Preservation of skeletal muscle mass is of great importance for maintaining both metabolic health and functional capacity. Muscle mass maintenance is regulated by the balance between muscle protein breakdown and synthesis rates. Both muscle protein breakdown and synthesis rates have been shown to be highly responsive to physical activity and food intake. Food intake, and protein ingestion in particular, directly stimulates muscle protein synthesis rates. The postprandial muscle protein synthetic response to feeding is regulated on a number of levels, including dietary protein digestion and amino acid absorption, splanchnic amino acid retention, postprandial insulin release, skeletal muscle tissue perfusion, amino acid uptake by muscle, and intramyocellular signaling. The postprandial muscle protein synthetic response to feeding is blunted in many conditions characterized by skeletal muscle loss, such as aging and muscle disuse. Therefore, it is important to define food characteristics that modulate

Purpose: Erythropoietin (EPO) is a renal cytokine that is primarily involved in hematopoiesis while also playing a role in non-hematopoietic tissues expressing the EPO-receptor (EPOR). The EPOR is present in human skeletal muscle. In mouse skeletal muscle, EPO stimulation can activate the AKT serine/threonine kinase 1 (AKT) signaling pathway, the main positive regulator of muscle protein synthesis. We hypothesized that a single intravenous EPO injection combined with acute resistance exercise would have a synergistic effect on skeletal muscle protein synthesis via activation of the AKT pathway.Methods: Ten young (24.2 ± 0.9 years) and 10 older (66.6 ± 1.1 years) healthy subjects received a primed, constant infusion of [ring-13C6] L-phenylalanine and a single injection of 10,000 IU epoetin-beta or placebo in a double-blind randomized, cross-over design. 2 h after the injection, the subjects completed an acute bout of leg extension resistance exercise to stimulate skeletal muscle protein synthesis

TY - JOUR. T1 - Rapamycin administration in humans blocks the contraction-induced increase in skeletal muscle protein synthesis. AU - Drummond, Micah J.. AU - Fry, Christopher. AU - Glynn, Erin L.. AU - Dreyer, Hans C.. AU - Dhanani, Shaheen. AU - Timmerman, Kyle L.. AU - Volpi, Elena. AU - Rasmussen, Blake. PY - 2009. Y1 - 2009. N2 - Muscle protein synthesis and mTORC1 signalling are concurrently stimulated following muscle contraction in humans. In an effort to determine whether mTORC1 signalling is essential for regulating muscle protein synthesis in humans, we treated subjects with a potent mTORC1 inhibitor (rapamycin) prior to performing a series of high-intensity muscle contractions. Here we show that rapamycin treatment blocks the early (1-2 h) acute contraction-induced increase (∼40%) in human muscle protein synthesis. In addition, several downstream components of the mTORC1 signalling pathway were also blunted or blocked by rapamycin. For instance, S6K1 phosphorylation (Thr421/Ser424) ...

Age-related muscle wasting (sarcopenia) is accompanied by a loss of strength which can compromise the functional abilities of the elderly. Muscle proteins are in a dynamic equilibrium between their respective rates of synthesis and breakdown. It has been suggested that age-related sarcopenia is due to: i) elevated basal-fasted rates of muscle protein breakdown, ii) a reduction in basal muscle protein synthesis (MPS), or iii) a combination of the two factors. However, basal rates of muscle protein synthesis and breakdown are unchanged with advancing healthy age. Instead, it appears that the muscles of the elderly are resistant to normally robust anabolic stimuli such as amino acids and resistance exercise. Ageing muscle is less sensitive to lower doses of amino acids than the young and may require higher quantities of protein to acutely stimulate equivalent muscle protein synthesis above rest and accrue muscle proteins. With regard to dietary protein recommendations, emerging evidence suggests ...

BACKGROUND. Systemic inflammation and muscle wasting are highly prevalent and coexist in patients on maintenance hemodialysis (MHD). We aimed to determine the effects of systemic inflammation on skeletal muscle protein metabolism in MHD patients. METHODS. Whole body and skeletal muscle protein turnover were assessed by stable isotope kinetic studies. We incorporated expressions of E1, E214K, E3αI, E3αII, MuRF-1, and atrogin-1 in skeletal muscle tissue from integrin β1 gene KO CKD mice models. RESULTS. Among 129 patients with mean (± SD) age 47 ± 12 years, 74% were African American, 73% were male, and 22% had diabetes mellitus. Median high-sensitivity C-reactive protein (hs-CRP) concentration was 13 (interquartile range 0.8, 33) mg/l. There were statistically significant associations between hs-CRP and forearm skeletal muscle protein synthesis, degradation, and net forearm skeletal muscle protein balance (P , 0.001 for all). The associations remained statistically significant after ...

BACKGROUND: The progressive loss of skeletal muscle mass with aging is attributed to a disruption in the regulation of skeletal muscle protein turnover. OBJECTIVE: We investigated the effects on whole-body protein balance and mixed-muscle protein synthesis rates of the ingestion of carbohydrate with or without protein and free leucine after simulated activities of daily living. DESIGN: Eight elderly (75 +/- 1 y) and 8 young (20 +/- 1 y) lean men were randomly assigned to 2 crossover experiments in which they consumed either carbohydrate (CHO) or carbohydrate plus protein and free leucine (CHO+Pro+Leu) after performing 30 min of standardized activities of daily living. Primed, continuous infusions with L-[ring-13C6]phenylalanine and L-[ring-2H2]tyrosine were applied, and blood and muscle samples were collected to assess whole-body protein turnover and the protein fractional synthetic rate in the vastus lateralis muscle over a 6-h period. RESULTS: Whole-body phenylalanine and tyrosine flux were ...

An abundant supply of amino acids enhances the metabolic effect of exercise on muscle protein. Am. J. Physiol. 273 (Endocrinol. Metab. 36): El22-E129, 1997. -Six normal untrained men were studied during the intravenous infusion of a balanced amino acid mixture (-0.15 g. kg-l. h-l for 3 h) at rest and after a leg resistance exercise routine to test the influence of exercise on the regulation of muscle protein kinetics by hyperaminoacidemia. Leg muscle protein kinetics and transport of selected amino acids (alanine, phenylalanine, leucine, and lysine) were isotopically determined using a model based on arteriovenous blood samples and muscle biopsy. The intravenous amino acid infusion resulted in comparable increases in arterial amino acid concentrations at rest and after exercise, whereas leg blood flow was 64 +/- 5% greater after exercise than at rest. During hyperaminoacidemia, the increases in amino acid transport above basal were 30-100% greater after exercise than at rest. Increases in muscle ...

