Serum metabolomics of Alaskan sled dogs during endurance racing

2018 ◽  
Vol 14 (3) ◽  
pp. 149-159 ◽  
Author(s):  
L.-J. Gamble ◽  
C.W. Frye ◽  
C.M. Hansen ◽  
J.W. Locasale ◽  
X. Liu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Carbohydrate Metabolism ◽  
Endurance Exercise ◽  
Long Distance ◽  
Baseline Serum ◽  
Sled Dogs ◽  
Dawson City ◽  
Amino Acid Depletion ◽  
Branched Chain

Long distance racing sled dogs are fed diets high in fat since lipid metabolism has long been thought to be the major substrate utilised during endurance racing. However, recent studies suggests that sled dogs are equally, if not more, dependent on carbohydrate metabolism. Considering the metabolic disparity regarding the energetics of endurance exercise, our study aimed to explore the serum metabolomic profiles of sled dogs running a 1,609 km (1000 mile) race. We hypothesised that there would be amino acid depletion due to gluconeogenesis and alteration in the citric acid cycle (CAC) based on the limited carbohydrate diet they consume. Serum was obtained from 6 Alaskan sled dogs approximately 24 h prior to the race (Whitehorse), at the midrace checkpoint (Dawson City), and again at the finish (Fairbanks). Serum was analysed using liquid chromatography-mass spectrometry for over 200 metabolites involved in amino acid, lipid, and carbohydrate metabolism with MetaboAnalyst Software 3.0. Major metabolic changes observed were decreased free fatty acids and enhanced acyl-carnitine derivatives during the race compared to baseline. Serum depletion of nearly all amino acids except for branched chain amino acids and phenylalanine was observed suggesting extensive protein catabolism. Many of the CAC intermediates were variable with increases in abnormal end glycation products. These results highlight that sled dogs display general amino acid depletion for pyruvate, acetyl CoA and CAC pathway intermediates with increased carnitine bound lipid metabolites, suggesting rate limiting beta-oxidation during endurance exercise, particularly at mid race. Further metabolomic studies to assess the influence of exercise and nutritional regimens are warranted to better understand substrate utilisation in working dogs.

Root uptake and xylem transport of cadmium in wheat and triticale as affected by exogenous amino acids

2017 ◽  
Vol 68 (5) ◽  
pp. 415 ◽  
Author(s):  
K. Khodamoradi ◽  
A. H. Khoshgoftarmanesh ◽  
S. A. M. Mirmohammady Maibody
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Bread Wheat ◽  
Nutrient Solution ◽  
Metal Ion ◽  
Xylem Sap ◽  
Root Uptake ◽  
Plant Roots ◽  
Control Treatment ◽  
Long Distance

Organic acids exuded from plant roots significantly modify uptake and long-distance translocation of metals. Little is known about the effect of amino acids on metal ion uptake by plant roots. The present study investigated the effects of exogenous amino acids (histidine and glycine) in a nutrient solution on root uptake and xylem sap transport of cadmium (Cd) in triticale (× Triticosecale cv. Elinor) and bread wheat (Triticum aestivum L. cv. Back Cross Rushan). Plant seedlings were grown in a Cd-free modified Hoagland nutrient solution to which 1 µm Cd was added with either 50 µm histidine or 50 µm glycine or without amino acids at 4 weeks after germination. A control treatment consisted of a nutrient solution free of Cd and amino acids. In bread wheat, addition of histidine to the Cd-containing nutrient solution resulted in a higher operationally defined symplastic Cd fraction but a lower apoplastic one in the roots. In triticale, addition of either amino acid decreased the symplastic Cd fraction but increased the apoplastic one. Addition of histidine to the nutrient solution increased Cd concentration in wheat xylem sap but had no significant effect on Cd concentration in triticale xylem sap. Compared with the Cd-only treatment, the glycine-containing treatment led to significantly reduced Cd concentrations in xylem sap of both plant species. Wheat plants supplied with histidine and Cd accumulated greater amounts of Cd in their shoots than those supplied with Cd alone. Glycine had no significant effects on the Cd content of wheat shoots but decreased it in triticale shoots. Results indicate that the effects of amino acids on plant root uptake and xylem sap translocation of Cd depend on the type of amino acid supplemented. This finding is of great importance for selecting and/or breeding cultivars with Cd-toxicity tolerance.

