis. This increase in muscle protein synthesis occurred only after a longer exposure to GH than the current study. In addition, in that study an increase in blood flow was observed, whereas in our study the systemic administration of GH was not associated with an increase in blood flow in the leg. Recently, these same investigators reported data on regional effects after a systemic infusion of GH, using a design similar to ours but without a concomitant infusion of somatostatin 44<\/sup>. They observed acute increases in forearm blood flow and amino acid uptake across the arm after GH, without evidence of increased protein synthesis in the whole body. However, increases in both insulin and IGFI concentrations were induced by the GH infusion, which may account for some of the differences observed between their studies and ours 44<\/sup>.\u201d<\/p>\n The authors explained the likely reason for the discrepancy by noting that the period of GH administration was too short to stimulate local productions of IGF-I in muscle, which may have caused an increased rate of muscle protein synthesis. Recent studies, however, have not shown any stimulation of muscle protein synthesis by IGF-I in humans 45,46<\/sup>.<\/p>\n [GH by itself in the short-term does not increase muscle protein synthesis. There is evidence that it may do so when its longer-term effect on paracrine IGF-1 is taken into account. <\/span><\/span><\/p>\n GH leads to two types of IGF-1 creation: endocrine IGF-1 which is created in the liver and circulates systemically and is easy to measure and the autocrine\/paracrine IGF-1 which is created in muscle cells and is used therein or in neighboring cells. This latter IGF-1 does not travel systemically but rather exerts its effect locally. Although difficult to measure it is this local IGF-1 which is anabolic in part because it may result in increased muscle protein synthesis.<\/span><\/span><\/p>\n It is now established that GH and testosterone increase local IGF-1 expression whereas exogenous IGF-1 suppresses local IGF-1 expression. Therefore it is not surprising that systemic IGF-1 fails in increasing muscle protein synthesis]<\/span><\/span><\/p>\n The Copeland <\/em>authors 1<\/sup> suspected \u201cthat the increase in muscle mass observed in GH-treated adults 48-51<\/sup> represents a chronic effect on inhibited proteolysis, mediated by IGF-I.<\/p>\n [So IGF-1 inhibits protein breakdown and GH leads to the creation of IGF-1]<\/span><\/span><\/p>\n Growth Hormone infusion in traumatized patients accelerates the rates of transmembrane transport of the essential amino acids leucine and phenylalanine 52<\/sup>. The GH-mediated increased ability of transmembrane systems to transport essential amino acids in vivo confirms previous observations in vitro 53,54<\/sup>.<\/p>\n [So while insulin increases transport of a few aminos (alanine & lysine), GH increases amino acid transport for leucine and phenylalanine. This would mean that GH would increase transport of the other aromatic amino acid tyrosine and the other branch-chain amino acids valine and isoleucine]<\/span><\/span><\/p>\n Besides stimulating whole body protein synthesis, growth hormone suppresses the rate of catabolism of the branched-chain amino acids leucine, isoleucine, and valine 52<\/sup>. This effect has been reported by several other authors using isotopic tracers of leucine at the whole body level 44,55<\/sup>.<\/p>\n [So growth hormone unlike insulin suppresses the breakdown and loss of branch-chain amino acids & probably all amino acids. Thus GH provides more raw materials for insulin-induced higher rate of protein synthesis.]