We have previously shown that non-specific blockade of the cyclooxygenase (COX) enzymes in skeletal muscle eliminates the normal increase in muscle protein synthesis following resistance exercise. The current study tested the hypothesis that this COX-mediated increase in postexercise muscle protein synthesis is specifically regulated by the COX-2 isoform. Sixteen males (23 ± 1 yr, 177 ± 2 cm, 81.5 ± 3.4 kg) were randomly assigned to one of two groups that received three doses of either a specific COX-2 inhibitor (celecoxib; 200 mg per dose, 600 mg total) or a placebo during the 24 hours following a single bout of resistance exercise with the knee extensors. Skeletal muscle fractional synthesis rate (FSR) was measured at rest and 24 hours postexercise using a primed constant infusion of [2H5]phenylalanine coupled with muscle biopsies of the vastus lateralis. Mixed muscle FSR was increased following exercise to a greater extent (206%, P,0.05) in the COX-2 group (0.052 ± 0.014 %Ih) as compared ...

There were 2 primary goals of this work. The first was to develop a minimally invasive method for measuring integrated rates of skeletal muscle protein synthesis over a period of days to weeks based on a single blood measurement - i.e., without the need for a physical sample of the tissue. Muscle biopsies are not likely to be widely used in the clinical setting, so a blood test of muscle protein synthesis rates that could be monitored over time would be attractive for drug development, as well as clinical management of disorders of muscle, including sarcopenia and cachexia. Because changes in muscle protein synthesis rates have been shown to occur rapidly in response to anabolic therapies and to predict subsequent changes in muscle mass, strength, and performance (5, 8-10), the availability of a blood test for skeletal muscle protein synthesis rates would greatly simplify translational drug development and monitoring of treatment efficacy in this growing, unmet medical need.. We describe here an ...

It is thought that the production of muscle protein after a meal in response to consuming protein and/or amino acids is impaired in the elderly compared to the young. Also, consuming carbohydrates at the same time increases secretion of the hormone insulin and increases muscle protein production in the young. However, it is unclear how the elderly respond to the combined intake of protein and carbohydrates. Likewise, consuming the amino acid leucine may also increase muscle protein production. Adding carbohydrate or leucine to protein may represent effective strategies to overcome the impaired muscle protein production in the elderly. This study consists of three substudies. The aim of the first study is to determine if the response to combined protein and carbohydrate intake is different between young and elderly men. The aim of the second study is to investigate whether consuming carbohydrate as well increases muscle protein production in elderly men. The aim of the third study is to examine ...

Muscle protein breakdown (MPB) is an important metabolic component of muscle remodeling, adaptation to training, and increasing muscle mass. Degradation of muscle proteins occurs via the integration of three main systems-autophagy and the calpain and ubiquitin-proteasome systems. These systems do not operate independently, and the regulation is complex. Complete degradation of a protein requires some combination of the systems. Determination of MPB in humans is technically challenging, leading to a relative dearth of information. Available information on the dynamic response of MPB primarily comes from stable isotopic methods with expression and activity measures providing complementary information. It seems clear that resistance exercise increases MPB, but not as much as the increase in muscle protein synthesis. Both hyperaminoacidemia and hyperinsulinemia inhibit the post-exercise response of MPB. Available data do not allow a comprehensive examination of the mechanisms behind these responses. ...

Victor R. Preedy, James Keating, Timothy J. Peters; Ethanol-Induced Reductions in Skeletal Muscle Protein Synthesis in the Rat in Vivo. Clin Sci (Lond) 1 October 1990; 79 (s23): 7P. doi: https://doi.org/10.1042/cs079007P. Download citation file:. ...

TY - JOUR. T1 - Reduced synthesis of muscle proteins in chronic renal failure. AU - Adey, Deborah. AU - Kumar, Rajiv. AU - McCarthy, James T.. AU - Sreekumaran Nair, K.. PY - 2000/2. Y1 - 2000/2. N2 - Muscle wasting and weakness occur frequently in patients with chronic renal failure. The mechanism(s) by which these abnormalities occur is unclear. We hypothesized that such findings were due to defective muscle protein synthesis. We measured synthetic rates of mixed muscle proteins, myosin heavy chain, and mitochondrial proteins in serial muscle biopsy samples during a continuous infusion of L[1-13C] leucine from 12 patients with chronic renal failure and 10 healthy control subjects under identical study conditions. Patients with chronic renal failure have significantly lower synthetic rates of mixed muscle proteins and myosin heavy chain (27 and 37% reductions, respectively, P , 0.05 and P , 0.02). Significant declines in the synthetic rates of muscle mitochondrial protein (27%) (P , 0.05), ...

The purpose of this investigation was to examine the effects of training either once or three times/day on the principal stages of skeletal muscle. The experiments were carried out on male albino rats fed either 3 or 5 times/day a diet containing 20% protein. Experimental animals swam either once or 3 times/day, 6 days/week for 10 weeks with weights attached. The total duration of daily activity was equal for both groups and at 10 weeks each animal was swimming for 60 min/day with 3% of his body weight attached. All the animals were examined at rest after the 10-week training programs. The adequacy of the weight-loading and training schedules was estimated by body weight dynamics and such energy metabolites as creatine phosphate and glycogen. Skeletal muscle RNA and protein synthesis were studied by means of 14C-orotic acid and 14C-leucine incorporation, respectively. Quadriceps and gastrocnemius muscles were used for analysis in all experiments. It was found that the increase in the number of daily

Optimal muscle protein synthesis requires a pulsatile increase in branch-chain amino acids (particularly leucine) with or without concomitant pulses in insulin levels. Pancreatic substrate clamp studies have demonstrated that insulin and branch-chain amino acids independently increase muscle synthesis with the effects of both being additive [45, 46]. Animal data demonstrates that muscle protein synthesis following a meal is rapid (within 30 min) and sustained for about 2 h but then declines toward baseline in parallel with the postprandial changes in circulating insulin and amino acids [34, 47]. Bohe and colleagues measured the latency and duration of the stimulation of human muscle protein synthesis during a continuous infusion of amino acids [48]. The rate of muscle protein synthesis increased after 30 min and reached a peak at 2 h rapidly returning to basal levels by 4 h despite continuous amino acid availability. In healthy individuals at rest, muscle protein synthesis displays a saturable ...

Insulin action on muscle protein kinetics and amino acid transport during recovery after resistance exercise. Biolo, Gianni; Williams, Bradley D.; Fleming, R.Y. Declan; Wolfe, Robert R. // Diabetes;May99, Vol. 48 Issue 5, p949 Determines the role of insulin on muscle protein kinetics and amino acid transport after heavy resistance exercise. Effect of insulin infusion on plasma insulin and glucose concentrations; Rate of muscle protein synthesis and degradation during hyperinsulinemia at rest and after exercise; Amino... ...

