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PubMed1994

Emerging aspects of amino acid metabolism. Where do we go from here?

The mechanisms are discussed by which the body maintains nitrogen balance and constancy of the amount and pattern of body proteins. A distinction is made between effectors, such as hormones, and regulators. Free amino acid concentrations, which are maintained remarkably constant, may play an important role. The key step in the regulation of urea production could be the stimulation of acetyl glutamate synthesis by amino acids entering the liver from the portal tract and the consequent activation of carbamoyl-phosphate synthetase I. Both protein synthesis and breakdown are regulated to some extent by amino acid supply. It is probable that the effects of diet are exerted mainly on the turnover of visceral proteins. Evidence is presented for the existence of a substantial pool of protein that turns over by lifetime kinetics. Such a pool could complicate the interpretation of data obtained in kinetic studies.

Amino Acids↗
PubMed1984

Changes in ovine fetal hindlimb amino acid metabolism during maternal fasting.

The flux of various substrates across the ovine fetal and maternal hindlimbs was measured in the fed state and after 5 days of maternal fasting. Whole blood concentrations of glucose, oxygen, ammonia, and six amino acids (glutamate, glutamine, alanine, valine, isoleucine, and leucine) were determined in the fetal and maternal femoral artery and distal inferior vena cava in 15 chronic animal preparations. During fasting the fetal arterial glucose concentration fell by 40% (from 0.828 to 0.494 mM), and the arteriovenous concentration difference decreased by 30% (from 0.148 to 0.099 mM). Similar changes were noted in maternal blood. Fetal oxygen concentrations remained similar between the fed and fasted state, and the fetal arteriovenous oxygen concentration difference increased slightly from 0.861 to 1.02 mM. The glucose oxygen quotient decreased in the fetus from 1.20 to 0.621. In addition, significant changes occurred in the net balance of several amino acids during the fasted state. Both alanine and glutamine, which demonstrated a positive uptake by the fetal hindlimb during the fed state, showed a substantial efflux from the fetal hindlimb during the fasting period. The fetal arteriovenous concentration difference of the branched-chain amino acids (leucine, isoleucine, and valine) increased significantly during fasting. These observations are consistent with the hypothesis that the ovine fetus adapts to a diminished supply of glucose from the mother by enhanced amino acid catabolism and, possibly, proteolysis with subsequent release of gluconeogenic precursors in the form of alanine and glutamine.

Amino Acids↗
PubMed1988

Carbohydrate and Amino Acid Metabolism in the Ectomycorrhizal Ascomycete Sphaerosporella brunnea during Glucose Utilization : A C NMR Study.

Nuclear magnetic resonance spectroscopy was utilized to study the metabolism of [1-(13)C]glucose in mycelia of the ectomycorrhizal ascomycete Sphaerosporella brunnea. The main purpose was to assess the biochemical pathways for the assimilation of glucose and to identify the compounds accumulated during glucose assimilation. The majority of the (13)C label was incorporated into mannitol, while glycogen, trehalose and free amino acids were labeled to a much lesser extent. The high enrichment of the C1/C6 position of mannitol indicated that the polyol was formed via a direct route from absorbed glucose. Randomization of the (13)C label was observed to occur in glucose and trehalose leading to the accumulation of [1,6-(13)C]trehalose and [1,6-(13)C]glucose. This suggests that the majority of the glucose carbon used to form trehalose was cycled through the metabolically active mannitol pool. The proportion of label entering the free amino acids represented 38% of the soluble (13)C after 6 hours of continuous glucose labeling. Therefore, amino acid biosynthesis is an important sink of assimilated carbon. Carbon-13 was incorporated into [3-(13)C]alanine and [2-(13)C]-, [3-(13)C]-, and [4-(13)C]glutamate and glutamine. From the analysis of the intramolecular (13)C enrichment of these amino acids, it is concluded that [3-(13)C]pyruvate, arising from [1-(13)C]glucose catabolism, was used by alanine aminotransferase, pyruvate dehydrogenase, and pyruvate carboxylase (or phosphoenolpyruvate carboxykinase). Intramolecular (13)C labeling patterns of glutamate and glutamine were similar and are consistent with the operation of the Krebs cycle. There is strong evidence for (a) randomization of the label on C2 and C3 positions of oxaloacetate via malate dehydrogenase and fumarase, and (b) the dual biosynthetic and respiratory role of the citrate synthase, aconitase, and isocitrate dehydrogenase reactions. The high flux of carbon through the carboxylation (presumably pyruvate carboxylase) step indicates that CO(2) fixation is an important component of the carbon metabolism in S. brunnea, and it is likely that this anaplerotic role is particularly prevalent during NH(4) (+) assimilation. The most relevant information resulting from this investigation is (a) the occurrence of the mannitol cycle, (b) a large part of the trehalose pool is synthesized after the cycling of glucose-carbon through the mannitol cycle, and (c) pyruvate (or phosphoenolpyruvate) carboxylation plays an important role in the primary metabolism of glucose-fed mycelia.

Journal Article↗
PubMed2006

Use of stable isotopes to assess protein and amino acid metabolism in children and adolescents: a brief review.

