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PubMed1985

Control of cell-free protein synthesis by amino acids: effects on tRNA charging.

In order to resolve the observation that addition of glutamine and glutamate appears to be of particular importance in enhancing the activity of a cell-free protein synthesis system derived from rat liver (Manchester and Tyobeka, 1980), we have measured the KM of the aminoacyl-tRNA synthetases towards amino acids and the extent of aminoacylation of tRNA under the conditions of our earlier experiments. During incubation of the cell-free system in the presence of an amino acid mixture the extent of acylation to tRNA of 15 amino acids studied showed no clear change from initial time values. When incubation took place in the absence of added amino acids, however, the levels of glutamate and glutamine bound to their appropriate tRNAs dropped more rapidly and to lower levels than for other amino acids except tryptophan. The pronounced drop for these two amino acids does not seem to result from an abnormally high KM value for the synthetases towards the respective amino acids, nor an abnormally low Vmax, but probably from the fact that the amounts of glutamyl and glutaminyl-tRNA in the cell-free system are comparatively low.

Amino Acids↗

PubMed1993

Plasma amino acid response to ingestion of L-amino acids and whole protein.

The effect of whole protein and L-amino acid ingestion on plasma amino acid concentrations was investigated in 10 men. Each subject ingested equivalent amounts of amino acids as cottage cheese (session 1), an L-amino acid mixture (session 2), and cottage cheese and L-amino acids (session 3). Postprandial changes from baseline were larger for essential versus nonessential amino acids in each session. Higher and more rapid rises followed by more rapid declines in individual plasma amino acid concentrations were observed after ingestion of L-amino acids alone or with whole protein than after ingestion of an equivalent amount of amino acids as whole protein. Individuals receiving the majority of their essential amino acid and nitrogen needs from elemental products may need, for example, to consume them more frequently or after consumption of other foods in an effort to slow down absorption rates.

Administration, Oral↗

PubMed2003

Regulation of muscle protein synthesis in neonatal pigs during prolonged endotoxemia.

In adults, protein synthesis in skeletal muscle is reduced by as much as 50% after a septic challenge, and is associated with repression of translation initiation. Neonates are highly anabolic and their muscle protein synthesis rates are elevated and uniquely sensitive to amino acid and insulin stimulation. In the present study, neonatal piglets were infused with Endotoxin (lipopolysaccharide, LPS) for 20 h at 0 (n = 6) and 13 microg/kg*h (n = 8). During the last 2 h, dextrose and an amino acid mixture were infused to attain fed plasma concentrations of amino acids, glucose, and insulin. Fractional protein synthesis rates and translational control mechanisms were examined. LPS reduced protein synthesis in glycolytic muscles by only 13% and had no significant effect in oxidative muscles. This depression was associated with reductions in the phosphorylation of 4E-BP1 (-31%) and S6 K1 (-78%), and a decrease in eIF4G binding to eIF4E (-62%), an event required for formation of the active mRNA binding complex. By comparison, LPS increased protein synthesis in the liver (+29%), spleen (+32%), and kidney (+27%), and in the liver, this increase was associated with augmented eIF4G to eIF4E binding (+88%). In muscle and liver, LPS did not alter eIF2B activity, an event that regulates initiator met-tRNA(i) binding to the 40S ribosomal complex. These findings suggest that during sustained endotoxemia, the high rate of neonatal muscle protein synthesis is largely maintained in the presence of substrate supply, despite profound changes in translation initiation factors that modulate the mRNA binding step in translation initiation.

Animals↗

PubMed1978

Limiting amino acids for milk protein synthesis by bovine mammary cells in culture.