It is well established that consuming protein and/or amino acids is necessary to stimulate post-exercise protein synthesis, thus creating a positive protein balance1-3. In accordance, dietary protein administration with or without carbohydrate ingestion before, during, and/or immediately after exercise has been shown to stimulate net muscle protein accretion during post-exercise recovery which is needed for the accrual of muscle mass.. Most of the research in this area examined the effect of food intake on the muscle protein synthesis response to exercise in an overnight fasted state2,4,5. It is reasonable to assume the limited availability of amino acids prevents a substantial rise in post-exercise muscle protein synthesis rate. This post-absorptive (fasted) condition differs from normal everyday practice in which sport activities are often performed in postprandial (after eating) conditions, such as in the evening. A study evaluated the efficacy of protein ingestion immediately after exercise ...

TY - JOUR. T1 - Preexercise aminoacidemia and muscle protein synthesis after resistance exercise. AU - Burke, Louise M.. AU - Hawley, John A.. AU - Ross, Megan L.. AU - Moore, Daniel R.. AU - Phillips, Stuart M.. AU - Slater, Gary R.. AU - Stellingwerff, Trent. AU - Tipton, Kevin D.. AU - Garnham, Andrew P.. AU - Coffey, Vernon G.. PY - 2012/10. Y1 - 2012/10. N2 - PURPOSE: We have previously shown that the aminoacidemia caused by the consumption of a rapidly digested protein after resistance exercise enhances muscle protein synthesis (MPS) more than the amino acid (AA) profile associated with a slowly digested protein. Here, we investigated whether differential feeding patterns of a whey protein mixture commencing before exercise affect postexercise intracellular signaling and MPS. METHODS: Twelve resistance-trained males performed leg resistance exercise 45 min after commencing each of three volume-matched nutrition protocols: placebo (PLAC, artificially sweetened water), BOLUS (25 g of whey ...

Many protein and amino acid supplements are touted as being able to maximize the gains achieved from resistance exercise by preventing muscle protein catabolism and stimulating anabolism. If effective, such supplements would be useful not only for athletes and for those trying to increase their fat free mass, but also for patients recovering from injuries or burns and for the prevention of aging-associated muscle loss. It has been shown that intravenous infusion or oral administration of complete mixtures of amino acids has a positive effect on muscle protein synthesis and net muscle anabolism following exercise. Since nonessential amino acids are synthesized by the body in response to resistance exercise, administration of essential amino acids only following exercise has the same positive anabolic effect on muscle as complete amino acid supplementation. Furthermore, oral administration of whole proteins following training has a similar anabolic effect, as whole proteins such as whey and casein ...

Abstracts of the Eighth European Conference on Muscle and Motility including the Erwin Riesch Symposium on Muscle Proteins - Polymorphism and Isoforms Heidelberg, 17-20 September ...

Sarcopenia is a well-known phenomenon in elderly individuals and resistance exercise together with sufficient amino acid (AA) availability has proved to be a counteractive implement. However, the source of AA and supplement timing require further investigation. The objective was to compare muscle protein synthesis (MPS) to intakes of whey and caseinate after heavy resistance exercise in healthy elderly individuals, and, furthermore, to compare the timing effect of caseinate intake. Twenty-four elderly men and women (mean ± SEM; 68 ± 1 years) were randomized to one of four groups: caseinate intake before exercise (CasPre), caseinate intake immediately after exercise (CasPost), whey intake immediately after exercise (Whey), or intake of a non-caloric control drink (Control). Muscle myofibrillar and collagen fractional synthesis rates (FSR) were measured by a primed continuous infusion of l-[1-13C]leucine using labeled proteins during a 6-h recovery period. No differences were observed in muscle ...

I think its fair to say that there are very few players who are not actively looking to increase their muscle mass or improve their body composition. Research suggests that additional muscle mass can improve the predicted success in some team sports such as rugby1. Building muscle is a multi-faceted approach and the following 3 tips will help you maximise those gains and improve performance.. Tip #1 - Engage in resistance training. Resistance Training (RT) is the single most important factor in building muscle. During RT muscle fibres are broken down and muscle protein synthesis (MPS) is increased. However, although MPS is increased, supporting nutrition in the form of protein is needed in order to ensure MPS is greater than muscle protein breakdown (MPB) and muscle grows. There is no change in muscle growth after one RT session but instead muscle hypertrophy is due to the accumulation of muscle protein in response to each individual bout of RT training plus protein that occurs ...

If patients could recognise themselves, or anyone else could recognise a patient from your description, please obtain the patients written consent to publication and send them to the editorial office before submitting your response [Patient consent forms] ...

Background & aim: Protein-energy supplementation is routinely employed to combat muscle loss. However, success is often compromised by increased satiety, poor palatability, high costs and low compliance. Methods: For 2-weeks we supplemented meals of older individuals with leucine (4 g/meal; 3 meals/day; days 2-14). Metabolic studies were performed prior to (Day 1) and following (Day 15) supplementation. Leucine was not provided on metabolic study days. Venous blood and vastus lateralis muscle biopsies were obtained during a primed constant infusion of L-[ring-C-13(6)] phenylalanine. Mixed muscle fractional synthesis rate (FSR), body composition and markers of nutrient signaling (mTOR, 4E-BP1 and p70S6K1 phosphorylation) were measured before and after a low protein/carbohydrate simulated meal. Results: The meal modestly increased FR on Day 1 (postabsorptive: 0.063 +/- 0.004 vs. postprandial: 0.075 +/- 0.006%/h; p = 0.03), however, two weeks of leucine supplementation increased postabsorptive FSR (p = 0

Dietary protein ingestion after exercise stimulates muscle protein synthesis, inhibits protein breakdown and, as such, stimulates net muscle protein accretion following resistance as well as endurance type exercise. Protein ingestion during and/or immediately after exercise has been suggested to fac …

Purpose: We have previously shown that the aminoacidemia caused by the consumption of a rapidly digested protein after resistance exercise enhances muscle protein synthesis (MPS) more than the amino acid (AA) profile associated with a slowly digested protein. Here, we investigated whether differential feeding patterns of a whey protein mixture commencing before exercise affect postexercise intracellular signaling and MPS. Methods: Twelve resistance-trained males performed leg resistance exercise 45 min after commencing each of three volume-matched nutrition protocols: placebo (PLAC, artificially sweetened water), BOLUS (25 g of whey protein + 5 g of leucine dissolved in artificially sweetened water; 1× 500 mL), or PULSE (15× 33-mL aliquots of BOLUS drink every 15 min). Results: The preexercise rise in plasma AA concentration with PULSE was attenuated compared with BOLUS (P less than 0.05); this effect was reversed after exercise, with two-fold greater leucine concentrations in PULSE compared ...

