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PubMed2000

Intravenous glutamine does not stimulate mixed muscle protein synthesis in healthy young men and women.

We investigated the effects of a glutamine-supplemented amino acid mixture on vastus lateralis muscle protein synthesis rate in healthy young men and women. Three men and 3 women (27.8 +/- 2.0 yr, 22.2 +/- 1.0 body mass index [BMI], 56.1 +/- 4.5 kg lean body mass [LBM]) received a 14-hour primed, constant intravenous infusion of L[1-13C]leucine to evaluate the fractional rate of mixed muscle protein synthesis. In addition to tracer administration, a clinically relevant amino acid mixture supplemented with either glutamine or glycine in amounts isonitrogenous to glutamine, was infused. Amino acid mixtures were infused on separate occasions in random order at a rate of 0.04 g/kg/h (glutamine at approximately 0.01 g/kg/h) with at least 2 weeks between treatment. For 2 days before and on the day of an infusion, dietary intake was controlled so that each subject received 1.5 g protein/kg/d. Compared with our previous report in the postabsorptive state, amino acid infusion increased the fractional rate of mixed muscle protein synthesis by 48% (P < .05); however, the addition of glutamine to the amino acid mixture did not further elevate muscle protein synthesis rate (ie, 0.071% +/- 0.008%/h for amino acids + glutamine v 0.060% +/- 0.008%/h for amino acids + glycine; P = .316). Plasma glutamine concentrations were higher (P < .05) during the glutamine-supplemented infusion, but free intramuscular glutamine levels were not increased (P = .363). Both plasma and free intramuscular glycine levels were increased when extra glycine was included in the infused amino acid mixture (both P < .0001). We conclude that intravenous infusion of amino acids increases the fractional rate of mixed muscle protein synthesis, but addition of glutamine to the amino acid mixture does not further stimulate muscle protein synthesis rate in healthy young men and women.

Adult↗
PubMed1993

Short-term growth hormone treatment does not increase muscle protein synthesis in experienced weight lifters.

The purpose of this study was to determine whether recombinant human growth hormone (GH) administration enhances muscle protein anabolism in experienced weight lifters. The fractional rate of skeletal muscle protein synthesis and the whole body rate of protein breakdown were determined during a constant intravenous infusion of [13C]leucine in 7 young (23 +/- 2 yr; 86.2 +/- 4.6 kg) healthy experienced male weight lifters before and at the end of 14 days of subcutaneous GH administration (40 microgram.kg-1 x day-1). GH administration increased fasting serum insulin-like growth factor-I (from 224 +/- 20 to 589 +/- 80 ng/ml, P = 0.002) but did not increase the fractional rate of muscle protein synthesis (from 0.034 +/- 0.004 to 0.034 +/- 0.002%/h) or reduce the rate of whole body protein breakdown (from 103 +/- 4 to 108 +/- 5 mumol.kg-1 x h-1). These findings suggest that short-term GH treatment does not increase the rate of muscle protein synthesis or reduce the rate of whole body protein breakdown, metabolic alterations that would promote muscle protein anabolism in experienced weight lifters attempting to further increase muscle mass.

Adult↗
PubMed2005

Control of muscle protein kinetics by acid-base balance.

PURPOSE OF REVIEW: Abnormalities of acid-base balance accompany many pathological conditions. Acidosis is associated with several diseases such as chronic renal failure, diabetic ketosis, severe trauma and sepsis, and chronic obstructive respiratory disease, which are often associated with muscle wasting. There is evidence that acidosis can induce muscle protein catabolism and it could therefore be an important factor contributing to loss of muscle protein in these conditions. This review aims at outlining the effects of acid-base balance abnormalities on muscle protein metabolism, and will in particular summarize and evaluate the most recent studies on the impact of pH on control of muscle protein metabolism. RECENT FINDINGS: Acidosis has been shown to promote muscle protein catabolism by stimulating protein degradation and amino acid oxidation. This effect is achieved through up-regulation of the ubiquitin-proteasome pathway - one of the major enzyme systems for protein degradation. Recent studies in animals and humans have also shown that acidosis inhibits muscle protein synthesis. Little is known about the mechanisms by which acidosis depresses protein synthesis, or of the impact of alkalosis on protein metabolism. SUMMARY: Increasing evidence suggests that acidosis promotes muscle protein wasting by both increasing protein degradation and inhibiting protein synthesis. Correction of acidosis may therefore help to preserve muscle mass and improve the health of patients with pathological conditions associated with acidosis.

