Concentrations Of Amino Acids In Muscle Research Articles

Effects of starvation on plasma and muscle amino acid concentrations in normal subjects : [formula omitted], J. Bergström, P. Fürst. Department of Anaesthesia and Intensive Care, St. Göran's Hospital, Stockholm and Department of Renal Medicine, Huddinge Hospital, Huddinge, Sweden

Effects of starvation on plasma and muscle amino acid concentrations in normal subjects : [formula omitted], J. Bergström, P. Fürst. Department of Anaesthesia and Intensive Care, St. Göran's Hospital, Stockholm and Department of Renal Medicine, Huddinge Hospital, Huddinge, Sweden

Branched Chain Amino Acid Uptake and Muscle Free Amino Acid Concentrations Predict Postoperative Muscle Nitrogen Balance

Amino acid solutions rich in branched chain amino acids (BCAA) are commonly utilized both clinically and in experimental protocols in an attempt to reduce skeletal muscle and whole body protein catabolism. To investigate the effectiveness of BCAA infusion, amino acid formulas containing varying concentrations of BCAA were given during operation in this study to three groups of dogs undergoing a standard laparotomy and retroperitoneal dissection. A fourth group was given saline alone. With the use of previously described hindquarter flux techniques, individual and total amino acid nitrogen exchange rates were measured and utilized in estimating skeletal muscle protein catabolism. Intracellular free amino acid concentrations were measured in percutaneous muscle biopsy samples. Although there was no relationship with the rate of BCAA infusion, there was a significant correlation between the rate of BCAA uptake by muscle and diminished total nitrogen release from hindquarter skeletal muscle after operation. There was also a significant relationship between muscle nitrogen balance and the postoperative change in the muscle concentration of either total amino acids or the single amino acid glutamine. When combined in a single equation, BCAA uptake and the change in muscle free amino acid concentration predict skeletal muscle nitrogen release with an r = 0.86. Thus, the rate of BCAA uptake and the free glutamine or total amino acid concentration in muscle appear to be independent predictors of muscle nitrogen balance. The nitrogen-sparing effect of BCAA in skeletal muscle is unrelated to infusion concentration or rate of infusion.

Liver- and muscle amino-acid concentrations during the development of domestic fowl

The concentrations of free amino acids in liver, leg muscle and wing muscle of developing domestic fowl chicks were measured and compared with those of adults. Leg and breast muscles showed a remarkably parallel pattern of change in free-amino-acid concentrations during development up to day 5 after hatching, in agreement with their lack of differentiation up to day 5. Liver free-amino-acid concentration pattern with the development were very similar to those of the muscles, in significant difference with Mammals. Adult free tissue amino acids were lower than those of developing chicks. Most changes in amino-acid concentration in chick tissues were observed around hatching, and have been tentatively attributed to changes in diet. Combined amino acids changed very little during the period studied in muscles and liver. Taurine constituted a very big share of total amino acids.

Amino acid concentrations in plasma and skeletal muscle of patients with acute hemorrhagic necrotizing pancreatitis.

We measured amino acid concentrations in plasma and skeletal muscle of three groups of patients with acute hemorrhagic pancreatitis: (a) patients without secondary organ lesions, (b) patients also suffering from kidney damage, and (c) patients in whom the pancreatitis was accompanied by sepsis and multiple organ failure. In all three groups, especially the third group, the amino acid concentrations in both plasma and muscle were below normal. Glutamine was only 14% of normal in muscle tissue of the third group. Onset of renal insufficiency was indicated by increasing values for 3-methylhistidine and cystathionine; multiple organ failure, by increased concentrations of methionine and phenylalanine in plasma. The low amino acid concentrations of patients with acute pancreatitis can be explained as a combined effect of semistarvation and hypercatabolism. Changes in the plasma concentrations of amino acids did not reflect necessarily the concentrations in muscle tissue.

Catabolic stress on intracellular amino acid pool.