LEUCINE IS THE TRIGGER!!!. New scientific studies show that Leucine is a powerful nutritional activator of muscle protein synthesis*. It activates the anabolic pathway for building muscle.. These new findings confirm that within the context of a mixed macronutrient intake, suboptimal protein doses can be made more effective in stimulating myofibrillar protein synthesis, through the addition of a high proportion of free Leucine.. This branched chained amino acid is essential for achieving a positive nitrogen balance in building lean muscle mass. Leucine is discribed as the trigger of muscle protein synthesis.. * Muscle protein synthesis (MPS) is the rebuilding of muscle tissue and it occurs as a result of the stresses that we place on our body, whether it is to repair injury (such as a muscle tear) or because we intentionally try to damage it (microtrauma from training).. ...

It turns out that only slight elevations of insulin above basal levels are all thats required to blunt muscle catabolic effects. Just consuming protein alone is enough to elicit a release of insulin that is sufficient to interact with the ingested amino acids in promoting muscle protein synthesis. Leucine alone is known to promote the release of insulin. This explains the recent studies showing that protein alone is enough to boost muscle protein synthesis following training. Indeed, one study showed that boosting insulin levels 30-times above fasting level did not further boost muscle protein synthesis if blood levels of amino acids were high. Just consuming protein alone, especially whey, which is rich in leucine, is enough to boost insulin levels 2-3-fold above resting levels. This level of insulin alone is enough to provide the anti-catabolic effects of insulin following exercise. Other studies show that adding 30 or 90 grams of carbs to 20 grams of protein does not boost muscle protein ...

Save 32% CytoSport - Muscle Milk Banana Creme 2.47 Pounds Muscle Milk Protein Powder Everyday Performance 310 Calories Per 2 Scoops 32g Protein Per 2 Scoops 20 Vitamins & Minerals Free of Banned Substances Gluten Free The Power of Protein Protein you eat breaks down into amino acids in the body, which support muscle growth, repair and maintenance Consuming both fast and slow release proteins, like those found in Muscle Milk Protein Powder, keeps your body in positive protein balance Protein after exercise aids in recovery and helps build lean muscle 32 Grams of Protein --Build lean muscles --Recover after exercise 20 Vitamins & Minerals --Antioxidant vitamins A, C and E --Vitamin D, Calcium, Magnesium and Phosphorus for strong bones BCAA (Branched Chain Amino Acids) --Leucine, Isoleucine, Valine help support muscle maintenance and growth --Leucine triggers muscle protein growth and helps prevent muscle protein breakdown. Protein Comparisons 2 Scoops of Muscle Milk = 4 Jumbo Eggs 2 Scoops of Muscle Milk

Save 32% CytoSport - Muscle Milk Cake Batter 2.47 Pounds Muscle Milk Protein Powder Everyday Performance 310 Calories Per 2 Scoops 32g Protein Per 2 Scoops 20 Vitamins & Minerals Free of Banned Substances Gluten Free The Power of Protein Protein you eat breaks down into amino acids in the body, which support muscle growth, repair and maintenance Consuming both fast and slow release proteins, like those found in Muscle Milk Protein Powder, keeps your body in positive protein balance Protein after exercise aids in recovery and helps build lean muscle 32 Grams of Protein --Build lean muscles --Recover after exercise 20 Vitamins & Minerals --Antioxidant vitamins A, C and E --Vitamin D, Calcium, Magnesium and Phosphorus for strong bones BCAA (Branched Chain Amino Acids --Leucine, Isoleucine, Valine help support muscle maintenance and growth --Leucine triggers muscle protein growth and helps prevent muscle protein breakdown. Protein Comparisons 2 Scoops of Muscle Milk = 4 Jumbo Eggs 2 Scoops of Muscle Milk =

Muscle protein synthesis is stimulated by resistance training and protein intake. Muscle growth is the outcome of effective MPS response in our body.

Biolo, G., K. Tipton, S. Klein, and R. Wolfe (1997). An abundant supply of amino acids enhances the metabolic effect of exercise on muscle protein. Am. J. Physiol. 273:E122-E129. Boirie, Y., M. Dangin, P. Gachon, M. Vasson, J. Maubois, and B. Beaufrère (1997). Slow and fast dietary proteins differently modulate postprandial protein accretion. Proc. Natl. Acad. Sci. USA. 94:14930-14935. Burd, N., S. Gorissen, and L. van Loon (2013). Anabolic resistance of muscle protein synthesis with aging. Exerc. Sport Sci. Rev. 41:169-173. Burd, N., D. West, D. Moore, P. Atherton, A. Staples, T. Prior, J. Tang, M. Rennie, S. Baker, and S. Phillips (2011). Enhanced amino acid sensitivity of myofibrillar protein synthesis persists for up to 24 h after resistance exercise in young men. J. Nutr. 141:568-573. Churchward-Venne, T., A. Holwerda, S. Phillips, and L. van Loon (2016). What is the optimal amount of protein to support post-exercise skeletal muscle reconditioning in the older adult? Sports Med. E-pub ...

Autor: Schraders, M. et al.; Genre: Zeitschriftenartikel; Im Druck veröffentlicht: 2011; Keywords: Adolescent; Adult; Child; Child, Preschool; *Codon, Nonsense; DNA Mutational Analysis; Female; Frameshift Mutation; *Genes, X-Linked; Hearing Loss/*genetics/pathology; Humans; Insulin-Like Growth Factor I/genetics; Male; Middle Aged; Molecular Sequence Annotation; Muscle Proteins/*genetics; Pedigree; Polymorphism, Single Nucleotide; Sequence Analysis; Young Adult; Titel: Next-generation sequencing identifies mutations of SMPX, which encodes the small muscle protein, X-linked, as a cause of progressive hearing impairment

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Muscle bulk and strength naturally decline with age, as the tissues regenerate more slowly. Without efforts to stay strong and healthy, this can accelerate into sarcopenia, a prevalent, muscle wasting condition with multiple dire health outcomes.. Poor wound healing, increased risk of falls, hospitalisation, loss of independence and mortality are just some of the ripple effects caused by declining muscle mass.. Its well known that protein is important for helping to maintain muscle mass, with evidence that older adults benefit from 1g protein per kilogram of body weight per day - which is higher than current recommendations of 0.8g/kg body weight.. Some researchers say the focus should be on consuming 25-30g protein per meal for optimum muscle protein synthesis.. In older adults, however, muscle protein synthesis is less efficient if protein and carbohydrates are eaten together. The researchers suggest this could be improved by supplementing mixed-nutrient meals with leucine.. The importance of ...

