scholarly journals Amino Acid Nutrition and Metabolism in Health and Disease

Nutrients ◽  
2019 ◽  
Vol 11 (11) ◽  
pp. 2623
Author(s):  
Rose

Here an overview of the special issue “Amino acid nutrition and metabolism in health and disease” is given. In addition to several comprehensive and timely reviews, this issue had some original research contributions on fundamental research in animal models as well as human clinical trials exploring how the critical nutrients amino acids affect various traits.

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1197
Author(s):  
Klaus Ley

This 11-chapter Special Issue of Cells spans the gamut from basic science in mechanistic animal models to translational science to outcomes of clinical trials, all focused on the role of inflammation in atherosclerosis [...]


2014 ◽  
Vol 3 ◽  
Author(s):  
Kristel Rochus ◽  
An Cools ◽  
Geert P. J. Janssens ◽  
Lynn Vanhaecke ◽  
Birgitte Wuyts ◽  
...  

AbstractIn strict carnivorous domestic cats, a metabolic competition arises between the need to use amino acids for gluconeogenesis and for protein synthesis both in health and disease. The present study investigated the amino acid-sparing potential of propionic acid in cats using dietary propionylated starch (HAMSP) supplementation. A total of thirty cats were fed a homemade diet, supplemented with either HAMSP, acetylated starch (HAMSA) or celite (Control) for three adaptation weeks. Propionylated starch was hypothesised to provide propionic acid as an alternative gluconeogenic substrate to amino acids, whereas acetic acid from HAMSA would not provide any gluconeogenic benefit. Post-adaptation, a 5-d total faecal collection was carried out to calculate apparent protein digestibility coefficients. Fresh faecal and blood samples were collected to analyse fermentation endproducts and metabolites. The apparent protein digestibility coefficients did not differ between supplements (P = 0·372) and were not affected by the protein intake level (P = 0·808). Faecal propionic acid concentrations were higher in HAMSP than in HAMSA (P = 0·018) and Control (P = 0·003) groups, whereas concentrations of ammonia (P = 0·007) were higher in HAMSA than in HAMSP cats. Tendencies for or higher propionylcarnitine concentrations were observed in HAMSP compared with HAMSA (P = 0·090) and Control (P = 0·037) groups, and for tiglyl- + 3-methylcrotonylcarnitine concentrations in HAMSP as compared with Control (P = 0·028) cats. Methylmalonylcarnitine concentrations did not differ between groups (P = 0·740), but were negatively correlated with the protein intake level (r –0·459, P = 0·016). These results suggest that HAMSP cats showed more saccharolytic fermentation patterns than those supplemented with HAMSA, as well as signs of sparing of valine in cats with a sufficient protein intake.


2018 ◽  
Vol 26 (2) ◽  
pp. 213-221
Author(s):  
Maxim V. Stogov ◽  
Elena A. Kireeva

Background. The ability of certain amino acids to stimulate anabolic processes in skeletal muscles has been proved by fundamental research, which makes it important to search for effective agents based on amino acids for stimulation of synthetic processes in skeletal muscles. Aim. To study the effect of oral administration of the original amino acid mixture (Larginine, Lmethionine, Lleucine, Lisoleucine) on protein, lipid and carbohydrate metabolism in skeletal muscles and liver of CBA male mice. Material and Methods. Two series of experiments were performed. In the first series (n=36), the animals were divided into three groups. In group 1 (n = 12), the mice received a diet balanced in protein and carbohydrates for two months. The animals of group 2 (n=12) were kept on a carbohydrate, proteindepleted isocaloric diet, in which wheat gliadin served as the protein source. Mice of group 3 (n=12) were kept on a diet similar to the second group, in which deficit of protein was compensated for with the tested mixture of Lamino acids. In the animals of the second series (n=36) acute liver failure was modeled by a single intraperitoneal injection of 20% carbon tetrachloride solution (CTC) in olive oil. Three days after the injection of CTC, all animals of the second series were randomly divided into three groups, depending on the received diet. Results. The results of the first series of experiments showed that compensation for protein deficiency with amino acid mixture reliably prevented excessive buildup of glycogen in muscles, led to a decrease in lipids in tissue, and also prevented reduction in the level of muscle protein. The results of the second series of experiments showed that intake of the amino acid mixture prevented loss of protein in muscles and supported the proteinsynthetic function of the liver. Conclusion. The study demonstrated that the tested mixture, when taken orally, can prevent disorders of proteincarbohydratelipid ratio in the muscles.


