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PubMed1998

Protein and amino acid metabolism in human muscle.

Muscle proteins turn over slowly and there are minimal diurnal changes in the size of the muscle protein pool in response to feeding and fasting. Nitrogen balance and tracer studies indicate that protein oxidation and net protein breakdown (degradation--synthesis) is not increased during dynamic exercise at intensities of < or = 70% VO2max. An imbalance between muscle protein synthesis and degradation does exist during one leg knee extensor exercise and during two legged cycling in patients with glycogen phosphorylase deficiency. In these latter cases amino acids liberated from the protein pool are used for synthesis of TCA-cycle intermediates and glutamine. Six amino acids are metabolized in resting muscle: leucine, isoleucine, valine, asparagine, aspartate and glutamate. Only leucine and part of the isoleucine molecule can be converted to acetylCoA and oxidized. The carbon skeleton of the other amino acids is used for synthesis of TCA-cycle intermediates and glutamine. The six amino acids provide the amino groups and the ammonia for synthesis of glutamine and alanine, which are released by muscle in excessive amounts. About half of the glutamine release from muscle originates from glutamate taken up from the blood. Glutamine produced by muscle is an important fuel and regulator of DNA and RNA synthesis in mucosal cells and immune system cells and fulfils several other important functions in human metabolism. The alanine aminotransferase reaction functions to establish and maintain high concentrations of TCA-cycle intermediates and a high TCA cycle flux in the first minutes of exercise. A gradual increase in leucine oxidation subsequently leads to a carbon drain on the TCA-cycle in glycogen depleted muscles and may thus reduce the maximal flux in the TCA-cycle and lead to fatigue. Deamination of amino acids and glutamine synthesis present alternative anaplerotic mechanisms in glycogen depleted muscles but only allow exercise at 40-50% of Wmax. It is proposed that the maximal flux in the TCA-cycle is reduced in glycogen depleted muscles due to insufficient TCA-cycle anaplerosis and that this presents a limitation for the maximal rate of fatty acid oxidation. Interactions between the amino acid pool and the TCA-cycle thus seem to play a central role in the energy metabolism of the exercising muscle.

Amino Acids↗
PubMed1999

Counter-regulatory hormones and mechanisms in amino acid metabolism with special reference to the catabolic response in skeletal muscle.

There is evidence that both counter-regulatory hormones, in particular glucocorticoids, and cytokines influence amino acid and protein metabolism in skeletal muscle, and that these two groups of regulators interact in the development of muscle catabolism. Glucocorticoids stimulate muscle proteolysis during sepsis and also in other catabolic conditions. In addition, glucocorticoids regulate muscle glutamine metabolism, resulting in increased glutamine release and reduced glutamine concentrations in skeletal muscle. Glucocorticoids inhibit the glutamine transporter in skeletal muscle and stimulate glutamine synthetase activity. Proinflammatory cytokines, in particular tumor necrosis factor and interleukin-1, inhibit muscle amino acid transport by system A, and these cytokine effects are probably indirect. Most of the catabolic effects of tumor necrosis factor in skeletal muscle, including stimulated protein degradation and inhibited amino acid uptake, are mediated by glucocorticoids.

Amino Acids↗
PubMed2001

Effects of exercise on amino acid metabolism in patients with chronic obstructive pulmonary disease.

Depletion of fat-free mass (FFM) significantly contributes to decreased skeletal muscle weakness and impaired exercise capacity in patients with chronic obstructive pulmonary disease (COPD). FFM wasting suggests disturbances in intermediary metabolism, confirmed by data showing profound alterations in the skeletal muscle amino acid (AA) status in COPD at rest. To unravel whether there is a role for AAs in the mechanisms for skeletal muscle dysfunction in COPD, basic knowledge of AA metabolism in the muscle during exercise is important. We examined the effects of 20 min of exercise on AA metabolism in 14 patients with COPD and eight control subjects. Arterialized venous blood and a quadriceps femoris muscle biopsy were obtained before and immediately after exercise. FFM was not significantly different between the groups. In COPD, a significant reduction of most muscle AAs was present postexercise, whereas several plasma AAs were increased (p < 0.05). Consequently, sum AAs was reduced in muscle (20%; p < 0.01) and increased in plasma (16%, p < 0.05), suggesting an enhanced AA release from muscle in COPD during exercise. In the COPD group, the increase in plasma alanine and glutamine was even higher postexercise (61%, p < 0.01 and 21%, p < 0.01, respectively), suggesting enhanced nitrogen efflux. This study shows that exercise alters amino acid (intermediary) metabolism in patients with COPD and independent of the presence of FFM wasting.