Resistance coaching and subsequent intake of a protein-rich food encourages muscle mass hypertrophy and gains in muscle mass toughness by stimulating myofibrillar muscle protein synthesis (MPS) and inhibiting muscle protein breakdown (MPB).[108][109] The stimulation of muscle mass protein synthesis by resistance education happens by means of phosphorylation in the mechanistic target of rapamycin (mTOR) and subsequent activation of mTORC1, which ends up in protein biosynthesis while in the ribosome by means of phosphorylation of mTORC1s speedy targets (the p70S6 kinase and the translation repressor protein 4EBP1 ...

Resistance schooling and subsequent usage of the protein-loaded meal promotes muscle mass hypertrophy and gains in muscle mass power by stimulating myofibrillar muscle mass protein synthesis (MPS) and inhibiting muscle protein breakdown (MPB).[108][109] The stimulation of muscle protein synthesis by resistance schooling takes place through phosphorylation in the mechanistic concentrate on of rapamycin (mTOR) and subsequent activation of mTORC1, which results in protein biosynthesis within the ribosome by means of phosphorylation of mTORC1s quick targets (the p70S6 kinase and the translation repressor protein 4EBP1 ...

Bioactive peptides have been identified in a range of foods, including plant, milk and muscle, e.g., beef, chicken, pork and fish muscle proteins. Bioactive peptides from food proteins offer major potential for incorporation into functional foods and nutraceuticals. The aim of this paper is to present an outline of the bioactive peptides identified in the muscle protein of meat to date, with a focus on muscle protein from domestic animals and fish. The majority of research on bioactives from meat sources has focused on angiotensin-1-converting enzyme (ACE) inhibitory and antioxidant peptides.

Bioactive peptides have been identified in a range of foods, including plant, milk and muscle, e.g., beef, chicken, pork and fish muscle proteins. Bioactive peptides from food proteins offer major potential for incorporation into functional foods and nutraceuticals. The aim of this paper is to present an outline of the bioactive peptides identified in the muscle protein of meat to date, with a focus on muscle protein from domestic animals and fish. The majority of research on bioactives from meat sources has focused on angiotensin-1-converting enzyme (ACE) inhibitory and antioxidant peptides.

Sarcopenia seems to be attributed to a blunted muscle protein synthetic response to food intake and exercise. This blunted response could be the result of impaired protein digestion and absorption kinetics and lead to lower postprandial plasma amino acid availability.

Protein supplements for building muscle Protein Supplements for Building Muscle Review Report Card: Beyond The Basics! By The Muscle Nerd,…. Read More » ...

There is no getting around it, we are a society that loves to find shortcuts to getting things done and now thanks scientists in Australia we may be able to promote muscle gain with out the pain of going to a gym.. Called Grb10 this newly discovered muscle protein seems to play a very big role in promoting muscle growth without you having to change your diet or activity and it appears to not have any adverse health effects.. The research which is being published in The FASEB Journal this week is still in its earliest stages but scientists say that the experiments with rats have shown some pretty encouraging results.. ...

Increase muscle area and strength, and improve nutritional markers of. A placebo or a dose of human growth hormone (hgh) four times the. 2003 · цитируется: 103 - exercise exerts a significant influence on protein metabolism (9). Whole body and muscle protein breakdown increase during exercise, whereas oxidation of. Many believe in the value of using igf to promote muscle building. 1997 - as anabolic steroids, growth hormone, insulin-like growth factor, and insulin. Articles advise athletes about dosage, side-effects, avoiding detection,. Stimulating lean muscle growth reduces age-related tissue loss. 2019 · цитируется: 2 - in fit people, gh in doses used in ethically-supervised studies does not affect muscle strength or aerobic capacity but improves anaerobic capacity. Doses occur several times per week or on a daily basis depending on how. Com forum - member profile , profil strona. Użytkownik: hygetropin dosage for bodybuilding, hgh dosage for fat loss,. Hgh helps repair ...

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Actual physical performance will depend on numerous muscle mass functions, including toughness. Muscle mass protein synthesis and breakdown are central in determining the two power and General operate. Even so, most research in the area of muscle operate and physical exercise has focused on energy metabolism in lieu of the regulation of muscle mass protein metabolism. Essential thoughts continue to be unanswered regarding the mechanisms governing the response of muscle protein synthesis and breakdown to training, and the result of exercising on protein specifications in individuals continues to be controversial. Methodologic troubles have confined the exploration of these along with other troubles about muscle mass protein kinetics due to best whey protein at amazing prices problem of quantifying muscle mass protein synthesis and breakdown in people. In lieu of direct measurement of protein kinetics, the result of protein ingestion on effectiveness variables including energy continues to be ...

Synthetic response of stimulated respiratory epithelium: modulation by prednisolone and iKK2 inhibition.: The airway epithelium plays a central role in wound re

So, it would make sense that eating barbaric amounts of protein will lead to colossal gains, right? Well, not really. Countless studies have shown that the law of diminishing returns applies to protein intake and muscle building. Researchers at the University of Stirling have discovered that muscle protein synthesis is maximally stimulated when 20 - 40g of a highly bioavailable protein source such as whey or meat is consumed after training (this range is dependent on the amount of lean body mass that is stimulated by resistance exercise). The remainder of the protein consumed was either used in non-muscle tissue protein synthesis or processed by the liver to make glucose or fatty acids - not to generate more skeletal muscle. Research has confirmed that to build muscle mass, a minimum of 1.6g/kg/d is required in healthy non-dieting adults. Protein intake above this, may be used for different purposes.. ...

1. Quadriceps muscle protein turnover was assessed in the post-absorptive state in six men immediately after the end of unilateral leg immobilization (37 ± 4 days) in a plaster cast after tibial fracture. A primed-constant intravenous infusion of l-[1-13C]leucine was administered over 7 h. Quadriceps needle biopsies, taken bilaterally at the end of the infusion, were analysed for muscle protein leucine enrichment with 13C.. 2. Quadriceps muscle protein synthetic rate, calculated from the fractional incorporation of [13C]leucine into protein compared with the average enrichment of blood α-ketoisocaproate, was 0.046 ±0.012%/h in the uninjured leg, but was only 0.034 ±0.007%/h in the quadriceps of the previously fractured leg (P , 0.05, means ± sd).. 3. Muscle RNA activity (i.e. protein synthetic rate per RNA) fell from 0.27 ±0.08 μg of protein synthesized h−1 μg−1 of RNA in the control leg to 0.14 ±0.03 μg of protein synthesized h−1 μg−1 of RNA in the immobilized leg (P , ...