Acid-Base Equilibrium↗
PubMed2001

Muscle protein metabolism in the elderly: influence of exercise and nutrition.

Although the causes of sarcopenia are multi-factorial, at least some, such as poor nutrition and inactivity, may be preventable. Changes in muscle mass must be a result of net muscle protein breakdown over that particular time period. Stable isotope methodology has been used to examine the metabolic basis of muscle loss. Net muscle protein breakdown may occur due to a decrease in the basal level of muscle protein synthesis. However, changes of this type would likely be of small magnitude and undetectable by current methodology. Hormonal mediators may also be important, especially in association with forced inactivity. Net muscle protein breakdown may be also attributed to alterations in the periods of net muscle protein synthesis and breakdown each day. Reduced activity, combined with ineffectual nutrient intake, could lead to decreased net muscle protein balance. Chronic resistance exercise training clearly is an effective means of increasing muscle mass and strength in elderly individuals. Although sometimes limited, acute metabolic studies provide valuable information for maintenance of muscle mass with age.

Aged↗
PubMed2000

Requirements of Kettin, a giant muscle protein highly conserved in overall structure in evolution, for normal muscle function, viability, and flight activity of Drosophila.

Kettin is a giant muscle protein originally identified in insect flight muscle Z-discs. Here, we determined the entire nucleotide sequence of Drosophila melanogaster kettin, deduced the amino acid sequence of its protein product (540 kD) along with that of the Caenorhabditis elegans counterpart, and found that the overall primary structure of Kettin has been highly conserved in evolution. The main body of Drosophila Kettin consists of 35 immunoglobulin C2 domains separated by spacers. The central two thirds of spacers are constant in length and share in common two conserved motifs, putative actin binding sites. Neither fibronectin type III nor kinase domains were found. Kettin is present at the Z-disc in several muscle types. Genetic analysis showed that kettin is essential for the formation and maintenance of normal sarcomere structure of muscles and muscle tendons. Accordingly, embryos lacking kettin activity cannot hatch nor can adult flies heterozygous for the kettin mutation fly.

Amino Acid Sequence↗
PubMed1982

Leucine incorporation into skeletal muscle proteins in vitro and protein synthesis by isolated ribosomes from skeletal muscle around a high velocity missile injury.

Protein synthesis in skeletal muscle around a high velocity missile injury was investigated in two series of experiments. In the first series a shot wound was induced in the hindleg of dogs. Muscle biopsies were taken at various distances from the wound channel and bundles of muscle fibre were incubated in a medium containing 14C-leucine under protein synthetizing conditions. A significant reduction in the rate of leucine incorporation into muscle protein was seen in the adjacent to the wound channel. At a distance of 3 cm from the bullet track no reduction in leucine incorporation into protein occurred. In the second series of experiments a high velocity missile injury was induced in the hindleg of pigs. The capacity of ribosomes to incorporate 14C-phenylalanine into protein was analyzed. Ribosomes were isolated from skeletal muscle around the shot wound. The effect of missile injury alone and that of the combined effect of missile injury and hemorrhage were studied. A marked reduction in ribosomal activity was found in tissue adjacent to and up to 2.4 cm from the wound channel. At a distance of 3 cm from the wound ribosomal activity remained unaffected. Ribosomal activity was significantly more reduced in tissue close to the wound channel after missile injury and hemorrhage than after missile injury alone. The reduced capacity for protein synthesis in muscle around the missile injury found in this study probably reflects a lowered cellular energy level. The local metabolic changes were aggrevated in animals where hemorrhage was also induced indicating that in the clinical situation prevention of hemorrhage and hypovolemia might reduce the amount of tissue that has to be excised following a short wound.

Animals↗
PubMed2006

Quantification of amino acid transport through interstitial fluid: assessment of four-compartment modeling for muscle protein kinetics.