As protein accretion is a prerequisite for growth, studying the mechanisms by which nutrients and hormones promote protein gain is of the utmost relevance to paediatric endocrinology. Tracers are ideally suited for the assessment of protein and amino acid kinetics in vivo, as they provide an estimate of synthesis and turnover. Current tracer approaches in children and adolescents utilize stable isotopes, 'heavier' forms of elements that have one or several extra neutrons in the nucleus. Such isotopes are already present at low, but significant, levels in all tissues and foodstuffs, are not radioactive and are devoid of any known side-effects when present in small amounts. L-[1-(13)C] labelled leucine, given as a 4- to 6-h intravenous infusion, has become the method of choice to assess whole-body protein kinetics. After infusion, any 13C-leucine that is oxidized appears in the breath as 13CO2, whereas the remainder is incorporated into body proteins through protein synthesis. The isotope enrichments are determined by isotope ratio mass spectrometry and gas chromatography mass spectrometry, and absolute rates of whole-body protein synthesis, oxidation, and breakdown can be extrapolated. This approach has been used extensively to investigate the regulation of protein kinetics by nutrients and by hormones. Attempts have also been made to measure amino acid/protein metabolism in selected body compartments, and to measure the kinetics of specific tissue proteins, for example, muscle, gut, or plasma proteins.

Adolescent↗
PubMed2005

Allosteric mechanisms in ACT domain containing enzymes involved in amino acid metabolism.

An important sequence motif identified by sequence analysis is shared by the ACT domain family, which has been found in a number of diverse proteins. Most of the proteins containing the ACT domain seem to be involved in amino acid and purine synthesis and are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. Here we explore the current understanding of the ACT domain function including its role as an allosteric module in a selected group of enzymes. We will further describe in more detail three of the proteins where some understanding is available on function and structure: i) the archetypical ACT domain protein E. coli 3PGDH, which catalyzes the first step in the biosynthesis of L-Ser, ii) the bifunctional chorismate mutase/prephenate dehydratase (P-protein) from E. coli, which catalyzes the first two steps in the biosynthesis of L-Phe, and iii) the mammalian aromatic amino acid hydroxylases, with special emphasis on phenylalanine hydroxylase, which catalyzes the first step in the catabolic degradation of L-phenylalanine (L-Phe). The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of 3PGDH and P-protein, respectively. On the other hand, for PAH, and probably for other enzymes, this domain appears to have been incorporated as a handy, flexible small module with the potential to provide allosteric regulation via transmission of finely tuned conformational changes, not necessarily initiated by regulatory ligand binding at the domain itself.

Allosteric Regulation↗
PubMed1981

Amino acid metabolism of Malassezia furfur.

The mechanism responsible for the hypopigmentation which follows pityriasis versicolor (P.V.) infection has not yet been satisfactorily explained. This work was done in order to study the effect of Malassezia furfur on the decomposition or the utilization of the amino acid tyrosine in vitro. No effect could be noted, which points to the assumption that the effect of the causative fungus of P.V. on melanogenesis is most probably due to the blocking of melanine synthesis by one of the product of M. furfur metabolism without using tyrosine.

Culture Media↗
PubMedDate not supplied

Relative influence of glucose and insulin on peripheral amino acid metabolism in severely burned patients.

BACKGROUND: Protein catabolism and glucose intolerance are prominent in critically injured patients. The objective of this study was to assess if glucose or insulin availability influences the extent of protein catabolism in hypermetabolic patients. METHODS: Amino acid net balance from the leg was quantitated in 6 severe burn victims. Furthermore, whole body and leg protein kinetics were assessed with 2H5 phenylalanine and 15N alanine. Measurements were obtained after a 9-hour fast, during an IV glucose infusion (30 micromol/kg per minute), and during a hyperinsulinemic (500 mIU/kg per minute) euglycemic clamp. RESULTS: Compared with fasting values, the administration of glucose resulted in a significantly increased efflux of amino acids from the leg. In contrast, insulin administration significantly decreased the cumulative net efflux of amino acids. During hyperinsulinemia, isotopic measurements demonstrated a significant decrease in alanine appearance and an increase in phenylalanine disappearance into the leg. CONCLUSIONS: These findings demonstrate that in critically injured patients, acute hyperglycemia increases muscle catabolism despite an endogenous insulin response. In contrast, exogenous insulin given in sufficient amount impedes muscle protein loss. The mechanism for this anabolic effect of insulin may vary between different amino acids.

Adult↗
PubMed2000

Renal amino acid metabolism during endotoxemia in the rat.

BACKGROUND: The kidney has an important function in the exchange of nitrogenous metabolites. Glutamine is the most important substrate for renal ammoniagenesis and thus plays a crucial role in acid-base homeostasis. Furthermore, the kidney is the main endogenous source for de novo arginine production from citrulline, which in turn is derived from intestinal glutamine metabolism. Sepsis is a condition in which glutamine availability is reduced, whereas the need for arginine biosynthesis may be increased. Limited bioavailability of glutamine may affect arginine synthesis, which may have consequences for nitric oxide (NO) synthesis. Therefore, we studied renal glutamine and arginine metabolism in a rat model of endotoxemia and related this to NO metabolism. MATERIALS AND METHODS: Rats were subject to double hit endotoxemia, and control rats received 0.9% NaCl. Renal blood flow was measured using para-aminohippuric acid. Concentrations of plasma amino acids and nitrate were measured in the aorta and renal vein to calculate net renal uptake or release of amino acids and address NO production. RESULTS: The arterial concentrations of glutamine and ammonia were not changed in endotoxemic rats. Although renal glutamine uptake was reduced, total renal ammonia production was not changed during endotoxemia. The arterial concentration of citrulline and renal citrulline uptake was not altered in endotoxin-treated rats, but renal arginine production was increased. However, no effect was observed on nitric oxide production. CONCLUSIONS: Although the kidney has very important functions in the excretion of waste products and in interorgan metabolism, this study suggests that the kidney has a limited role in glutamine, arginine, and NO metabolism during late endotoxemia in rats.

Amino Acids↗