Many studies have documented abnormal plasma concentrations of the free amino acids in patients with different catabolic disorders. The interpretation and the pathogenesis of these abnormal patterns, however, remain speculative. Certain abnormalities appear to be caused by the catabolic stress per se, whereas others, resembling those observed in subjects with low intake of protein and energy, may be related to malnutrition. During catabolic stress the distribution of free amino acids showed to be altered between the extracellular and intracellular compartments1–6. Therefore the plasma concentrations do not necessarily reflect the intracellular concentration. Since skeletal muscle contains the largest pool of free amino acids, determination of the free amino acid concentration in muscle might be of particular interest in the study of amino acid and protein metabolism during catabolic stress and subsequent repletion.

Interorgan metabolism of amino acids in streptozotocin-diabetic ketoacidotic rat

Amino acid concentrations in whole blood, liver, kidney, skeletal muscle, and brain were measured and arteriovenous differences calculated for head, hindlimb, kidney, gut, and liver in control and streptozotocin-diabetic rats. In the control rats, glutamine was released by muscle and utilized by intestine, intestine released citrulline and alanine, liver removed alanine, and the kidneys removed glycine and produced serine. In diabetic rats, the major changes from the pattern of fluxes seen in the normal rat were the release of many amino acids from muscle, with glutamine and alanine predominating, and the uptake of these amino acids by the liver. Glutamine removal by the intestine was suppressed in diabetes, but a large renal uptake of glutamine was evident. Branched-chain amino acids were removed by the diabetic brain, and consequently, brain levels of a number of large neutral amino acids were decreased in diabetes.

Effect of an Anabolic Steroid on Nitrogen Balance and Amino Acid Patterns after Total Hip Replacement

The effect of an anabolic steroid, nandrolone decanoate, on nitrogen balance and plasma and muscle amino acid concentrations was studied in patients undergoing total hip replacement and receiving daily postoperative infusions of 5% dextrose and 3.5% amino acids. An intramuscular injection of 200 mg immediately after operation resulted in a nitrogen balance of -48 mg N/kg . day for the first 3 days, as compared to 102 mg N/kg . day in noninjected controls. After steroid injection there was also an attenuation of trauma-induced changes in amino acid concentrations in muscle but not in plasma. This suggests that nandrolone decanoate may act directly on muscle to reduce the protein catabolism which follows a major form of operative trauma.

Metabolic disorders in severe abdominal sepsis: Glutamine deficiency in skeletal muscle

The metabolic profiles of 14 patients with prolonged abdominal sepsis were analysed on the second day after laparotomy. The profiles of survivors were compared with those of non-survivors who died one to five days after the time of evaluation due to uncontrollable multiple organ failure. In the non-surviving patients plasma gluoose and glucagon levels were significantly higher than in surviving patients. The plasma concentrations of phosphoserine, cysteine, valine, phenylalanine, and 3-methylhistidine were found to be significantly increased in non-survivors and their muscle tissue showed significantly decreased concentrations of glutamine, proline and lysine with increases in valine and leucine. A correct classification of non-survivors and survivors could be obtained from the plasma and muscle amino acid concentrations, the highest discriminant power being from muscle glutamine. In severe sepsis metabolic changes correlate with the outcome of the patients, and amino acid metabolism seems to be characterised by low concentrations of muscle glutamine and high levels of the branched chain amino acids possibly indicating an inhibited intracellular glutamine formation in muscle tissue.

Muscle and plasma amino acids after injury: hypocaloric glucose vs. amino acid infusion.

