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.

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 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.

PSX-A-17 Late-Breaking: Methionine and total sulfur amino acid requirements for pups (>14 wk to 9 months), adults, and senior Labrador Retrievers using the indicator amino acid oxidation (IAAO) technique

2021 ◽  
Vol 99 (Supplement_3) ◽  
pp. 374-374
Author(s):  
Jessica L Varney ◽  
Charlene Watson ◽  
Nicole Colopy ◽  
John Moss ◽  
Jordan T Weil ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Control Diet ◽  
Age Groups ◽  
Isotope Ratio Mass Spectrometry ◽  
Co2 Production ◽  
Acid Oxidation ◽  
Total Sulfur ◽  
Amino Acid Oxidation ◽  
Labrador Retrievers

Abstract Methionine and cystine are often considered limiting amino acids in canine diets but limited requirement studies have been conducted especially for different life stages. Eighteen Labrador Retrievers (6 pups (>14 wk-9 month), 6 adults, and 6 seniors [>8yr)] were utilized in feeding studies to evaluate the changing requirements of methionine (Met) and total sulfur amino acids (TSAA) as canines age. For this study, the indicator amino acid oxidation (IAAO) technique was utilized to determine the amino acid (AA) requirements in each of the three age groups. Dogs were subjected to diets ranging from deficient to excess, with indispensable amino acids formulated at 1.6x NRC values. To allow for adaptation, a control diet with same dietary ingredients, protein and amino acid levels was fed for two days prior to feeding the test diets on the third day. On test day, a baseline breath sample was collected for determining CO2 production using a respiration mask (Oxymax, Columbus Instruments). A priming dose of L-[1-13C] phenylalanine (Cambridge Isotope Laboratories, Inc.) based on body weight was utilized, followed by [1-13C] Phe doses every 30 minutes, spanning a four hour period. After each dose 13CO2 was collected, and enrichment was determined by isotope ratio mass spectrometry (IRMS). Results for IRMS were converted to atom percent excess (APE) and analyzed using a piecewise model of best fit (JMP® Pro 16). A segmented line regression showed Met and TSAA mean and population requirements for pups (>14 wk-9 mo.) were 0.78 ± 0.16 and 1.53 ± 0.21 g/1000kcal (mean ± 2SD), respectively. Meanwhile, for adults, mean and population requirements for Met and TSAA were estimated to be 0.68 ± 0.19 and 1.4 ± 0.30 g/1000kcal (mean ± 2SD), respectively, and for seniors, Met and TSAA mean and population requirements were determined to be 0.62 ± 0.17 and 1.27 ± 0.23 g/1000kcal (mean ± 2SD), respectively.

scholarly journals Prolonged maternal amino acid infusion in late-gestation pregnant sheep increases fetal amino acid oxidation

2009 ◽  
Vol 297 (3) ◽  
pp. E638-E646 ◽  
Author(s):  
Paul J. Rozance ◽  
Michelle M. Crispo ◽  
James S. Barry ◽  
Meghan C. O'Meara ◽  
Mackenzie S. Frost ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Supplementation ◽  
Late Gestation ◽  
Acid Oxidation ◽  
Leucine Incorporation ◽  
Oxygen Utilization ◽  
Amino Acid Oxidation ◽  
Amino Acid Infusion ◽  
Pregnant Sheep

Protein supplementation during human pregnancy does not improve fetal growth and may increase small-for-gestational-age birth rates and mortality. To define possible mechanisms, sheep with twin pregnancies were infused with amino acids (AA group, n = 7) or saline (C group, n = 4) for 4 days during late gestation. In the AA group, fetal plasma leucine, isoleucine, valine, and lysine concentrations were increased ( P < 0.05), and threonine was decreased ( P < 0.05). In the AA group, fetal arterial pH (7.365 ± 0.007 day 0 vs. 7.336 ± 0.012 day 4, P < 0.005), hemoglobin-oxygen saturation (46.2 ± 2.6 vs. 37.8 ± 3.6%, P < 0.005), and total oxygen content (3.17 ± 0.17 vs. 2.49 ± 0.20 mmol/l, P < 0.0001) were decreased on day 4 compared with day 0. Fetal leucine disposal did not change (9.22 ± 0.73 vs. 8.09 ± 0.63 μmol·min−1·kg−1, AA vs. C), but the rate of leucine oxidation increased 43% in the AA group (2.63 ± 0.16 vs. 1.84 ± 0.24 μmol·min−1·kg−1, P < 0.05). Fetal oxygen utilization tended to be increased in the AA group (327 ± 23 vs. 250 ± 29 μmol·min−1·kg−1, P = 0.06). Rates of leucine incorporation into fetal protein (5.19 ± 0.97 vs. 5.47 ± 0.89 μmol·min−1·kg−1, AA vs. C), release from protein breakdown (4.20 ± 0.95 vs. 4.62 ± 0.74 μmol·min−1·kg−1), and protein accretion (1.00 ± 0.30 vs. 0.85 ± 0.25 μmol·min−1·kg−1) did not change. Consistent with these data, there was no change in the fetal skeletal muscle ubiquitin ligases MaFBx1 or MuRF1 or in the protein synthesis regulators 4E-BP1, eEF2, eIF2α, and p70S6K. Decreased concentrations of certain essential amino acids, increased amino acid oxidation, fetal acidosis, and fetal hypoxia are possible mechanisms to explain fetal toxicity during maternal amino acid supplementation.

scholarly journals Development of the Indicator Amino Acid Oxidation Technique to Determine the Availability of Amino Acids from Dietary Protein in Pigs

2005 ◽  
Vol 135 (12) ◽  
pp. 2866-2870 ◽  
Author(s):  
Soenke Moehn ◽  
Robert F. P. Bertolo ◽  
Paul B. Pencharz ◽  
Ronald O. Ball
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Dietary Protein ◽  
Acid Oxidation ◽  
Amino Acid Oxidation

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.

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