The purpose of this study was to assess a novel technique for quantifying in vivo muscle protein metabolism and phenylalanine transport in septic patients and normal volunteers and thereby assess the influence of sepsis on muscle protein kinetics. In patients resuscitated from sepsis, blood flow and edema may influence the extent of muscle loss. Six adult patients septic from pneumonia underwent a study protocol consisting of infusion of isotopic phenylalanine, indocyanine green dye, and sodium bromide; biopsies of skeletal muscle; and sampling from the femoral artery, vein, and interstitial fluid. Study results demonstrate a substantial net catabolism of muscle, an accelerated flux of phenylalanine, and an increased leg blood flow for septic patients compared with normal volunteers. For septic patients and normal volunteers, the rate of phenylalanine transport through the interstitium was rate limiting for the movement of phenylalanine between vasculature and muscle. Measurements demonstrate a concentration gradient of phenylalanine favoring the net efflux of amino acids from the leg in the septic patients. Despite whole body edema, the extracellular fluid volume within muscle of septic patients was similar to normal. These findings demonstrate that the extent of muscle loss in critically ill patients results from the net increase in the rate of muscle protein breakdown, which subsequently drives amino acids through the interstitial compartment down their concentration gradient. Therefore, any effective therapy to correct illness-induced muscle catabolism should be directed at altering the rates of breakdown and synthesis of muscle protein and are not likely related to tissue edema.

Adult↗
PubMed2005

Method for the determination of the arteriovenous muscle protein balance during non-steady-state blood and muscle amino acid concentrations.

We describe a method based on the traditional arteriovenous balance technique in conjunction with muscle biopsies for the determination of leg muscle protein balance during the nonsteady state in blood amino acid concentrations. Six young, healthy individuals were studied in the postabsorptive state (pre-Phe) and after a bolus ingestion of approximately 0.5 g phenylalanine (post-Phe). Post-Phe free phenylalanine concentrations in blood and muscle increased (P < 0.05), but the respective concentrations of the amino acid threonine did not change. The average post-Phe leg net balance (NB) for threonine decreased from basal (P < 0.05), but that for phenylalanine did not change. A volume of distribution for free phenylalanine in the leg was calculated based on the leg lean mass and the relative muscle water content and used to estimate the rate of accumulation of free phenylalanine in the leg. When the post-Phe NB for phenylalanine was corrected for the rate of accumulation of free phenylalanine in the leg, the post-Phe NB for phenylalanine decreased from basal (P < 0.05). This corrected value was not different (P > 0.05) from the value predicted for the phenylalanine NB based on the pre- and post-Phe NB responses for threonine. We conclude that the protein NB in non-steady-state blood phenylalanine concentrations can be determined from the arteriovenous phenylalanine NB by accounting for changes in free phenylalanine within its volume of distribution.

Adult↗
PubMed1992

Uncomplicated surgery, but not general anesthesia, decreases muscle protein synthesis.

The impact of anesthesia and surgery on protein metabolism is not well characterized. The single effect of general anesthesia and the combined effects of surgery and general anesthesia on protein synthesis in skeletal muscle were studied in metabolically healthy patients (n = 14) undergoing elective abdominal surgery. The rate of muscle protein synthesis was calculated from the increase in enrichment of [1-13C]leucine in protein during 90 min after an intravenous infusion of [1-13C]leucine (0.05 g/kg, 20 atom percent excess). The 1-13C enrichments of plasma leucine and plasma alpha-ketoisocaproate were used to indicate the enrichment of muscle free leucine. The protein synthesis rate was unaffected by general anesthesia; however, at the end of surgery, a 31.5% decline was seen from 2.19(2.13,2.33)%/24 h before anesthesia to 1.50(1.21,1.77)%/24 h (P less than 0.05) immediately after cholecystectomy while the patients were still under general anesthesia.

Anesthesia, General↗
PubMed2003

Active involvement of PKC for insulin-mediated rates of muscle protein synthesis in Zucker rats.