Genes ◽  
2020 ◽  
Vol 11 (10) ◽  
pp. 1173
Author(s):  
Howard Gamper ◽  
Ya-Ming Hou

Aminoacylation of tRNA generates an aminoacyl-tRNA (aa-tRNA) that is active for protein synthesis on the ribosome. Quantification of aminoacylation of tRNA is critical to understand the mechanism of specificity and the flux of the aa-tRNA into the protein synthesis machinery, which determines the rate of cell growth. Traditional assays for the quantification of tRNA aminoacylation involve radioactivity, either with a radioactive amino acid or with a [3′-32P]-labeled tRNA. We describe here a label-free assay that monitors aminoacylation by biotinylation-streptavidin (SA) conjugation to the α-amine or the α-imine of the aminoacyl group on the aa-tRNA. The conjugated aa-tRNA product is readily separated from the unreacted tRNA by a denaturing polyacrylamide gel, allowing for quantitative measurement of aminoacylation. This label-free assay is applicable to a wide range of amino acids and tRNA sequences and to both classes of aminoacylation. It is more sensitive and robust than the assay with a radioactive amino acid and has the potential to explore a wider range of tRNA than the assay with a [3′-32P]-labeled tRNA. This label-free assay reports kinetic parameters of aminoacylation quantitatively similar to those reported by using a radioactive amino acid, suggesting its broad applicability to research relevant to human health and disease.


1978 ◽  
Vol 174 (3) ◽  
pp. 931-938 ◽  
Author(s):  
C J Kelly ◽  
T C Johnson

The phenylalanine analogues p-chlorophenylalanine and alpha-methylphenylalanine were used to inhibit phenylalanine hydroxylase in animal models for phenylketonuria. The present report examines the affects of these analogues on the metabolism of neuroblastoma cells. p-Chlorophenylalanine inhibited growth and was toxic to neuroblastoma cells. Although in vivo this analogue increased cell monoribosomes by 42%, it did not significantly affect poly(U)-directed protein synthesis in vitro. P-Chlorophenylalanine did not compete with phenylalanine or tyrosine for aminoacylation of tRNA and was therefore not substituted for those amino acids in nascent polypeptides. The initial cellular uptake of various large neutral amino acids was inhibited by this analogue but did not affect the flux of amino acids already in the cell; this suggested that an alteration of the cell's amino acid pools was not responsible for the cytotoxicity of the analogues. In contrast with p-chlorophenylalanine, alpha-methylphenylalanine did not exert these direct toxic effects because the administration of alpha-methylphenylalanine in vivo did not affect brain polyribosomes and a comparable concentration of this analogue was neither growth inhibitory nor cytotoxic to neuroblastoma cells in culture. The suitability of each analogue as an inhibitor of phenylalanine hydroxylase in animal models for phenylketonuria is discussed.


1992 ◽  
Vol 284 (2) ◽  
pp. 333-340 ◽  
Author(s):  
S Y Low ◽  
P M Taylor ◽  
H S Hundal ◽  
C I Pogson ◽  
M J Rennie

There is increasing evidence that membrane transporters for glutamine and glutamate are involved in control of liver metabolism in health and disease. We therefore investigated the effects of three catabolic states [starvation (60 h), diabetes (4 days after streptozotocin treatment) and corticosteroid (8-day dexamethasone) treatment] associated with altered hepatic amino acid metabolism on the activity of glutamine and glutamate transporters in sinusoidal membrane vesicles from livers of treated rats. In control preparations, L-[14C]glutamine uptake was largely Na(+)-dependent, but L-[14C]glutamate uptake was largely Na(+)-independent. Vmax. values for Na(+)-dependent uptake of glutamine and/or glutamate exceeded control values (by about 2- and 12-fold respectively) in liver membrane vesicles from starved (glutamine), diabetic (glutamate) or steroid-treated (glutamine and glutamate) rats. The Km values for Na(+)-dependent transport of glutamine or glutamate and the rates of their Na(+)-independent uptake were not significantly altered by any treatment. Na(+)-independent glutamate uptake appeared to include a dicarboxylate-exchange component. The patterns of inhibition of glutamine and glutamate uptake by other amino acids indicated that the apparent induction of Na(+)-dependent amino acid transport in catabolic states included increased functional expression of systems A, N (both for glutamine) and X-ag (for glutamate). The results demonstrate that conditions resulting in increased secretion of catabolic hormones (e.g. corticosteroid, glucagon) are associated with increased capacity for Na(+)-dependent transport of amino acids into liver cells from the blood. The modulation of hepatic permeability to glutamine and glutamate in these situations may control the availability of amino acids for intrahepatic metabolic processes such as ureagenesis, ammonia detoxification and gluconeogenesis.