Experiments are presented to determine the effect of labeled precursor amino acid on synthesis of beta-lactoglobulin and beta-casein and to identify the most limiting amino acids in Eagle's minimal essential medium for synthesis of milk protein. Protein synthesis was measured by incorporation of carbon-14 labeled amino acids into milk protein from bovine mammary cell culture. Mammary tissue from 13 Holsteins (12.7 kg milk/day) was dispersed and cultured for 18 h. In Experiment 1, three replications (cows) with three amino acid mixtures, utilizing labeled lysine or leucine as the marker amino acid, showed that labeled lysine overestimated the effect of medium lysine, and labeled leucine overstimated the effect of leucine on beta-lactoglobulin and beta-casein synthesis. Subsequently Experiment 2 utilized 10 replications (cows) to determine the effect of a three-fold increase of each of 13 amino acids in Eagle's medium. Increased threonine or methionine improved beta-lactoglobulin synthesis and cystine increased beta-casein. Second and third best response in beta-casein were from addition of methionine and threonine. Combined analysis from 10 cows and two protein responses by multivariate procedures identified, in order of decreasing magnitude, cystine, threonine, and methionine as limiting amino acids in the dispersed cell culture.

Amino Acids↗

PubMed2001

Antiapoptotic effects of the peptidergic drug cerebrolysin on primary cultures of embryonic chick cortical neurons.

Cerebrolysin (EBEWE Arzneimittel, Austria, Europe) is a widely used drug relieving the symptoms of a variety of neurological disorders, particularly of neurodegenerative dementia of the Alzheimer's type. It consists of approximately 25% of low molecular weight peptides (<10k DA) and a mixture of approximately 75% free amino acids, this being based on the total nitrogen content. In this study we used a low serum (2% serum supplement) cell stress in-vitro model to assess drug effectiveness on neuronal viability and programmed cell death (PCD). In this in-vitro model the type of cell death was previously shown to be primarly apoptotic, which was verified by DNA-laddering and TUNEL-staining. For evaluation of neuronal viability a MTT-reduction assay was performed after 4 DIV and 8 DIV and the percentage of apoptotic neurons was determined by bis-benzimide staining of nuclear chromatin. To differentiate between possible effects of the free amino acids and the peptide fraction of Cerebrolysin an artificial amino acid mixture (AA-mix) was used as a control. Cerebrolysin, the AA-mix and 10% foetal calf serum (FCS) caused a similar increase in viability after 4 DIV, whereas the effects of the growth factors BDNF and FGF-2 were less pronounced. After 8 DIV Cerebrolysin, but not the AA-mix, was able to ameliorate neuronal viability, which could reflect a neuro-protective effect or an increased activity of the mitochondrial dehydrogenase measured in a MTT-reduction assay. The percentage of cells showing apoptotic chromatin changes was significantly reduced (p < 0.01) in cultures treated with Cerebrolysin, whereas the AA-mix failed to decrease the percentage of cells showing apoptotic chromatin changes. These findings ascertain an anti-apoptotic effect of the peptide fraction of Cerebrolysin and reveal a transient viability promoting effect of the amino acid fraction, which is most likely due to improved nutritional supply.

Amino Acids↗

PubMed2000

Quantitative electrospray ionization mass spectrometric studies of ternary complexes of amino acids with Cu(2+) and phenanthroline.

Electrospray ionization (ESI) mass spectra of ternary complexes of Cu(2+) and 1,10-phenanthroline with the 20 essential amino acids (AA) were investigated quantitatively. Non-basic amino acids formed singly charged complexes of the [Cu(AA - H)phen](+) type. Lysine (Lys) and arginine (Arg) formed doubly charged complexes of the [Cu(HAA - H)phen](2+) type. Detection limits were determined for the complexes of phenylalanine (Phe), glutamic acid (Glu) and Arg, which were at low micromolar or submicromolar concentrations under routine conditions. Detection limits of low nanomolar concentrations are possible for amino acids with hydrophobic side-chains (Phe, Tyr, Trp, Leu, Ile) as determined for Phe. The efficiencies for the formation by ESI of gaseous [Cu(AA - H)phen](+) ions were determined and correlated with the acid-base properties of the amino acids, ternary complex stability constants and amino acid hydrophobicities expressed as the Bull-Breese indices (DeltaF). A weak correlation was found between DeltaF and the ESI efficiencies for the formation of gaseous [Cu(AA - H)phen](+) [Cu(HAA - H]phen](2+) and [AA + H](+) ions that showed that amino acids with hydrophobic side-chains were ionized more efficiently. In the ESI of binary and ternary amino acid mixtures, the formation of gas-phase Cu-phen complexes of amino acids with hydrophobic side-chains was enhanced in the presence of complexes of amino acids with polar or basic side-chains. An interesting enhancement of the ESI formation of [Cu(Glu - H)phen](+) was observed in mixtures. The effect is explained by ion-cluster formation at the droplet interface that results in enhanced desorption of the glutamic acid complex.