TY - JOUR. T1 - Growth hormone and insulin reverse net whole body and skeletal muscle protein catabolism in cancer patients. AU - Wolf, R. F.. AU - Pearlstone, D. B.. AU - Newman, E.. AU - Heslin, M. J.. AU - Gonenne, A.. AU - Burt, M. E.. AU - Brennan, M. F.. AU - Herndon, D. N.. AU - Wilmore, D. W.. AU - Lowry, S.. AU - Blakemore, W. S.. N1 - Copyright: Copyright 2017 Elsevier B.V., All rights reserved.. PY - 1992. Y1 - 1992. N2 - The authors examined the effect of recombinant-human growth hormone (r- hGH) and insulin (INS) administration on protein kinetics in cancer patients. Twenty-eight cancer patients either received r-hGH for 3 days (GH group, n = 12, weight loss = 6 ± 2%) or were not treated (control [CTL] group, n = 16, weight loss = 11 ± 2%) before metabolic study. Recombinant-human growth hormone dose was 0.1 mg/kg/day (n = 6) or 0.2 mg/kg/day (n = 6). Patients then underwent measurement of baseline protein kinetics (GH/B, CTL/B) followed by a 2-hour euglycemic insulin infusion (1 ...

Strenuous exercise following overnight fasting increases fat oxidation during exercise, which can modulate training adaptation. However, such exercise induces muscle protein catabolism by decreasing blood insulin concentrations and increasing amino acid oxidation during the exercise. Leucine-enriched essential amino acids (LEAAs) enhance muscle protein synthesis (MPS) at rest and after exercise. However, it remains to be clarified if the co-ingestion of carbohydrate with LEAAs induces an additional increase in MPS, particularly in a hypoinsulinemic state induced by strenuous exercise. Eight-week-old male Sprague-Dawley rats were made to perform strenuous jump exercise (height 35 cm, 200 jumps, 3-s intervals), after which they ingested distilled water and 1 g/kg LEAAs with or without 1 g/kg of glucose. The fractional synthesis rate was determined by measuring the incorporation of l-[ring-2H5]-phenylalanine into skeletal muscle protein. Immediately after the exercise, plasma insulin concentration was

Author: Mller, Rikke S. et al.; Genre: Journal Article; Published in Print: 2008-04-16; Title: Truncation of the Down syndrome candidate gene DYRK1A in two unrelated patients with microcephaly

Due to insufficient exercise training, skeletal mucle loss is beginning form 25 years old. Sarcopenia is the critical reason to effect activities of daily life in seniors. Strength training has been proven to be a great strategy to increase mucle mass and functions. Exercise training provokes skeletal muscle protein synthesis, in the meantime also causes muscle injury, induces muscle protien degradation and muscle cell inflammatory. Net muscle protein balace will become negative in nutrients or rest deficiency. Muscle biogenesis decreasing with aging may induce by signal transmit weakening in muscle protein synthesis pathway. Current studies showed that the phosphatidylinositol 3-kinase /AKT/mammalian target of rapamycin (PI3K/Akt/ mTOR) pathway is an important pathway to regulate skeletal muscle hypertrophy. Therefore, the first year, resveratrol is uesd as a nutriental ergogenic aid which may activate related protein expression of muscle synthesis pathway. In order to understand promotion or ...

Ingestion of sufficient dietary protein is a fundamental prerequisite for muscle protein synthesis and maintenance of muscle mass and function. Elderly people are often at increased risk for protein-energy malnutrition, sarcopenia, and a diminished quality of life. This study sought to compare chang …

Rationale: The giant protein titin plays key roles in myofilament assembly and determines the passive mechanical properties of the sarcomere. The cardiac titin molecule has 2 mayor elastic elements, the N2B and the PEVK region. Both have been suggested to determine the elastic properties of the heart with loss of function data only available for the N2B region.. Objective: The purpose of this study was to investigate the contribution of titins proline-glutamate-valine-lysine (PEVK) region to biomechanics and growth of the heart.. Methods and Results: We removed a portion of the PEVK segment (exons 219 to 225; 282 aa) that corresponds to the PEVK element of N2B titin, the main cardiac titin isoform. Adult homozygous PEVK knockout (KO) mice developed diastolic dysfunction, as determined by pressure-volume loops, echocardiography, isolated heart experiments, and muscle mechanics. Immunoelectron microscopy revealed increased strain of the N2B element, a spring region retained in the PEVK-KO. ...

1. We have used l-[1-13C,15N]leucine as the substrate tracer to study leucine and muscle protein metabolism across the forearm of eight normal fasting adults.. 2. The rates of protein synthesis and breakdown, de- and re-amination of leucine, and the oxidative de-carboxylation of its keto acid were calculated directly from the arteriovenous metabolite balances and isotope dilutions as described by the metabolic model.. 3. The results were compared with those obtained previously when subjects were fed. The effects of fasting on protein and leucine metabolism were a significant decrease in protein synthesis from 127 (sem 11; n = 6) to 70 (sem 6; n = 12) nmol of leucine min−-1 100 ml−-1 of forearm tissue (P , 0.001) and a marked decrease in leucine catabolism in the forearm muscle.. 4. This model has demonstrated that each subject was in negative protein balance across the forearm during fasting while positive during feeding, the mean values being −29(sem 5; n = 12) and + 39(sem 9; n = 6) nmol ...

The peroxisome proliferator-activated receptor γ (PPARγ) agonist rosiglitazone (Rosi) appears to provide protection against organ dysfunction during endotoxaemia. We examined the potential benefits of Rosi on skeletal muscle protein maintenance and carbohydrate metabolism during lipopolysaccharide (LPS)-induced endotoxaemia. Sprague-Dawley rats were fed either standard chow (control) or standard chow containing Rosi (8.5±0.1 mg.kg-1.day-1) for two weeks before and during 24 h continuous intravenous infusion of LPS (15 μg.kg-1.h-1) or saline. Rosi blunted LPS-induced increases in muscle tumor necrosis factor-α (TNF-α) and interleukin-6 (IL-6) mRNA by 70% (P,0.05) and 64% (P,0.01), respectively. Furthermore, Rosi suppressed the LPS-induced reduction in phosphorylated AKT and phosphorylated Forkhead box O (FOXO) 1 protein, as well as the upregulation of muscle RING finger 1 (MuRF1; P,0.01) mRNA, and the LPS-induced increase in 20S proteasome activity (P,0.05). Accordingly, LPS reduced the ...

Leucine supplementation enhances integrative myofibrillar protein synthesis in free-living older men consuming lower- and higher-protein diets: a parallel-group crossover study Academic Article ...

