scholarly journals Amino acid homeostasis and signalling in mammalian cells and organisms

2017 ◽  
Vol 474 (12) ◽  
pp. 1935-1963 ◽  
Author(s):  
Stefan Bröer ◽  
Angelika Bröer
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Food Intake ◽  
Essential Amino Acids ◽  
Acid Oxidation ◽  
Plasma Amino Acids ◽  
Amino Acid Oxidation ◽  
Amino Acid Levels ◽  
Amino Acid Depletion

Cells have a constant turnover of proteins that recycle most amino acids over time. Net loss is mainly due to amino acid oxidation. Homeostasis is achieved through exchange of essential amino acids with non-essential amino acids and the transfer of amino groups from oxidised amino acids to amino acid biosynthesis. This homeostatic condition is maintained through an active mTORC1 complex. Under amino acid depletion, mTORC1 is inactivated. This increases the breakdown of cellular proteins through autophagy and reduces protein biosynthesis. The general control non-derepressable 2/ATF4 pathway may be activated in addition, resulting in transcription of genes involved in amino acid transport and biosynthesis of non-essential amino acids. Metabolism is autoregulated to minimise oxidation of amino acids. Systemic amino acid levels are also tightly regulated. Food intake briefly increases plasma amino acid levels, which stimulates insulin release and mTOR-dependent protein synthesis in muscle. Excess amino acids are oxidised, resulting in increased urea production. Short-term fasting does not result in depletion of plasma amino acids due to reduced protein synthesis and the onset of autophagy. Owing to the fact that half of all amino acids are essential, reduction in protein synthesis and amino acid oxidation are the only two measures to reduce amino acid demand. Long-term malnutrition causes depletion of plasma amino acids. The CNS appears to generate a protein-specific response upon amino acid depletion, resulting in avoidance of an inadequate diet. High protein levels, in contrast, contribute together with other nutrients to a reduction in food intake.

Food Intake Regulation: Amino Acid Toxicity and Changes in Rat Brain and Plasma Amino Acids

1973 ◽  
Vol 103 (4) ◽  
pp. 608-617 ◽  
Author(s):  
Y. Peng ◽  
J. Gubin ◽  
A. E. Harper ◽  
M. G. Vavich ◽  
A. R. Kemmerer
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Food Intake ◽  
Rat Brain ◽  
Plasma Amino Acids ◽  
Food Intake Regulation ◽  
Acid Toxicity ◽  
Intake Regulation

Target of Rapamycin drives unequal responses to essential amino acid depletion in egg laying

2021 ◽  
Author(s):  
André Nogueira Alves ◽  
Carla M Sgrò ◽  
Matthew D Piper ◽  
Christen K Mirth
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Egg Production ◽  
Essential Amino Acids ◽  
Egg Laying ◽  
Drop Out ◽  
Single Amino Acid ◽  
Amino Acid Depletion ◽  
Holidic Diet ◽  
Related Trait

Nutrition shapes a broad range of life history traits, ultimately impacting animal fitness. A key fitness-related trait, female fecundity is well known to change as a function of diet. In particular, the availability of dietary protein is one of the main drivers of egg production, and in the absence of essential amino acids egg laying declines. However, it is unclear whether all essential amino acids have the same impact on phenotypes like fecundity. Using a holidic diet, we fed adult female D. melanogaster diets that contain all necessary nutrients except one of the 10 essential amino acids and assessed the effects on egg production. For most essential amino acids, depleting a single amino acid induced as rapid a decline in egg production as when there were no amino acids in the diet. However, when either methionine or histidine were excluded from the diet, egg production declined more slowly. Next, we tested whether GCN2 and TOR were involved in this difference in response across amino acids. While mutations in GCN2 did not eliminate the differences in the rates of decline in egg laying among amino acid drop-out diets, we found that inhibiting TOR signalling caused egg laying to decline rapidly for all drop-out diets. TOR signalling does this by regulating the yolk-forming stages of egg chamber development. Our results suggest that amino acids differ in their ability to induce signalling via the TOR pathway. This is important because if phenotypes differ in sensitivity to individual amino acids, this generates the potential for mismatches between the output of a pathway and the animal's true nutritional status.

Quantitative analysis of amino acid oxidation and related gluconeogenesis in humans

1992 ◽  
Vol 72 (2) ◽  
pp. 419-448 ◽  
Author(s):  
R. L. Jungas ◽  
M. L. Halperin ◽  
J. T. Brosnan
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Urea Cycle ◽  
Liver Mitochondria ◽  
Carbon Flow ◽  
Acid Oxidation ◽  
Peripheral Tissues ◽  
Amino Acid Oxidation ◽  
Atp Production ◽  
Acid Load