Aged↗
PubMed1991

[Effect of acute carbaryl poisoning on various indicators of amino acid metabolism in rats].

Male Wistar rats were orally poisoned with carbaryl in a single dose 474 mg/kg (1/2 LD50). After 2, 4, 24, 72 and sometimes 120 hours from the administration of the insecticide the studied biochemical parameters have been determined. Trials showed an essential effect of carbaryl on the amino acid balance and metabolism. Significant decreases of the most amino acids concentrations in the brain tissue (a maximum decrease in the second hour) and in the liver (at 4-th h of intoxication). Normalization of the amino acid levels occurred more early in the brain than in the liver. Furthermore a decrease of total keto-acids concentration in erythrocytes (at 4-th h) and activity changes of some plasma and liver plasmatic aminotransferases in the reaction with alpha-ketoglutarate and pyruvate was observed.

Acute Disease↗
PubMed1994

The role of glucagon in the control of protein and amino acid metabolism in vivo.

The relative contribution of hyperglucagonemia to the mechanisms of nitrogen loss during catabolic states has not been clearly established. The present study examines the independent effect of physiologic elevations of plasma glucagon on whole-body protein kinetics, as well as on net amino acid balance across the liver and gastrointestinal tract tissues, in conscious 18-hour-fasted dogs (n = 7). Each study consisted of a 120-minute equilibration period, a 30-minute basal period, and a 150-minute experimental period. Leucine kinetics were measured using L-[1-14C]leucine. Pancreatic hormones were maintained by infusing intravenous somatostatin (0.8 micrograms/kg.min), intraportal insulin (275 microU/kg.min), and intraportal glucagon (0.65 ng/kg.min basally and 2.5 experimentally). Dextrose was infused to maintain plasma glucose constant (14.1 +/- 0.3 mumol/L), thereby providing a consistent metabolic steady state for the study of protein and amino acid metabolism. In the experimental period, plasma glucagon was fourfold basal levels (112 +/- 10 v 32 +/- 6 pg/mL), whereas plasma insulin remained stable (mean, 10 +/- 1 microU/mL). Hepatic glucose production was increased 30%, but leucine rates of appearance ([Ra] proteolysis), oxidative disappearance (Rd), and nonoxidative Rd (protein synthesis) were not altered during the experimental period. Furthermore, the net release of amino acids by the gastrointestinal tract was not increased by glucagon. However, uptake and extraction of amino acids by the liver were increased, resulting in a 17% decrease in total plasma amino acids.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acids↗
PubMed2006

Biochemical basis of specialization for dispersal vs. reproduction in a wing-polymorphic cricket: morph-specific metabolism of amino acids.

The biochemical basis of specializations for dispersal vs. reproduction is an understudied aspect of dispersal polymorphism in insects. Using a radiolabelled amino acid, we quantified differences in in vivo amino acid metabolism between morphs of the wing-polymorphic cricket, Gryllus firmus, that trade-off early age reproduction and dispersal capability. Studies were conducted in crickets fed a variety of diets expected to influence amino acid and lipid metabolism. On the day of molt to adulthood, prior to the morph-specific trade-off between ovarian growth and biochemical preparation for flight (e.g. biosynthesis of triglyceride flight fuel), morphs did not differ in any aspect of amino acid metabolism. However, on day 5 of adulthood, when the morph-specific trade-off between ovarian growth and flight fuel production was manifest, the morphs differed substantially in each of the three aspects of amino acid metabolism studied: conversion to protein, oxidation, and conversion to lipid. Morphs also differed in degree of allocation of products of amino acid metabolism to ovaries vs. the soma. Most importantly, morphs differed in the relative metabolism of radiolabelled glycine through these pathways (i.e. biochemical trade-offs), and in the relative allocation of end products of amino acid metabolism to the soma vs. ovaries (allocation trade-offs). A functionally important interaction between amino acid and lipid metabolism was noted: greater oxidation of amino acids in the flight-capable morph spared fatty acids for enhanced conversion into triglyceride flight fuel. By contrast, greater oxidation of fatty acids by the flightless morph spared amino acids for enhanced conversion into ovarian protein. Diet significantly affected amino acid metabolism. However, MORPHxDIET interactions were rare and morphs differed in amino acid metabolism to a similar degree under the range of diets tested.