The active and passive contractile performance of skeletal muscle fibers largely depends on the myosin heavy chain (MHC) isoform and the stiffness of the titin spring, respectively. Open questions concern the relationship between titin-based stiffness and active contractile parameters, and titins importance for total passive muscle stiffness. Here, a large set of adult rabbit muscles (n = 37) was studied for titin size diversity, passive mechanical properties, and possible correlations with the fiber/MHC composition. Titin isoform analyses showed sizes between ∼3300 and 3700 kD; 31 muscles contained a single isoform, six muscles coexpressed two isoforms, including the psoas, where individual fibers expressed similar isoform ratios of 30:70 (3.4:3.3 MD). Gel electrophoresis and Western blotting of two other giant muscle proteins, nebulin and obscurin, demonstrated muscle type-dependent size differences of ≤70 kD. Single fiber and single myofibril mechanics performed on a subset of muscles ...

Insulin stimulates muscle protein synthesis when the levels of total amino acids, or at least the essential amino acids, are at or above their postabsorptive concentrations. Among the essential amino acids, branched-chain amino acids (BCAA) have the primarily role in stimulating muscle protein synthesis, and are commonly sought alone to stimulate muscle protein synthesis in humans. Fourteen healthy, young subjects were studied before and after insulin infusion to examine whether insulin stimulates muscle protein synthesis in relation to the availability of BCAA alone. Half of the subjects were studied in the presence of postabsorptive BCAA concentrations (Control), while the other half in the presence of increased plasma BCAA (BCAA). When compared to that prior to the initiation of the insulin infusion, fractional synthesis rate of muscle protein (%/hour) did not change (P , 0 .05) during insulin in either the Control (0.04 ± 0.01 vs 0.05 ± 0.01) or the BCAA (0.05 ± 0.02 vs 0.05 ± 0.01) ...

If youre a serious student of muscle, you may have heard of the mTOR pathway. Well, mTORC1 includes not only mTOR, but also several additional processes that stimulate muscle protein synthesis.. The mTORC1 pathway controls the anabolic and catabolic signaling of skeletal muscle mass, regulating muscle growth and muscle breakdown. And research has shown that supplementing essential amino acids in conjunction with resistance training has an additive effect on stimulating muscle protein synthesis through this pathway compared to just resistance training.. The translation for you: Essential amino acids can help maximize the hard work we put in at the gym to stimulate muscle protein synthesis. If youre stimulating muscle protein synthesis you put yourself in a favorable position to gain muscle or at least not break down your existing muscle.. When Looking to Supplement With EAAs, Check For These Key Features:. All Nine Essential Amino Acids: While conditionally essential and nonessential amino ...

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The use of ambient desorption electrospray ionization (DESI-MS) mass spectrometry and liquid extraction surface analysis mass spectrometry (LESA-MS) is explored for the first time to analyse skeletal muscle proteins obtained from mixture of standard proteins and raw meat. Single proteins and mixtures of up to five proteins (myoglobin, troponin C, actin, BSA, tropomyosin) were deposited onto a polymer surface, followed by in-situ tryptic digestion and comparative analysis using DESI-MS and LESA-MS using tandem electrospray MS. Peptide peaks specific to individual proteins were readily distinguishable with good signal-to-noise ratio in the five-component mixture. LESA-MS gave a more stable analysis and greater sensitivity compared with DESI-MS. Meat tryptic digests were subjected to peptidomics analysis by DESI-MS and LESA-MS. Bovine, horse, pig, chicken and turkey muscle digests were clearly discriminated using multivariate data analysis (MVA) of the peptidomic datasets. The most abundant ...

Professor Stuart Phillips, McMaster University, Canada delivers a lecture at the International Union of Physiological Sciences held in Birmingham in July 2013. Part of a symposium called Ageing, exercise training, gender, inactivity and nutrition: Implications to skeletal muscle mass and metabolic function in humans his lecture is titled Maximising muscle protein synthesis: influence of nutrition and training modalities

Advancing age is associated with a reduction in skeletal muscle protein, muscle strength, muscle quality, and chemical modifications that may impair protein function. Sarcopenia has been coupled with physical disability, frailty, and a loss of independent function (5, 19). Using stable isotope tracer methodologies and mass spectrometric detection, we observed: (a) 76-92-year-old physically frail and 62-74-year-old middle-age adults have lower mixed muscle protein synthetic rates than 20-32-year-old men and women; (b) 2 weeks and 3 months of weightlifting exercise increased the synthetic rate of myosin heavy chain (MHC) and mixed muscle proteins to a similar magnitude in frail, middle-age, and young women and men; (c) Serum myostatin-immunoreactive protein levels were elevated in physically frail women and were inversely correlated with lean mass. This suggests that the protein synthetic machinery adapts rapidly to increased contractile activity and that the adaptive response(s) are maintained ...

Read Degradation of skeletal muscle protein during growth and development of salmonid fish, Russian Journal of Developmental Biology on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.

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We use single molecule techniques to study the mechanical design of the giant muscle protein titin. Titin spans half the length of a muscle sarcomere and can be...

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NutraBio HMB is a clinically proven ergogenic aid that has been shown in over 50 human studies to improve strength and power gains, increase lean mass, and aid recovery. HMB (short for beta-hydroxy beta-methylbutyrate) in an active metabolite of leucine that has both anticatabolic and anabolic properties. Due to these attributes HMB reduces muscle protein breakdown while also inducing muscle protein synthesis. This means HMB can lead to rapid strength gains in less time, significantly increase lean muscle mass, support more complete muscle recovery, and reduce muscle damage from resistance exercise. In fact, a recent position stand by the International Society of Sports Nutrition validates these claims. Based upon the comprehensive review of the HMB literature they concluded that HMB enhances muscle recovery by attenuating muscle damage; HMB increases muscle hypertrophy, strength, and power in trained and untrained populations when the appropriate exercise protocol is applied; HMB efficacy is ...

To find the optimal level of protein intake at a meal we must determine what the optimal level of protein at a meal for stimulating muscle protein synthesis is. It appears that maximizing skeletal muscle protein synthesis requires approximately ~15g of essential amino acids. It has been postulated that the amino acid leucine is responsible for the stimulatory effect of dietary protein on protein synthesis and 15g of essential amino acids would contain 3.2g of leucine. Thus, in order to determine how much protein from a specific source is required to elicit the maximal response it may be useful to also calculate how much leucine is contained in the source. One could then determine how much of the source must be consumed in order to reach the leucine threshold. For example, whey protein is approximately 12% leucine; therefore, about 27g of whey protein would need to be consumed to reach the threshold for maximal anabolism, whereas a source like chicken, which has a protein content of about 7.5% ...