Significant gaps remain in our knowledge of the pathways of amino acid catabolism in humans. Further quantitative data describing amino acid metabolism in the kidney are especially needed as are further details concerning the pathways utilized for certain amino acids in liver. Sufficient data do exist to allow a broad picture of the overall process of amino acid oxidation to be developed along with approximate quantitative assessments of the role played by liver, muscle, kidney, and small intestine. Our analysis indicates that amino acids are the major fuel of liver, i.e., their oxidative conversion to glucose accounts for about one-half of the daily oxygen consumption of the liver, and no other fuel contributes nearly so importantly. The daily supply of amino acids provided in the diet cannot be totally oxidized to CO2 in the liver because such a process would provide far more ATP than the liver could utilize. Instead, most amino acids are oxidatively converted to glucose. This results in an overall ATP production during amino acid oxidation very nearly equal to the ATP required to convert amino acid carbon to glucose. Thus gluconeogenesis occurs without either a need for ATP from other fuels or an excessive ATP production that could limit the maximal rate of the process. The net effect of the oxidation of amino acids to glucose in the liver is to make nearly two-thirds of the total energy available from the oxidation of amino acids accessible to peripheral tissues, without necessitating that peripheral tissues synthesize the complex array of enzymes needed to support direct amino acid oxidation. As a balanced mixture of amino acids is oxidized in the liver, nearly all carbon from glucogenic amino acids flows into the mitochondrial aspartate pool and is actively transported out of the mitochondria via the aspartate-glutamate antiport linked to proton entry. In the cytoplasm the aspartate is converted to fumarate utilizing urea cycle enzymes; the fumarate flows via oxaloacetate to PEP and on to glucose. Thus carbon flow through the urea cycle is normally interlinked with gluconeogenic carbon flow because these metabolic pathways share a common step. Liver mitochondria experience a severe nonvolatile acid load during amino acid oxidation. It is suggested that this acid load is alleviated mainly by the respiratory chain proton pump in a form of uncoupled respiration.(ABSTRACT TRUNCATED AT 400 WORDS)

scholarly journals Radiometric studies on the oxidation of (U-14C) L-amino acids by drug-susceptible and drug-resistant mycobacteria

1987 ◽  
Vol 29 (5) ◽  
pp. 312-316
Author(s):  
Edwaldo E. Camargo ◽  
Teresa M. Kopajtic ◽  
Glinda K. Hopkins ◽  
Nancy P. Cannon ◽  
Henry N. Wagner Jr
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Reaction System ◽  
Tuberculosis H37rv ◽  
Assay System ◽  
Acid Oxidation ◽  
Resistant Organism ◽  
Drug Resistant ◽  
Amino Acid Oxidation ◽  
Radiometric Assay

A radiometric assay system has been used to study oxidation patterns of (U-14C) L-amino acids by drug-susceptible and drug-resistant mycobacteria. Drug-susceptible M. tuberculosis (H37Rv TMC 102 and Erdman) along with the drug-resistant organism M. tuberculosis (H37 Rv TMC 303), M. bovis, M. avium, M. intracellulare, M. kansasii and M. chelonei were used. The organisms were inoculated into a sterile reaction system with liquid 7H9 medium and one of the (U-14C) L-amino acids. Each organism displayed a different pattern of amino acid oxidation, but these patterns were not distinctive enough for identification of the organism. Complex amino acids such as proline, phenylalanine and tyrosine were of no use in identification of mycobacteria, since virtually all organisms failed to oxidize them. There was no combination of substrates able to separate susceptible from resistant organisms.

scholarly journals Effects of essential amino acids on food and water intake of rats

1994 ◽  
Vol 72 (8) ◽  
pp. 841-848 ◽  
Author(s):  
G. Harvey Anderson ◽  
Shuqin Luo ◽  
Leonidas Trigazis ◽  
Greta Kubis ◽  
Edmund T. S. Li
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Food Intake ◽  
Water Intake ◽  
Essential Amino Acids ◽  
Time Period ◽  
Food And Water Intake ◽  
Intake Water ◽  
Comparable Magnitude

This study examined the effects of selected groups of essential amino acids (EAAs), given by gavage, on short-term food and water intake. Amino acid groups were selected on the basis of their common physiologic functions in relation to current hypotheses on the role of amino acids in food intake control, and the quantities given were based on the proportions in 1.5 g of the EAA content of albumin. The complete EAA mixture (1.5 g) suppressed food intake by an average of 60 and 37% during the 1st and 2nd h of feeding, respectively, but had no influence on feeding in the subsequent 12 h. Total daily (14 h) intake was decreased by 9%. With the exception of the aromatic amino acid (Phe + Tyr + Trp, 0.34 g) group, all groups significantly decreased food intake by a comparable magnitude (32%) during the 1st h. In this time period, rats given the EAAs, Arg + Met + Val (0.38 g), and Arg + His + Lys (0.44 g) mixtures increased their water intake, whereas intake by rats given the Phe + Tyr + Trp + Thr (0.46 g) and Ile + Leu + Val (0.45 g) mixtures was unchanged. Thus, the food intake suppression caused by EAAs was not accounted for by an equal effect of its component amino acid groups. As well, food intake suppression by amino acid groups was not explained by increased water consumption, nor was it simply related to the quantity of nitrogen provided by the treatment.Key words: food intake, water intake, essential amino acids.

scholarly journals Diurnal response in endogenous amino acid oxidation of meal-fed rats