Amino Acids↗

PubMed2000

Isoleucine imbalance using selected mixtures of imbalancing amino acids in diets of the broiler chick.

Three experiments were conducted to determine the isoleucine requirement of a broiler from the time of hatch to 16 d of age. Chicks in the experiments were fed an isoleucine-limiting diet composed of wheat and peanut meal as the primary protein sources; this diet was used to investigate various mixtures of amino acids as imbalancing agents for isoleucine. The isoleucine requirement for maximum weight gain and feed efficiency was determined on the basis of broken-line regression analysis to be 0.63 to 0.65% of the diet or 3.28 to 3.38% of dietary protein. A similar diet, marginally limiting in isoleucine, was used to investigate the response of chicks to the addition of various mixtures of amino acids to the diet. Chicks that received a 5% dietary addition of 11 amino acids consisting of equimolar concentrations of leucine, valine, histidine, methionine, phenylalanine, tryptophan, tyrosine, alanine, glycine, serine, and threonine had significantly lower weight gain and feed consumption and a higher feed conversion ratio than did chicks fed the basal diet. These adverse effects were only partly prevented by an isoleucine supplement. The large neutral amino acids, histidine, methionine, phenylalanine, tryptophan, and tyrosine, accounted for most of the effect of the mixture. No effect of a mixture of leucine and valine or a mixture of the small neutral amino acids (alanine, glycine, serine, and threonine) at the same concentrations as those in the mixture of the 11 amino acids was observed. Lysine and arginine were the only two indispensable amino acids not present in the mixture of 11 amino acids. A subsequent experiment demonstrated that these amino acids did not become co-limiting with isoleucine when the diet was imbalanced with the amino acid mixture. These results indicate that an isoleucine imbalance in chicks is readily precipitated by excessive dietary concentrations of large neutral amino acids in diets that are otherwise marginally adequate in isoleucine.

Aging↗

PubMed1987

Effect of peptide chain length on absorption of egg protein hydrolysates in the normal human jejunum.

The influence of the peptide chain length of partial enzymic hydrolysates of protein on nitrogen and amino acid absorption was studied in 12 subjects using a jejunal perfusion technique. Three hydrolysates of egg white and an equivalent amino acid mixture were perfused at 30 mmol/L and 100 mmol/L in two separate experiments. Two hydrolysates (OH1 and OH2) contained mainly dipeptides and tripeptides, whereas the third (OH3) comprised tripeptide to pentapeptides as judged chromatographically. Nitrogen absorption was significantly slower from the higher chain length mixture, OH3, than from the short chain mixtures, OH1 and OH2, at both concentrations. Similarly, several amino acid residues were absorbed less well from OH3 than from OH1 and OH2. These data demonstrate that the chain length of heterogeneous mixtures of peptides affects absorption of nitrogen and individual amino acid residues, and suggest that brush border hydrolysis of tetrapeptides and pentapeptides limits absorption from enzymic hydrolysates of protein which simulate the composition of the postprandial luminal contents.

Amino Acids↗

PubMed1998

Effects of tryptophan depletion in drug-free depressed patients who responded to total sleep deprivation.