This study examines the effect of three different hypocaloric diets on the patterns of muscle and plasma amino acids in patients undergoing total hip replacement. Group I (seven patients) received 90 g/day of glucose, Group II (seven patients) received 70 g/day of amino acids, Group III (eight patients) received both 90 g of glucose and 70 grams of amino acids per day. Utilizing the percutaneous biopsy technique of Bergström, free amino acid patterns in muscle and plasma were analyzed pre- and postoperatively (day 4). The postoperative pattern of amino acids was characterized by elevated levels in muscle and plasma of the branched chain amino acids, phenylalanine, tyrosine and methionine. There was a marked decrease in muscle glutamine and smaller decreases in the basic amino acids in both muscle and plasma. Muscle:plasma concentration ratios increased for the neutral amino acids, decreased for glutamine and the basic amino acids and were unchanged for the acidic amino acids. The patterns seen after hip replacement are almost identical to those seen after colectomy or accidental injury. There was little effect of diet on amino acid concentrations in muscle. In plasma, concentrations of leucine, isoleucine, valine and proline were higher in Group II in the absence of glucose intake, than in the other groups. Lysine was lower in Group I with no amino acid intake than in the other groups. Thus, there is a unique amino acid pattern associated with operative trauma which is relatively unaffected by hypocaloric, intravenous nutrition.

Effect of isoproterenol on amino acid levels and protein turnover in skeletal muscle.

The effect of isoproterenol on amino acid concentrations in perfusate and skeletal muscle was studied during a 3-h perfusion of the isolated rat hemicorpus. The beta-adrenergic agonist inhibited the accumulation of alanine, threonine, phenylalanine, tyrosine, lysine, arginine, leucine, and valine and increased the loss of glutamate, aspartate, serine, and isoleucine from the pool of free amino acids in perfusate and muscle. The loss of glutamate was accompanied by a greater accumulation of glutamine. Changes in alanine levels showed the greatest response with a net accumulation of 98 mumol in the controls becoming a net loss of 54 mumol in the experimentals. These changes in amino acid levels were accounted for in part by a 20% decrease in protein degradation. Protein synthesis was not affected by isoproterenol. In addition to an effect on degradation, it appeared that isoproterenol affected amino acid levels by increasing alanine utilization and causing formation of glutamine instead of alanine. Other effects of the drug included increased rates of lactate production, muscle glycogen breakdown, and oxygen consumption, whereas no effects were observed on ATP and creatine phosphate levels. Pyruvate content of muscle was maintained at a higher level in the presence of the drug than in control perfusions.

Influence of denervation of the free amino acids of the rat diaphragm

The concentrations of free amino acids in diaphragm muscle have been measured at intervals following unilateral nerve action. Marked increases of alanine, glycine, glutamine and the serine/asparagine peakd were seen between 3 and 7 days, but little change occurred for most other amino acids. Comparison is made with the data on changes of amino acid concentration in muscle in response to insulin, in liver during regeneration and with metabolic changes taking place in the denervated tissue.

Amino acid levels in plasma, liver, muscle, and kidney during and after exercise in fasted and fed rats.