Amino Acids↗
PubMed1976

Amino acid metabolism and protein synthesis in streptomycin resistant Vibrio El Tor.

Metabolic activities in relation to protein synthesis and amino acid utilization are altered in Vibrio El Tor after development of resistance towards streptomycin. Efficiency of in vivo and in vitro protein synthesis is markedly reduced in streptomycin resistant Vibrio El Tor. The rate of incorporation of 14C-amino acids into protein, uptake of 14C-valine and oxidation of certain amino acids are also altered.

Amino Acids↗
PubMed1994

Stress hormone and amino acid infusion in healthy volunteers: short-term effects on protein synthesis and amino acid metabolism in skeletal muscle.

To study the immediate effects of stress hormones and intravenous amino acid support, healthy male volunteers were administered a stress-hormone infusion including epinephrine, cortisol, and glucagon either alone (Triple, n = 8) or combined with a balanced glutamine-free amino acid solution (Triple AA, n = 8) over a period of 6 hours. The amino acid infusion was started 2 hours after the hormone infusion. A third group (AA, n = 8) received the balanced amino acid solution alone. After 6 hours of the stress-hormone infusion, a decrease was observed in skeletal muscle protein synthesis as measured by the size distribution and concentration of ribosomes. The decrease was prevented by an infusion of the balanced amino acid solution. Following the triple-hormone infusion, a decrease was noted in the content of the total free amino acids in both muscle and plasma. After including amino acids in the infusion solution, the significant decrease in muscle glutamine caused by the triple hormones was not seen. Plasma cortisol, insulin, and glucose increased in response to the triple-hormone infusion alone or in combination with amino acids. In summary, the results show that the signs of muscle protein catabolism elicited by administration of stress hormones can be attenuated by simultaneous administration of a conventional amino acid solution, although it does not contain glutamine.

Adult↗
PubMed1985

Changes in muscle and plasma amino acid metabolism in severe malnutrition--the influence of total parenteral nutrition.

The concentrations of free amino acids in muscle and plasma were determined in nine female patients with severe anorexia nervosa before and after 3 to 5 weeks of total parenteral nutrition (TPN). The patients had lost 25 to 42% of their pre-morbid weight. During TPN their weight gain was around 2.5 kg/week. Initially total non-essential amino acids (NEAA) in muscle were decreased 30% compared to controls. The major part of this depletion was due to a 40% reduction in glutamine. After TPN the level of glutamine normalized. Alanine, being normal before TPN, decreased after TPN. Proline and several other non-essential amino acids in muscle were decreased before and after TPN. Total essential amino acids (EAA) in muscle were initially normal and were not significantly affected by TPN. Total NEAA in plasma were decreased at admission and normalized after TPN. Total EAA in plasma, however, were normal both before and after TPN. This study demonstrates that severely malnourished patients with anorexia nervosa have changes in amino acid patterns in both muscle and plasma. These changes were largely, though not completely, reversed after 3 to 5 weeks of TPN.

Journal Article↗
PubMed1983

Effect of nutritional state and insulin on hind-limb amino acid metabolism in steers.

The effects of dietary protein level, exogenous insulin and starvation on amino acid (AA) uptake or release from the hindquarters of steers were studied. Irrespective of diet fed, physiologic state or time after feeding there was a net release of alanine and glutamine from hind limbs of steers. Steers from control 1 exhibited a net release of leucine, valine and isoleucine (branched-chain amino acids, BCAA) in the postabsorptive (prefeeding) state, but steers from control group 2 exhibited some BCAA uptake by the hind limb. At 2 and 4 hours postfeeding, there was marked net uptake by hind limbs of BCAA and total AA in steers fed the control (12.8% protein) diets. At 2 and 4 hours after feeding there was slight hind-limb uptake of BCAA and total AA in steers fed the low protein diet, while there was a massive uptake of BCAA and total AA by hind limbs of steers fed the high protein diet. Upon insulin injection to postabsorptive steers, BCAA and total AA uptake by hind limbs was markedly stimulated at 1 and 2 hours, but by 4 hours the AA flux pattern had reverted to that in the postabsorptive state. After 24 and 48 hours of starvation, steer hindquarters released significant quantities of BCAA, essential amino acids and total amino acids.