A recent report from our group demonstrated that insulin facilitates muscle protein synthesis in obese Zucker rats. The purpose of this study was to determine whether PKC, a probable modulator of insulin signal transduction and/or mRNA translation, has a role in this insulin-mediated anabolic response. In the first portion of the study, gastrocnemius muscles of lean and obese Zucker rats (n = 5-7 for each phenotype) were bilaterally perfused with or without insulin to assess cytosolic and membrane PKC activity. Limbs perfused with insulin demonstrated greater PKC activity in both lean and obese Zucker rats (P < 0.05) compared with no insulin, but overall activity was greater in obese animals (by approximately 27% compared with lean, P < 0.05). To determine whether PKC plays a role in muscle protein synthesis, hindlimbs (n = 6-8 for each phenotype) were bilaterally perfused with or without insulin and/or GF-109203X (GF; a PKC inhibitor). The presence of GF did not influence the rates of insulin-mediated protein synthesis in gastrocnemius muscle of lean Zucker rats. However, when obese rats were perfused with GF (P < 0.05), the effect of insulin on elevating rates of protein synthesis was not observed. We also used phorbol 12-myristate 13-acetate (TPA, a PKC activator; n = 5-7 for each phenotype) with and without insulin to determine the effect of PKC activation on muscle protein synthesis. TPA alone did not elevate muscle protein synthesis in lean or obese rats. However, TPA plus insulin resulted in elevated rates of protein synthesis in both phenotypes that were similar to rates of insulin alone of obese rats. These results suggest that PKC is a modulator and is necessary, but not sufficient, for insulin-mediated protein anabolic responses in skeletal muscle.

Animals↗
PubMed1978

Ntau-methylhistidine (3-methylhistidine) and muscle protein turnover: an overview.

Actin and myosin, the contractile proteins of skeletal muscle, are methylated following peptide bond synthesis, with production of Ntau-methylhistidine (3-methylhistidine, 3-MeHis). During intracellular breakdown of these proteins, the 3-MeHis is released and excreted in the urine. Studies on tissue distribution of 3-MeHis and on its qunatitative excretion following administration to rats and to man show that urinary output of this amino acid provides a reliable index of the rate of myofibrillar protein breakdown in the musculature of intact rats and human subjects. Estimates of the fractional rate of muscle protein breakdown based on 3-MeHis data are consistent with rates computed by other techniques. By this technique, it has been shown that the fractional rate of muscle protein breakdown is not significantly different in the elderly as compared with young adults. However, since muscle mass is less in the elderly, it makes a smaller contribution to whole body protein breakdown with aging in humans. Output of 3-MeHis diminishes in growing rats and obese human subjects with protein or energy restriction, though the initial response of myofibrillar protein breakdown in growing rats to protein and protein-energy restriction differs. Measurement of 3-MeHis excretion has also proved useful in exploring the effects of physical and thermal trauma on the rate of muscle useful in exploring the effects of physical and thermal trauma on the rate of muscle protein breakdown.

Aging↗
PubMed2006

Skeletal muscle protein metabolism and resistance exercise.

Stable isotope tracer techniques have been developed to quantify rates of muscle protein synthesis and breakdown in human subjects. These methods were applied to the study of the response to resistance exercise as well as to amino acid intake. The fractional synthetic rate (FSR) of muscle protein is stimulated for as long as 48 h following exercise. However, the anabolic effect of the stimulation of FSR after exercise is blunted by a simultaneous increase in muscle protein breakdown, such that the net balance between synthesis and breakdown remains negative in the fasted state. Elevation of plasma amino acids stimulates muscle protein synthesis. The extent of the stimulation is dependent on the dose, the profile of amino acids given, the pattern of ingestion (bolus vs. constant intake), the age of the subject, and the hormonal profile. Importantly, there is an interactive effect between resistance exercise and amino acids, such that the net anabolic response to amino acids following exercise is greater than the sum of the amino acid effects and the exercise effects alone.

Amino Acids↗
PubMed2002

The nesprins are giant actin-binding proteins, orthologous to Drosophila melanogaster muscle protein MSP-300.