ARTICLESAmino acid levels in plasma, liver, muscle, and kidney during and after exercise in fasted and fed ratsJ Christophe, J Winand, R Kutzner, and M HebbelinckJ Christophe, J Winand, R Kutzner, and M HebbelinckPublished Online:01 Aug 1971https://doi.org/10.1152/ajplegacy.1971.221.2.453MoreSectionsPDF (1 MB)Download PDF ToolsExport citationAdd to favoritesGet permissionsTrack citations ShareShare onFacebookTwitterLinkedInEmailWeChat Previous Back to Top Next Download PDF FiguresReferencesRelatedInformationCited ByExercise in ZDF rats does not attenuate weight gain, but prevents hyperglycemia concurrent with modulation of amino acid metabolism and AKT/mTOR activation in skeletal muscle13 August 2014 | European Journal of Nutrition, Vol. 54, No. 5Hyperpolarized 13C lactate as a substrate for in vivo metabolic studies in skeletal muscle6 February 2014 | Metabolomics, Vol. 10, No. 5Impact of glutamine supplementation on glucose homeostasis during and after exerciseSoh Iwashita, Phillip Williams, Kareem Jabbour, Takeo Ueda, Hisamine Kobayashi, Shawn Baier, and Paul J. 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Biochemical and molecular adjustments in bloodBolletino di zoologia, Vol. 55, No. 1-4Development of the gestational plasma hypoaminoacidemia in the ratComparative Biochemistry and Physiology Part A: Physiology, Vol. 85, No. 4Effect of starvation and protein-feeding on blood amino acid compartmentation of domestic fowl hatchlingsComparative Biochemistry and Physiology Part A: Physiology, Vol. 84, No. 3Liver- and muscle amino-acid concentrations during the development of domestic fowl26 September 2008 | Archives Internationales de Physiologie et de Biochimie, Vol. 94, No. 3Effect of daily exercise and food intake on leucine oxidationBiochemical Medicine, Vol. 33, No. 1Defect in α-ketobutyrate metabolism: a new inborn errorClinica Chimica Acta, Vol. 145, No. 2Gas—liquid chromatography of free amino acids in the cytosol of mammalian atrium and ventricle of the heartJournal of Chromatography B: Biomedical Sciences and Applications, Vol. 276Distribution of amino acids and amino-acid enzymes in whole kidney and renal cortex. 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Katz1 August 1981 | American Journal of Physiology-Endocrinology and Metabolism, Vol. 241, No. 2Adrenalectomy alters acid-soluble leucine pool in rat kidney and heartInternational Journal of Biochemistry, Vol. 13, No. 4Glutaminase activity in rat skeletal muscle mitochondriaExperientia, Vol. 34, No. 2Determination of plasma amino acids in small samples with the use of Dansyl-chlorideBiochimie, Vol. 58, No. 10Changes of free amino acids in plasma of healthy subjects induced by physical exerciseEuropean Journal of Applied Physiology and Occupational Physiology, Vol. 35, No. 1The Control of Ammonia Production in the RatMedical Clinics of North America, Vol. 59, No. 3Effects of Long Lasting Physical Exercise and Training on Protein MetabolismFree Amino Acids in Normal and Varicose Human Saphenous Veins27 September 2008 | Archives Internationales de Physiologie et de Biochimie, Vol. 83, No. 1Gluconeogenesis from Serine by the Serine-Dehydratase-Dependent Pathway in Rat LiverEuropean Journal of Biochemistry, Vol. 43, No. 3Distribution of plasma amino acids in humans during submaximal prolonged exerciseEuropean Journal of Applied Physiology and Occupational Physiology, Vol. 32, No. 2The glucose-alanine cycleMetabolism, Vol. 22, No. 2GluconeogenesisMetabolism, Vol. 21, No. 10Pattern of Twenty-Four Plasma Amino Acids in Rats Before and After Muscular Exercise27 September 2008 | Archives Internationales de Physiologie et de Biochimie, Vol. 80, No. 5 More from this issue > Volume 221Issue 2August 1971Pages 453-457 Copyright & PermissionsCopyright © 1971 by American Physiological Societyhttps://doi.org/10.1152/ajplegacy.1971.221.2.453PubMed5560294History Published online 1 August 1971 Published in print 1 August 1971 Metrics

Effects of environmental salinity of free amino acids of Crassostrea virginica gmelin

1. 1. Total free amino acid (FAA) concentration in Crassostrea virginica adductor muscle increases proportionally with increasing salinity. Individual FAA are to some extent regulated. A few (glycine, proline, taurine, leucine and isoleucine) are maintained at minimum concentrations in low salinities. Other FAA (cysteic acid, aspartic acid, threonine, serine, cysteine, tyrosine, phenylalanine, ornithine, lysine and arginine) and ammonia are maintained at relatively constant concentrations through the salinity range. 2. 2. Free taurine, proline, glycine and alanine concentrations increase with increasing salinity over at least part of the salinity range. Free histidine is the only amino acid to exhibit a decrease in concentration with increasing salinity over part of the range. 3. 3. The mechanisms that regulate the FAA concentration in adductor muscle are not known, but are probably dependent to some extent on cation concentrations.