BACKGROUND: There is some evidence that sleep deprivation (SD) might exert its antidepressant properties by involving serotonergic mechanisms. We investigated the effects of short-term tryptophan depletion (TD) on depressed patients who responded to a single night of total SD. METHODS: Drug-free depressed inpatients (n = 30) were randomly assigned to either TD or sham depletion. Tryptophan depletion was induced by a 24-hour low-tryptophan diet (day 1) followed the next morning by ingestion of a tryptophan-free amino acid mixture (day 2). During sham depletion, the diet and the amino acid beverage were supplemented with tryptophan. Sleep deprivation was performed from day 1 until day 2. Only SD responders received the amino acid beverage the morning after SD. Behavioral ratings and total and free plasma tryptophan levels were obtained before and after the test sessions. RESULTS: Twenty-two of 30 patients showed a favorable outcome after SD. As predicted, TD significantly lowered total and free plasma tryptophan levels, whereas both levels increased during sham depletion. No acute effects on mood were observed during the day after SD in either treatment group. Unexpectedly, TD, but not control testing, prevented the depressive relapse after the recovery night in most of the patients. CONCLUSIONS: Tryptophan depletion did not reverse the antidepressant effects of SD, but it prevented the relapse beyond a night of recovery sleep. These findings suggest that SD does not act via a single monoamine-related mechanism, but they allow the assumption that TD may induce neurochemical alterations that transiently improve depression.

Adult↗

PubMed2006

Miniaturized liquid core waveguide-based fluorimetric detection cell for capillary separation methods: application in CE of amino acids.

A miniaturized post-column fluorimetric detection cell for capillary separation methods based on optical fibers and liquid core waveguides (LCWs) is described. The main part of the detection cell is a fused-silica capillary coated with Teflon AF serving as an LCW. The optical fibers are used both for coupling the excitation source with the detection domain in the LCW and for the axial fluorescence collection from the LCW end. The latter fiber is connected with a compact CCD spectrometer that serves for the rejection of the scattered excitation light and for the fluorescence signal detection. The proposed design offers a compact fluorescence detector for various microcolumn separation techniques without optical elements such as filters or objectives. Moreover, its construction and optical adjustment are very simple and the whole system is highly miniaturized. The function of the detection cell is demonstrated by CE of amino acids labelled by fluorescein-based tags. Separations of different standard amino acid mixtures and plasma samples are presented. The comparison of plasma amino acid levels of individuals being in good health with those of patients with inherited metabolic disorders is also shown.

Amino Acids↗

PubMed2004

The effects of oral amino acid intake on ambulatory capacity in elderly subjects.

BACKGROUND AND AIMS: The combination of high prevalence of inactivity in the older population, and high risk of ill-health and disability associated with inactivity, suggests that interventions that are successful in increasing levels of activity may have a great impact on population health in later life. With advancing age, the risk of developing serious nutritional deficiencies also increases. This study was designed to assess the effects of dietary amino acid supplementation on effort tolerance in healthy elderly subjects with reduced physical activity. METHODS: Forty-four subjects (age > 65 years) with sedentary life-style and lower health-related quality of life were studied. Subjects, in an open-label fashion, received an oral amino acid mixture (AAM, 12 g/day) containing essential and non-essential amino acids for a 3-month period. Ambulatory dysfunction resulting in sedentary life-style was assessed by a 6-min walk test. A walking impairment questionnaire (WIQ) was used to evaluate self-perceived ambulatory dysfunction. Maximal isometric muscular strength of the right hand was measured during isometric exercise by a handgrip dynamometer. RESULTS: The 6-min walk distance increased from 214.5 +/- 32 to 262.8 +/- 34.8 m (p < 0.001) after AAM treatment. The baseline scores on the three subscales of WIQ changed significantly during treatment: WIQ distance increased from 56.2 +/- 12.9 to 66.3 +/- 12.8% (p < 0.001); WIQ speed from 52 +/- 12.6 to 69.2 +/- 14.8% (p < 0.001) and WIQ stairs from 74.4 +/- 22.6 to 94.2 +/- 25% (p < 0.001), as did maximal isometric muscular strength (16.6 +/- 2.4 vs 19.2 +/- 2.2 kg, p < 0.001). Changes in plasma glucose (+11 +/- 11 mg/dL), total cholesterol (0 +/- 39 mg/dL), HDL cholesterol (0 +/- 17 mg/dL), and triglycerides (-11 +/- 58 mg/dL) were not significant between baseline and AAM. CONCLUSIONS: An oral amino acid supplement, as used in this pilot study, improves ambulatory capacity and maximal isometric muscle strength in elderly subjects without affecting the main metabolic parameters. Amino acid supplementation may thus represent useful non-pharmacological intervention to maintain physical fitness in these subjects.