Amino Acids↗
PubMed1991

Effect of fasting on uteroplacental amino acid metabolism in the pregnant sheep.

In the fed state, the net utilization of most amino acids by the ovine uteroplacental unit (defined as uterine uptake minus umbilical uptake) is zero. This study was to determine if this is true for the fasted pregnant ewe also, when uteroplacental glucose uptake is diminished. Glucose and amino acid concentrations were determined in 9 pregnant ewes across the uterine and umbilical circulations. Uterine and umbilical blood flows were determined by the steady state antipyrine diffusion method, and net uptakes across each circulation calculated by application of the Fick principle. Five amino acids were found to have a consistently greater uterine uptake than umbilical uptake. In addition, glutamate had a negative net umbilical uptake coupled with no net uterine uptake. Fasting resulted in an increase in the differences between the respective uptakes for all five amino acids. No additional amino acids were found to have disparate uptakes than were seen in the fed state. Umbilical glutamate uptake became less negative during fasting, but the difference between the uterine and umbilical circulations remained unchanged, as the uterine circulation took up glutamate during fasting. The umbilical circulation took up alpha-ketoisocaproate 0.626 +/- 0.18, fed), and the uptake was increased during fasting (1.8 +/- 0.6). These findings suggest that the branched chain amino acids and glutamine are utilized by the ovine uteroplacenta to a greater degree than are most other amino acids, and at increased rates during fasting of the ewe. These amino acids, through deamination, may be the source of uteroplacental ammonia production, as well as serving as an energy substrate when glucose supply is limited.

Amino Acids↗
PubMed1990

Effects of partial hepatectomy on the enzymes of cerebral glutamate and branched-chain amino acid metabolism.

Cerebral activities of glutamate dehydrogenase (GDH), glutamine synthetase (GS), and branched-chain amino acid aminotransferase (BCAA-T) along with the levels of ammonia in serum and brain were determined in normal, sham-operated and partially hepatectomized rats. Mild hyperammonemia was observed in sham-operated animals, and the cerebral activities of all the enzymes studied were found to be decreased when compared with those of normal animals. In hepatectomized animals, blood and brain ammonia levels were elevated further. In these animals, GS activity returned to the normal values and that of BCCA-T was elevated, while there was a continued suppression of GDH activity. These results were discussed in relation to the utilization of BCAA (leucine, isoleucine, and valine) for the synthesis of glutamate and glutamine in brain in hyperammonemic states.

Amino Acids, Branched-Chain↗
PubMed1988

Influence of cold exposure on liver amino acid metabolism enzymes of the rat.

The activities of alanine, aspartate and branched-chain amino acid transaminases, glutamate dehydrogenase, glutamine synthetase and adenylate deaminase have been studied in liver of male rats exposed [12 hours at 4 degrees C] or acclimated [15 days at 4 degrees C] to cold temperature. Cold temperature induced an increase of the activities of glutamate dehydrogenase and alanine and aspartate transaminases both in cold-exposed and cold-acclimated animals; adenylate deaminase activity diminished after 15-day cold acclimation. There were not significant changes induced by cold temperature in the activities of the other two enzymes studied. These results agree with a possible direct implication of amino acid utilization by the liver in the context of the overall thermogenic response to cold temperature.

AMP Deaminase↗
PubMedDate not supplied

[Amino acid metabolism in the human placenta during its functional maturation].

The total content of free amino acids in chorion villi of the 7-40-week human placenta rises from 41 up to 71 mg%, which is mostly due to an increase in the content of replaceable amino acids. In the process of development the intensity of glutaminic acid desamination changes essentially and correlates with changes in its content in the placenta. The aspartate and alanine aminotransferase activity in the placenta during the period under study rises almost twice, that correlates with changes in the content of alanine, glutaminic and asparginic acids in the corresponding periods of development.

Alanine Transaminase↗