<\/span><\/span><\/p>\n Glutamine and alanine constitute the major carriers of nitrogen among body tissues 56<\/sup>.In skeletal muscle, these amino acids are constantly being synthesized and released into the bloodstream 52<\/sup>. In severe trauma, alanine release from muscle is greatly accelerated, whereas glutamine release was found to be increased or unchanged 57<\/sup>. The results in the Biolo<\/em> study 52<\/sup> indicate that GH administration selectively decreases the rates of synthesis and release of glutamine, whereas alanine synthesis is unchanged during the hormone administration.<\/p>\n [Growth hormone has a negative effect on glutamine synthesis.]<\/span><\/span><\/p>\n In the Biolo<\/em> study 52<\/sup> in their patients, whole body skeletal muscle released 19 g of glutamine per day into the bloodstream before GH administration. After GH administration, glutamine release from skeletal muscle decreased by 50%, whereas at the whole body level, glutamine clearance tended to decrease by 15%.<\/p>\n [So glutamine which is very important to the immune system & is urgently needed in times or severe trauma is not really made available. This in part may be the reason why death occurs in critically ill patients given GH.]<\/span><\/span><\/p>\n\u201cThe metabolic basis for skeletal muscle growth lies in the relationship of muscle protein synthesis to muscle protein breakdown. Muscle hypertrophy occurs only from net protein synthesis; that is, when muscle protein synthesis exceeds breakdown\u2026.resistance exercise, has a profound effect on muscle protein metabolism, often resulting in muscle growth. Acutely, resistance exercise may result in improved muscle protein balance, but, in the absence of food intake, the balance remains negative (i.e., catabolic). \u2026Amino acid availability is critical to the control of muscle protein metabolism. Thus, a meal or a supplement containing protein or amino acids will influence muscle protein. \u2026[and if] ingested after exercise should result in muscle anabolism.\u201d<\/span> \u2013 Kevin Tipton 6<\/sup><\/h4>\n
![\"Meal](\"https:\/\/i0.wp.com\/www.synthetek.com\/Images\/SynthePUREarticle\/1.jpg?resize=570%2C304&ssl=1\")
<\/p>\n![\"Exercise](\"https:\/\/i0.wp.com\/www.synthetek.com\/Images\/SynthePUREarticle\/2.jpg?resize=570%2C317&ssl=1\")
<\/p>\n\n
![\"mTOR](\"https:\/\/i0.wp.com\/www.synthetek.com\/Images\/SynthePUREarticle\/3.jpg?resize=570%2C541&ssl=1\")
<\/p>\nReferences:<\/h3>\n
\n2 \u2013 Cug, J. L. & Friedman, M. (1989)<\/em>, Effect of heat on tryptophan in food: chemistry, toxicology, and nutritional consequences<\/strong> Absorption and Utilization of Amino Acids, (Friedman, M., ed.), vol. 3, pp. 103-115, CRC Press, Boca Raton, FL<\/span>
\n3 \u2013 Nielsen, H. K., Finot, P. A & Hurrell, R. F. (1985)<\/em>, Reactions of proteins with oxidizing lipids: 2. Influence on protein quality and on the bioavailability of lysine, methionine, cyst(e)ine and tryptophan as measured in rat assays<\/strong>, Br. J. Nutr. 53: 75-86<\/span>
\n4 \u2013 Hartman JW, Tang JE, Wilkinson SB, Tarnopolsky MA, Lawrence RL, Fullerton AV, Phillips SM<\/em>, Consumption of fat-free fluid milk after resistance exercise promotes greater lean mass accretion than does consumption of soy or carbohydrate in young, novice, male weightlifters<\/strong>, Am J Clin Nutr 86: 373\u00e2\u20ac\u201c381, 2007<\/span>
\n5 \u2013 Wilkinson SB, Tarnopolsky MA, Macdonald MJ, MacDonald JR, Armstrong D, Phillips SM<\/em>, Consumption of fluid skim milk promotes greater muscle protein accretion after resistance exercise than does consumption of an isonitrogenous and isoenergetic soy-protein beverage<\/strong>, Am J Clin Nutr 85: 1031\u00e2\u20ac\u201c1040, 2007<\/span>
\n6 \u2013 Tipton, Kevin, et al.<\/em>, Ingestion of Casein and Whey Proteins Result in Muscle Anabolism after Resistance Exercise<\/strong>, Med Sci Sports Exerc. 2004 Dec;36(12):2073-81<\/span>
\n7 \u2013 Rigaud, D.<\/em>, Effect of psyllium on gastric emptying, hunger feeling and food intake in normal volunteers: a double blind study<\/strong>, European Journal of Clinical Nutrition (1998) 52, 239-245<\/span>