1974 ◽  
Vol 46 (2) ◽  
pp. 173-182 ◽  
Author(s):  
B. D. Cox ◽  
J. S. Cameron

1. By using ion-exchange columns coupled to a sensitive automated Sakaguchi reaction, in addition to the normal ninhydrin reaction for amino acids, homoarginine, a guanidino homologue of arginine, was found in the plasma and urine of both normal and cystinuric individuals. 2. In all seven cystinuric subjects studied, urinary excretion of homoarginine was approximately ten times that found in normal subjects; the plasma levels of this amino acid were considerably reduced relative to normal individuals. 3. Homoarginine in the plasma can be derived either metabolically from lysine or from dietary sources. 4. In normal subjects homoarginine was cleared at a higher rate than arginine. On the other hand, the clearance of arginine exceeded that for homoarginine in the majority of cystinuric subjects although the values obtained for homoarginine indicate that the defect in amino acid transport also affects this amino acid. 5. The defect in the proximal tubular reabsorption of homoarginine is less severe than that for arginine, suggesting that the reabsorptive site for homoarginine may not be the same as that for arginine. 6. In the design of models for the tubular reabsorption of amino acids in health and disease, the presence of homoarginine and its excessive loss in cystinuria must be accounted for.


2018 ◽  
Vol 26 (2) ◽  
pp. 213-221
Author(s):  
Maxim V. Stogov ◽  
Elena A. Kireeva

Background. The ability of certain amino acids to stimulate anabolic processes in skeletal muscles has been proved by fundamental research, which makes it important to search for effective agents based on amino acids for stimulation of synthetic processes in skeletal muscles. Aim. To study the effect of oral administration of the original amino acid mixture (Larginine, Lmethionine, Lleucine, Lisoleucine) on protein, lipid and carbohydrate metabolism in skeletal muscles and liver of CBA male mice. Material and Methods. Two series of experiments were performed. In the first series (n=36), the animals were divided into three groups. In group 1 (n = 12), the mice received a diet balanced in protein and carbohydrates for two months. The animals of group 2 (n=12) were kept on a carbohydrate, proteindepleted isocaloric diet, in which wheat gliadin served as the protein source. Mice of group 3 (n=12) were kept on a diet similar to the second group, in which deficit of protein was compensated for with the tested mixture of Lamino acids. In the animals of the second series (n=36) acute liver failure was modeled by a single intraperitoneal injection of 20% carbon tetrachloride solution (CTC) in olive oil. Three days after the injection of CTC, all animals of the second series were randomly divided into three groups, depending on the received diet. Results. The results of the first series of experiments showed that compensation for protein deficiency with amino acid mixture reliably prevented excessive buildup of glycogen in muscles, led to a decrease in lipids in tissue, and also prevented reduction in the level of muscle protein. The results of the second series of experiments showed that intake of the amino acid mixture prevented loss of protein in muscles and supported the proteinsynthetic function of the liver. Conclusion. The study demonstrated that the tested mixture, when taken orally, can prevent disorders of proteincarbohydratelipid ratio in the muscles.


Nutrients ◽  
2020 ◽  
Vol 12 (4) ◽  
pp. 1049 ◽  
Author(s):  
Catherine Méplan ◽  
David J. Hughes

In this Special Issue of Nutrients, “The Role of Selenium in Health and Disease” covers diverse diseases in the 8 original research articles and 2 reviews, such as cardiovascular disorders (CVD), metabolic syndrome, obesity, cancer, and viral infection, and highlights novel potential biomarkers of disease risk and prognosis [...]


2021 ◽  
Vol 22 (6) ◽  
pp. 2787
Author(s):  
Christopher Mayer-Bacon ◽  
Neyiasuo Agboha ◽  
Mickey Muscalli ◽  
Stephen Freeland

Here, we summarize a line of remarkably simple, theoretical research to better understand the chemical logic by which life’s standard alphabet of 20 genetically encoded amino acids evolved. The connection to the theme of this Special Issue, “Protein Structure Analysis and Prediction with Statistical Scoring Functions”, emerges from the ways in which current bioinformatics currently lacks empirical science when it comes to xenoproteins composed largely or entirely of amino acids from beyond the standard genetic code. Our intent is to present new perspectives on existing data from two different frontiers in order to suggest fresh ways in which their findings complement one another. These frontiers are origins/astrobiology research into the emergence of the standard amino acid alphabet, and empirical xenoprotein synthesis.


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