Administration, Oral↗

PubMed2001

A fast and sensitive method for measuring picomole levels of total free amino acids in very small amounts of biological tissues.

In the present study we describe a simple and fast method to measure the concentration of total free amino acids in very small amounts of biological tissues. The procedure described here is based on the reaction of free amino acids with o-phthaldialdehyde (OPA) in the presence of a reducing agent, beta-mercaptoethanol (MET), to give a complex which can be measured by fluorescence. It is a very rapid process and has the same reliability as the conventional ninhydrin method of Moore and Stein but is about 500 times more sensitive. The sensitivity of the new protocol is such to permit the determination with high reliability of very small amounts of free amino acids at picomole levels, either in a standard amino acid mixture or in biological tissues, without chromatographic separation of the amino acids. It is particularly useful when the amount of the sample is very low, e.g. on a single pituitary or pineal gland of small animals or on single cells, such as oocytes or eggs, as well as single ganglions or axons of marine invertebrates.

Amino Acids↗

PubMed1985

A comparison of internal and external standardization in amino acid analysis.

To assess quantitatively the merits of internal standardization, an amino acid mixture of known composition has been analyzed by conventional automated amino acid analysis before and after being subjected to total acid hydrolysis. Both the precision (reproducibility) and the accuracy (lack of bias) were generally, but not invariably, greatly enhanced by the use of internal standardization with norleucine as opposed to external standardization. Incorporation of internal standards into samples is strongly recommended.

Amino Acids↗

PubMed1982

Effects of amino acid alterations caused by protein synthesis inhibitors on brain monoamine formation.

Cerebral amino acid concentrations in mice were determined following in vivo treatment with cycloheximide and anisomycin. Synaptosomes from untreated mice were then exposed to concentrations of amino acids designed to simulate the conditions existing extraneuronally following in vivo drug treatment. The synthesis of [3H]norepinephrine, [3H]dopamine and [3H]5-hydroxytryptamine from their labelled amino acid precursors was determined, as well as the accumulation of the precursors by the synaptosomes. Although the synthesis of both [3H]dopamine and [3H]norepinephrine was decreased below expected values predicted from samples in which only tyrosine was altered to represent the concentrations following drug treatment, it was not decreased significantly below control levels. Synthesis of [3H]5-hydroxytryptamine was increased in the presence of amino acid mixtures simulating drug treatment. The results suggest that alteration of amino acid levels is not involved in the inhibition of brain monoamine synthesis caused by these protein synthesis inhibitors.

Amino Acids↗

PubMed1985

Nitrogen balance studies in aging rats.

Nitrogen balance studies were conducted to compare the protein requirements of aged (24-month-old) and mature (12-month-old) rats for possible age-related differences. Four diets with protein supplied as amino acid mixtures simulating casein protein at 4.5%, 4.5% plus 1.5% indispensable amino acids of casein, 4.5% plus 1.5% dispensable amino acids of casein or 6.0% casein protein were offered for one week each during a four-week counter-balanced dietary sequence. Lower food and nitrogen intake of aged rats resulted in a lower mean nitrogen balance compared to that of the mature animals. Calculations of the level of N intake necessary to provide for N equilibrium in the aged rats indicated an apparent increase in the actual net need for nitrogen and indispensable amino acids when compared with the needs of the mature animals.

Age Factors↗

PubMed1994

Tumour and host tissue responses to branched-chain amino acid supplementation of patients with cancer.