\n8 \u2013 Holt S, Heading RC<\/em>, Cater DC, Prescott LF & Tothill P (1979): Effect of gel fibre on gastric emptying and absorption of glucose and paracetamol<\/strong>, Lancet 1, 636-639<\/span>
\n9 \u2013 Blackburn NA, Redfern JS, Jarjis HA, Holgate AM<\/em>, Hanning I & Scarpello JH (1984): The mechanism of action of guar gum in improving glucose tolerance in man<\/strong>, Clin. Sci. 66, 329-36<\/span>
\n10 \u2013 Ralphs DNL & Lawaetz NJG (1978)<\/em>: Effect of a dietary fibre on gastric emptying in dumpers<\/strong>, Gut 19, A 986-987<\/span>
\n11 \u2013 Schwartz SE, Levine RA, Singh A, Scheidecker JR & Track NS (1982)<\/em>: Sustained pectin ingestion delays gastric emptying<\/strong>, Gastroentero. 83, 812-817<\/span>
\n12 \u2013 Hulmi, J. J.<\/em>, Resistance exercise with whey protein ingestion affects mTOR signaling pathway and myostatin in men<\/strong>, Appl Physiol 106: 1720\u00e2\u20ac\u201c1729, 2009<\/span>
\n<\/span><\/p>\nProtein Metabolism \u2013 How various hormones create anabolism.<\/h1>\n
\n
\n
Insulin<\/h1>\n
References:<\/h3>\n
\n21 \u2013 Fukagawa NK. Minaker KL. Rowe JW. Goodman MN. Matthews DE. Bier DM, et al.<\/em> Insulin-mediated reduction of whole body protein breakdown: dose-response effects on leucine metabo\u00c2\u00ac lism in postabsorptive men.<\/strong> J Clin Invest 1985:76:2306-11<\/span>
\n22 \u2013 Tessari P, Trevisan R, Inchiostro S, Biolo G, Nosadini R, De Kreutzenberg SV, et al.<\/em> Dose-response curves of effects of insulin on leucine kinetics in humans.<\/strong> Am J Physiol 1986;251:E334-42<\/span>
\n23 \u2013 Tessari P. Nosadini R. Trevisan R. De Kreutzenberg SV. Inchiostro S. Duner E. et al.<\/em> Defective suppression by insulin of leucine-carbon appearance and oxidation in type 1, insulin dependent diabets mellitus: evidence for insulin resistance involving glucose amino acid metabolism.<\/strong> J Clin Invest 1986:77:1797-804<\/span>
\n24 \u2013 Luzi L, Castellino P. Simonson DC, Petrides AS, DeFronzo RA.<\/em> Leucine metabolism in IDDM: role of insulin and substrate availability.<\/strong> Diabetes 1990:39:38-48<\/span>
\n25 \u2013 De Feo P. Volpi E, Lucidi P, Cruciani G. Reboldi G. Siepi D, et al.<\/em> Physiological increments in plasma insulin concentrations have selective and different effects on synthesis of hepatic proteins in normal humans.<\/strong> Diabetes 1993:42:995-1002<\/span>
\n26 \u2013 Alvestrand A, DeFronzo RA, Smith D, Wahren J.<\/em> Influence of hyperinsulinaemia on intracellular amino acid levels and amino acid exchange across splanchnic and leg tissues in uraemia.<\/strong> Clin Sci 1988;74:155-63<\/span>
\n27 \u2013 De Feo P. Haymond MW.<\/em> Effect of insulin on protein metabolism in humans: methodological and interpretative questions.<\/strong> Diab Nutr Metab 1991:4:241-9<\/span>
\n28 \u2013 Fukagawa NK. Minaker KL. Young VR. Rowe JW.<\/em> Insulin dosedependent reductions in plasma amino acids in man.<\/strong> Am J Physiol 1986;250:E13-7<\/span>
\n29 \u2013 Lecavalier L, De Feo P. Haymond MW.<\/em> Isolated hypoisoleucinemia impairs whole body but not hepatic protein synthesis in humans.<\/strong> Am J Physiol 1991;261:E578-86<\/span>
\n30 Biolo G, Declan Fleming RY. Wolfe RR.<\/em> Physiologic hyperinsulinemia stimulates protein synthesis and enhances transport of selected amino acids in human skeletal muscle.<\/strong> J Clin Invest 1995:95:811-9<\/span>
\n31 \u2013 Kettlehut IC. Wing SS. Goldberg AL.<\/em> Endocrine regulation of protein breakdown in skeletal muscle.<\/strong> Diab Metab Rev 1988;4:751-72<\/span>
\n40. \u2013 Bennett, W. M., A. A. Connacher, C. M. Scringeour, R. T. Jung, and M. J. Rennie 1990<\/em> Euglycemic hyperinsulinemia augments amino acid uptake by human leg tissues during hyperaminoacidemia<\/strong> Am. J. PhysioL 259:E185-E194<\/span>
\n<\/span><\/p>\nGrowth Hormone<\/h1>\n