We determined myofibrillar and mitochondrial protein fractional synthesis rates (FSR), intramuscular signaling protein phosphorylation, and mRNA expression responses after isolated bouts of resistance exercise (RE), aerobic exercise (AE), or in combination [termed concurrent exercise (CE)] in sedentary middle-aged men. Eight subjects (age = 53.3 ± 1.8 yr; body mass index = 29.4 ± 1.4 kg·m2) randomly completed 8 × 8 leg extension repetitions at 70% of one repetition-maximum, 40 min of cycling at 55% peak aerobic power output (AE), or (consecutively) 50% of the RE and AE trials (CE). Biopsies were obtained (during a primed, constant infusion of l-[ring-13C6]phenylalanine) while fasted, and at 1 and 4 h following postexercise ingestion of 20 g of protein. All trials increased mitochondrial FSR above fasted rates (RE = 1.3-fold; AE = 1.5; CE = 1.4; P , 0.05), although only CE (2.2) and RE (1.8) increased myofibrillar FSR (P , 0.05). At 1 h postexercise, phosphorylation of Akt on Ser473 (CE = ...

Imagine grabbing two snakes by the tail so that they cant wriggle off...Under the microscope muscle looks like millions of tiny pistons stac... ...Wilmanns lab and the team of Mathias Gautel an EMBL alumnus and now ...The latest study which arises from more than a decade of collaborativ...,The,giant,protein,titin,helps,build,muscles,biological,biology news articles,biology news today,latest biology news,current biology news,biology newsletters

In this study, we aimed to further dissect the molecular components required for the coordinated organization of Z-line components into regular, hexagonal lattices. We took the approach of searching for protein interactions that anchor the COOH-terminal region of nebulin within the sarcomere. This allowed us to identify the specific binding of the nebulin modules M160-M183, from the peripheral (I-band side) region of the Z-line (Millevoi et al. 1998), with the intermediate filament protein, desmin. Studies are currently under investigation to determine whether desmin and nebulin indeed participate in a coordinated cytoskeletal network that could provide lateral linkages in the Z-line perimyofibrillar space, allowing for efficient force transmission and mechanochemical signaling.. This study has also led to the identification of a novel nebulin-binding protein, myopalladin, which we named based on its striking homology with the recently described ubiquitously expressed protein, palladin (Parast ...

TY - JOUR. T1 - Cardiac titin. T2 - A multifunctional giant. AU - Lewinter, Martin M.. AU - Granzier, Hendrikus Henk. PY - 2010/5/18. Y1 - 2010/5/18. N2 - Titin is responsible for the passive and restoring force of the cardiac sarcomere and makes a major contribution to the diastolic wall stress of the LV, the level of which can be tuned through differential splicing and phosphorylation. PKA and PKG phosphorylation lower stress, and PKC increases it. Changes in titin phosphorylation and titin splicing occur in cardiac disease, in addition to mutations in the titin gene. A host of titin-binding proteins have been discovered that implicate titin as a key player in the organization and development of the sarcomere, in protein turnover, and in sensing mechanical stress. Several stress-sensing signalosomes along the molecule have been discovered, of which only the FHL-based signalosome binds to a spring element (N2B). This N2B-FHL signalosome is ideally situated to sense sarcomere strain and link ...

BCAAs have been proposed to benefit performance in several ways including as a stimulant for muscle protein synthesis (through leucine). BCAAs may also prevent muscle protein breakdown and reduce markers of exercise induced muscle damage. There is also some research suggesting that BCCAs have the potential to act as a fuel source for muscles during exercise, although the research surrounding this is inconclusive. Lastly, BCAAs may interfere with the transport of tryptophan into the brain, reducing the synthesis of serotonin thereby reducing feelings of fatigue.. ...

PHILADELPHIA - Researchers at the University of Pennsylvania School of Medicine have discovered that a protein called leiomodin (Lmod) promotes the assembly of an important heart muscle protein called actin. Whats more, Lmod directs the assembly of actin to form the pumping unit of the heart. The findings appear in this weeks issue of Science.. Very little was known about Lmod when we began this study, says lead author Roberto Dominguez, PhD, Associate Professor of Physiology. It appeared that this protein was present in muscle cells but this had not been demonstrated directly and nobody knew what it did, explains Dominguez. We compared the amino acid sequence of Lmod with the sequence of another protein called tropomodulin [Tmod] that was already known to bind actin filaments in muscle cells. We found that one part of Lmod was very similar to Tmod, but Lmod was a bigger protein than Tmod and contained unique features that made us suspect that it could assemble the actin filaments of the ...

A new study has compared the effect of EAAs in a single doses vs divided doses on muscle protein synthesis in young males at rest. The results may surprise

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Caoileann has a PhD in exercise physiology, focusing on protein metabolism under the supervision of Stu Phillips at McMaster University. She has recently moved back to Dublin to work with Dr. Brendan Egans research group.. ...

Unfortunately, this study leaves us with way more questions than answers. I personally, for example would venture the guess that the ingestion of a complete EAA product would result in an even more profound amelioration of the fasting induced reduction in fractional protein synthesis. That being said, the latter could also compromise another advantage of the non-essential amino acids, I have not even mentioned, yet: their almost non-existent effect on intra-muscular AMPK-expression (cf. figure 2, right). If you read all Intermittent Thoughts articles which dealt with the AMPK/mTOR Metabolic Seesaw and the respective follow-ups, you will be familiar with notion that the fasting-induced phosphorylation of intra-muscular AMPK is responsible for the majority of the health, as well as the closely related fat-burning effects of (intermittent) fasting. Now, if the ingestion of a ~20g bolus of alanine, glycine, proline, histidine, asparagine and serine could increase your skeletal muscle protein ...

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/PRNewswire/ -- Arvinas Inc., a biotechnology company creating a new class of drugs based on protein degradation, today announced it has raised $15 million in...

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References:. 1. Harvard Health Letter. Inflammation: A unifying theory of disease. Harvard Health Publishing, Harvard Medical School, Apr 2006.www.health.harvard.edu/newsletter_article/Inflammation_A_unifying_theory… Accessed 4 Mar. 2019.. 2. Talaro, Kathleen Park. Foundations in Microbiology. Seventh ed., CTI Reviews, 2017.. 3. Toth, M. J.; Matthews, DE; Tracy, RP; Previs, MJ (29 December 2004). Age-related differences in skeletal muscle protein synthesis: relation to markers of immune activation. AJP: Endocrinology and Metabolism. 288 (5): E883-E891. doi:10.1152/ajpendo.00353.2004. 4.Visser, M; Pahor, M; Taaffe, DR; Goodpaster, BH; Simonsick, EM; Newman, AB; Nevitt, M; Harris, TB (May 2002). Relationship of interleukin-6 and tumor necrosis factor-alpha with muscle mass and muscle strength in elderly men and women: the Health ABC Study. The Journals of Gerontology.Series A, Biological Sciences and Medical Sciences. 57 (5): M326-32. doi:10.1093/gerona/57.5.M326. 5. Parimisetty A, ...