1980 ◽  
Vol 190 (3) ◽  
pp. 663-671 ◽  
Author(s):  
R W Wannemacher ◽  
R E Dinterman
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Dietary Protein ◽  
Normal Diet ◽  
Acid Oxidation ◽  
Body Protein ◽  
Amino Acid Oxidation ◽  
Collagen Protein ◽  
Meal Feeding ◽  
Endogenous Amino Acid

A model has been developed to measure the effects of dietary protein on daily fluctuations in the rate of endogenous amino acid oxidation in meal-fed and starved rats. In addition, N tau-methylhistidine and hydroxyproline were utilized to determine changes in the rate of degradation of myofibrillar and collagen proteins. In rats meal-fed a normal diet of 18% (w/w) casein, a diurnal response was observed in rate of oxidation of radioactive amino acids contained in endogenous labelled body protein, with a nadir 16—20 h and maximum 4—8 h after beginning the feeding. This observation in part may be related to alterations in flux of amino acids from non-hepatic tissues to site of oxidation in liver, as well as alterations in rates of amino acid oxidation after a protein meal. When meal-fed a 70% protein diet, the maximal rates of endogenous amino acid oxidation were significantly increased by 4—8 h after meal-feeding, with no change in fractional rates of degradation of myofibrillar- or collagen-protein breakdown. This could suggest increases in activities of enzymes involved in amino acid oxidation, in rats meal-fed 70% compared with 18% dietary protein. In contrast, meal-feeding of a protein-free diet muted the diurnal response in the rate of oxidation of endogenously labelled amino acids, which correlated with a decrease in the fractional rate of degradation of myofibrillar or collagen protein. Thus dietary protein is apparently responsible for the observed diurnal rhythm rhythms in the rate of amino acid oxidation, whereas carbohydrates tend to mute the response.

Meal stimulation of albumin synthesis: a significant contributor to whole body protein synthesis in humans

1992 ◽  
Vol 263 (4) ◽  
pp. E794-E799 ◽  
Author(s):  
P. De Feo ◽  
F. F. Horber ◽  
M. W. Haymond
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Combined Treatment ◽  
Essential Amino Acids ◽  
Whole Body ◽  
Albumin Synthesis ◽  
Body Protein ◽  
Peripheral Tissues ◽  
Stimulation Of

The present studies were performed to test the hypothesis that the liver, by increasing the synthesis of specific plasma proteins during the absorption of an amino acid meal, may play an important role in the temporary "storage" of ingested essential amino acids and to explore the effects of glucocorticosteroids and recombinant human growth hormone (rhGH) on these processes. The fractional synthetic rates of albumin and fibrinogen were determined using simultaneous infusions of intravenous [1-14C]leucine and intraduodenal [4,5-3H]leucine after 22 h fasting and during absorption of glucose and amino acids in four groups of normal subjects treated for 1 wk with placebo, prednisone (0.8 mg.kg-1.day-1), rhGH (0.1 mg.kg-1.day-1), or combined treatment. When compared with the fasted state and independent of the route of tracer delivery and hormonal treatment, albumin, but not fibrinogen, synthesis increased (P < 0.0001) during absorption of a mixed glucose amino acid meal in all groups. This increase in albumin synthesis accounted for 28% of the increase in whole body protein synthesis associated with feeding and for 24, 22, and 14% in the prednisone, rhGH, and combined treatment groups, respectively. These data suggest that the stimulation of albumin synthesis observed during feeding prevents irreversible oxidative losses of a significant fraction of ingested essential amino acids and may serve as a vehicle to capture excess dietary amino acids and transport them to peripheral tissues to sustain local protein synthesis.

Nutritional evaluation of meat meals for poultry. VIII.* Nutritive values of and limiting amino acids in cereal diets, supplemented with meat meal

1974 ◽  
Vol 25 (1) ◽  
pp. 193 ◽  
Author(s):  
GR Skurray ◽  
RB Cumming
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nutritive Value ◽  
Essential Amino Acids ◽  
Feed Conversion ◽  
Chick Growth ◽  
Meat Meal ◽  
Amino Acid Levels ◽  
Limiting Amino Acids ◽  
Conversion Efficiencies

When a commercial meat meal was used to supplement wheat, corn and sorghum diets to growing chicks, there was a wide variation in performance. Feed conversion efficiencies were higher on diets based on wheat and corn than those based on sorghum. The nutritive value as determined by chick growth tests of a wheat-plus-meat meal diet was higher than a corn or sorghum-plus-meat meal diet. The nutritive value of a wheat–plus–meat meal diet, supplemented with lysine and methionine, was the same as that of a crystalline amino acid reference diet. The weight gains of chicks given these two diets were higher than those obtained with diets based on wheat, corn and sorghum, not supplemented with lysine and methionine. The results were explained in terms of the limiting and digestible essential amino acids in these diets. The limiting amino acids in the diets were determined from the plasma amino acid levels in chicks given these diets. ______________________ *Part VII, Aust. J. agric. Res., 23: 913-22 (1972).

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