Nesprin-1 and nesprin-2 (also known as Syne-1 and Syne-2,) are large ( approximately 3300-residue) vertebrate proteins associated with emerin and lamin A at the nuclear envelope of muscle cells and other cell types. We show that the previously described nesprins are short isoforms of giant proteins comprising an actin-binding amino-terminus connected to a carboxy-terminal klarsicht-related transmembrane domain by a massive ( approximately 6000-8000 amino acid) spectrin-like rod domain, making full-length nesprin-1, at one megadalton, the largest non-titin protein hitherto described in humans. We find that MSP-300, a 7000-residue Drosophila melanogaster protein whose disruption results in defects of muscle development, corresponds to the N-terminal two-thirds of the Drosophila nesprin ortholog. A nesprin-like protein is also encoded by the nematode genome. Moreover, we demonstrate that the larger isoforms of nesprin-1, like MSP-300, are localized to the sarcomeric Z-line of both skeletal and cardiac muscle. The recognition that a characteristic muscle-specific mutant phenotype in the fly results from a disruption of its nesprin ortholog reinforces the candidacy of the human proteins for involvement in genetic diseases of skeletal and cardiac muscle.

Amino Acid Sequence↗
PubMed2003

Acute in vivo elevation of insulin-like growth factor (IGF) binding protein-1 decreases plasma free IGF-I and muscle protein synthesis.

This study examined whether the acute elevation of IGF-binding protein-1 (IGFBP-1) decreases the plasma free IGF-I concentration and alters in vivo rates of muscle protein synthesis and glucose uptake. The plasma concentration of human IGFBP-1 was increased to approximately 95 ng/ml in conscious catheterized rats infused iv with human IGFBP-1 for 4 h. Infusion of IGFBP-1 also increased the concentration of endogenous (e.g. rat) IGFBP-1 in the blood, and this response was associated with a 2- to 3-fold elevation of IGFBP-1 mRNA in liver and kidney. IGFBP-1 did not significantly alter the plasma concentration of total IGF-I, but decreased circulating free IGF-I levels by about 50%. IGFBP-1 decreased protein synthesis in the predominantly fast-twitch gastrocnemius muscle (20%), and this change resulted from a decreased translational efficiency that was associated with a decreased phosphorylation of S6K1, but not 4E-BP1. Complementary studies demonstrated that IGFBP-1 also decreased the rates of protein synthesis under basal conditions and in response to stimulation by IGF-I when added in vitro to the fast-twitch epitrochlearis muscle. In contrast, IGFBP-1 did not alter in vivo-determined rates of protein synthesis in the slow-twitch soleus muscle, heart, liver, or kidney. The infusion of IGFBP-1 did not significantly alter the plasma glucose or lactate concentration or the whole body rate of glucose production or disposal. The above-mentioned changes were not mediated indirectly by changes in the plasma insulin or corticosterone concentrations, decreased high energy phosphate content in muscle, or hepatoxicity produced by the infused IGFBP-1. These results demonstrate that acute in vivo elevation in IGFBP-1, of the magnitude observed in various catabolic conditions, is capable of selectively decreasing protein synthesis in fast-twitch skeletal muscle and up-regulating the hepatic and renal syntheses of IGFBP-1 per se. Hence, elevations in circulating and tissue levels of IGFBP-1 may be an important mediator for the muscle catabolism observed in various stress conditions.

Animals↗
PubMed1997

Effects of recombinant human growth hormone on muscle protein turnover in malnourished hemodialysis patients.