1. Rates of protein synthesis have been measured from the incorporation of 57 mg of L-[1-13C]leucine/kg for 90 min into muscle tissue and colorectal tumours removed at surgery from cancer patients. 2. For the 20 h preceding surgery and during the measurement of protein synthesis, the patients received intravenous saline, conventional intravenous nutrition (0.2 g of N and 103 non-protein kJ/kg body weight) or intravenous nutrition enriched with the branched-chain amino acids leucine, isoleucine and valine (0.2 g of N with 30% from branched-chain amino acids and 103 non-protein kJ/kg body weight). 3. Conventional intravenous nutrition resulted in a significant stimulation of the rate of protein synthesis in both muscle tissue (2.64 +/- 0.75%/day versus 1.78 +/- 0.51%/day in saline control, means +/- SD) and tumour tissue (43.9 +/- 10.3%/day versus 22.6 +/- 5.6%/day in saline control). 4. Pre-operative nutrition enriched with branched-chain amino acids was less effective than conventional intravenous nutrition in stimulating protein synthesis in both muscle and tumour. The rates of protein synthesis were 2.12 +/- 0.41%/day in muscle and 33.7 +/- 5.3%/day in the tumours. 5. The expression of proliferating cell nuclear antigen in sections of the tumours showed changes with intravenous feeding of the two different amino acid mixtures that were similar to the changes in protein synthesis, and these two variables were significantly correlated. This is evidence that feeding with conventional mixtures and mixtures enriched with branched-chain amino acids stimulates tumour growth.(ABSTRACT TRUNCATED AT 250 WORDS)

Aged↗

PubMed1986

Conditional deficiencies of ornithine or arginine.

Relative deficiencies of ornithine or arginine occur in the presence of excessive ammonia, excessive lysine, growth, pregnancy, trauma, or protein deficiency and malnutrition. Ammonia excess may occur in the presence of a normal liver when amino acid mixtures lacking ornithine, arginine, or citrulline are infused; when specific amino acids such as glycine are injected; when ammonium salts, urea, or urease are injected; or when the gastrointestinal tract contains an excess of protein, urea, or NH4+, as occurs after a gastrointestinal hemorrhage. In these states, ornithine is often rate-limiting for urea cycle function. Ornithine is also rate-limiting when ammonia excess occurs in the presence of hepatic failure. In three of the inherited urea cycle disorders, ornithine insufficiency and ammonia excess also occur. These disorders are citrullinemia, argininosuccinic aciduria, and argininemia. In the presence of excessive lysine the availability of arginine is reduced and the formation of ornithine is decreased in the liver; urea synthesis is reduced, but orotic acid synthesis is increased, and orotic aciduria results as carbamyl phosphate is directed toward the pyrimidine pathway. Hereditary lysinuric protein intolerance results in ornithine depletion, hyperammonemia, and orotic acid uria. Optimal growth in several species of animals requires 0.4-1.0% arginine in the diet. Diets deficient in arginine are associated with poor wound healing as well as stunted growth. The measurement of orotic acid excretion has been a convenient indicator of insufficiency of ornithine or arginine during growth or pregnancy in animals and should prove useful in assessing the requirement for arginine after trauma. Normal human pregnancy is associated with low-grade orotic aciduria. Protein deficiency and malnutrition increase the vulnerability of the animal or child to ammonia toxicity. This is presumably due to insufficient ornithine for normal urea cycle responsiveness.

Amino Acids↗

PubMed1964

Use of thymineless death to enrich for doubly auxotrophic mutants of Bacillus megaterium.

Wachsman, J. T. (University of Illinois, Urbana), and L. Hogg. Use of thymineless death to enrich for doubly auxotrophic mutants of Bacillus megaterium. J. Bacteriol. 87:1118-1122. 1964.-When strain KM:T(-), a thymine auxotroph of Bacillus megaterium strain KM, is allowed to undergo thymineless death on a minimal medium, the survivors are greatly enriched in polyauxotrophic mutants. Cells were irradiated with ultraviolet light, grown in the presence of thymidine and a complete amino acid mixture, and then starved for thymidine in the absence of amino acids. Doubly auxotrophic mutants (thymine(-) amino acid(-)) may account for more than 90% of the survivors. The most reproducible results were obtained when sucrose (0.4 m) was added to both growth and starvation media. Although the percentage of mutants among the survivors increases with the time of thymine starvation, the absolute number of double auxotrophs per milliliter decreases. It is probable that the extent of cross-feeding determines both the mutant yield and the mutants types. Substrains of KM:T(-) having additional requirements for each of the following amino acids have been isolated: histidine, threonine, tyrosine, tryptophan, arginine, isoleucine, methionine, serine, and cysteine.

Amino Acids↗