To assess the effect of recombinant human growth hormone (rhGH) on muscle protein metabolism in uremic patients with malnutrition, forearm [3H]phenylalanine kinetics were evaluated in six chronically wasted (body weight 79% of ideal weight) hemodialysis (HD) patients in a self-controlled, crossover study. Forearm protein dynamics were evaluated before, after a 6-wk course of rhGH (5 mg thrice weekly) and after a 6-wk washout period. After rhGH: (a) forearm phenylalanine net balance--the difference between phenylalanine incorporation into and phenylalanine release from muscle proteins--decreased by 46% (-8+/-2 vs. -15+/-2 nmol/min x 100 ml at the baseline and -11+/-2 after washout, P < 0.02); (b) phenylalanine rate of disposal, an index of protein synthesis, increased by 25% (25+/-5 vs. 20+/-5 at the baseline and 20+/-4 after washout, P < 0.03); (c) phenylalanine rate of appearance, an index of protein degradation, was unchanged (33+/-5 vs. 35+/-5 at the baseline and 31+/-4 after washout); (d) forearm potassium release declined (0.24+/-0.13 vs. 0.60+/-0.15 microeq/min at the baseline, and 0.42+/-0.20 microeq/min after washout P < 0.03); (e) changes in the insulin-like growth factor binding protein (IGFBP)-1 levels and insulin-like growth factor-I (IGF-I)/IGFBP-3 ratios accounted for 15.1% and 47.1% of the percent variations in forearm net phenylalanine balance, respectively. Together, these two factors accounted for 62.2% of variations in forearm net phenylalanine balance during and after rhGH administration. These data indicate: (a) that rhGH administration in malnourished hemodialysis patients is followed by an increase in muscle protein synthesis and by a decrease in the negative muscle protein balance observed in the postabsorptive state; and (b) that the reduction in net protein catabolism obtained with rhGH can be accounted for by the associated changes in circulating free, but not total, IGF-I levels.

Adult↗
PubMedDate not supplied

Comparative effects of thermal and surgical trauma on rat muscle protein metabolism.

A modified intraperitoneal pool flooding technique, employing L-3H-tyrosine, was developed for measuring muscle protein synthetic rates following traumatic injury. Sufficient radiolabeled tyrosine was injected intraperitoneally to effect a six-fold increase in plasma tyrosine concentration (124-800 microM) resulting in constant, sustained specific radioactivities in plasma- and intracellular-free tyrosine pools. Localized vs systemic effects of thermal and surgical trauma on gastrocnemius muscle protein turnover were assessed 2 and 4 days postinjury. Thermal trauma increased total, myofibrillar, and sarcoplasmic muscle protein synthesis (44%) and protein degradation (300%). Conversely, surgical trauma decreased synthesis of total (24%), myofibrillar (14%), and sarcoplasmic (43%) muscle proteins without altering protein degradation. Short-term restriction of pair-fed controls did not affect either aspect of protein turnover.

Animals↗
PubMed1978

Effects of age, sex and starvation on the turnover of plasma, liver and breast muscle proteins in the Japanese quail.

Half-lives of the plasma, liver and breast muscle proteins in female, old male, young male and starved young male Japanese quail were measured by following the changes in protein specific radioactivity over a period of 7 days. The female birds showed the shortest half-lives for plasma and liver proteins and very long half-lives for breast muscle proteins. Compared to the proteins from the female birds, the old and young male birds showed slightly longer half-lives for plasma and insoluble liver proteins and shorter half-lives for soluble liver and breast muscle proteins. Starved birds showed greatly increased half-lives for all proteins when compared to the corresponding proteins from the other groups of quail. In general, the trends shown for the turnover of proteins from plasma, liver and breast muscle of the four groups of quail were similar to turnovers reported for rats under similar treatment conditions.

Aging↗
PubMed1989

Effect of dietary thyroxine on growth and muscle protein metabolism in broiler chickens.

The effects of thyroxine (T4) on growth, feed efficiency, breast muscle (Musculus pectoralis profundus) weight, liver weight, abdominal fat content, and rates of muscle protein synthesis (Ks) and breakdown (Kd) estimated by N tau-methylhistidine excretion were investigated in broiler chickens of both sexes. Dietary inclusion of .4 ppm T4 resulted in a less abdominal fat content in female chickens and a higher muscle protein synthesis rate in male chickens. Administration of T4 at the level of 1.2 ppm produced higher feed efficiency in both sexes and greater muscle weight and muscle protein synthesis rate in male chickens. This treatment also produced less abdominal fat content in female chickens. Administration of T4 at the level of 3.6 ppm produced lower body weight gain, breast muscle weight, liver weight, and abdominal fat content in both sexes and both higher protein synthesis and breakdown in skeletal muscle in male chickens. These experiments demonstrated that the abdominal fat content could be successfully reduced by dietary inclusion of T4, especially in female broiler chickens. The findings in the present investigation suggested that the improved feed efficiency and muscle growth were largely accomplished by the increase in muscle protein synthesis induced by the dietary inclusion of thyroxine.

Abdomen↗