scholarly journals Rhizobium leguminosarum Has a Second General Amino Acid Permease with Unusually Broad Substrate Specificity and High Similarity to Branched-Chain Amino Acid Transporters (Bra/LIV) of the ABC Family

2002 ◽  
Vol 184 (15) ◽  
pp. 4071-4080 ◽  
Author(s):  
A. H. F. Hosie ◽  
D. Allaway ◽  
C. S. Galloway ◽  
H. A. Dunsby ◽  
P. S. Poole
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Rhizobium Leguminosarum ◽  
Binding Protein ◽  
Amino Acid Transporters ◽  
Acid Uptake ◽  
Amino Acid Permease ◽  
Branched Chain Amino Acid ◽  
General Amino Acid Permease ◽  
Branched Chain

ABSTRACT Amino acid uptake by Rhizobium leguminosarum is dominated by two ABC transporters, the general amino acid permease (Aap) and the branched-chain amino acid permease (BraRl). Characterization of the solute specificity of BraRl shows it to be the second general amino acid permease of R. leguminosarum. Although BraRl has high sequence identity to members of the family of hydrophobic amino acid transporters (HAAT), it transports a broad range of solutes, including acidic and basic polar amino acids (l-glutamate, l-arginine, and l-histidine), in addition to neutral amino acids (l-alanine and l-leucine). While amino and carboxyl groups are required for transport, solutes do not have to be α-amino acids. Consistent with this, BraRl is the first ABC transporter to be shown to transport γ-aminobutyric acid (GABA). All previously identified bacterial GABA transporters are secondary carriers of the amino acid-polyamine-organocation (APC) superfamily. Also, transport by BraRl does not appear to be stereospecific as d amino acids cause significant inhibition of uptake of l-glutamate and l-leucine. Unlike all other solutes tested, l-alanine uptake is not dependent on solute binding protein BraCRl. Therefore, a second, unidentified solute binding protein may interact with the BraDEFGRl membrane complex during l-alanine uptake. Overall, the data indicate that BraRl is a general amino acid permease of the HAAT family. Furthermore, BraRl has the broadest solute specificity of any characterized bacterial amino acid transporter.

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.

Effect of free fatty acids on blood amino acid levels in human

1986 ◽  
Vol 250 (6) ◽  
pp. E686-E694 ◽  
Author(s):  
E. Ferrannini ◽  
E. J. Barrett ◽  
S. Bevilacqua ◽  
R. Jacob ◽  
M. Walesky ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Plasma Insulin ◽  
Plasma Free Fatty Acid ◽  
Blood Levels ◽  
Experimental Conditions ◽  
Lipid Infusion ◽  
Amino Acid Levels ◽  
Branched Chain

Raised plasma free fatty acid (FFA) levels effectively impede glucose uptake in vivo, thereby conserving plasma glucose and sparing glycogen. To test whether FFA have any effect on blood amino acid levels, we infused Intralipid plus heparin or saline into healthy volunteers under four different experimental conditions: A) overnight fast; B) euglycemic hyperinsulinemia (approximately 100 microU/ml); C) hyperglycemic (approximately 200 mg/100 ml) hyperinsulinemia (approximately 50 microU/ml); and D) hyperglycemic (approximately 300 mg/100 ml) normoinsulinemia (approximately 20 microU/ml). In the fasting state (A), lipid infusion was associated with lower blood levels of most amino acids, both branched chain and glucogenic. This effect, however, could not be ascribed to lipid infusion alone, because plasma insulin levels were also stimulated. The clamp studies (B, C, and D) allowed to assess the influence of lipid on blood amino acid levels at similar plasma insulin and glucose levels. It was thus observed that lipid infusion has a significant hypoaminoacidemic effect of its own under both euglycemic (B) and hyperglycemic (C) conditions; this effect involved many glucogenic amino acids (alanine, glycine, phenylalanine, serine, threonine, and cystine) but none of the branched-chain amino acids (leucine, isoleucine, and valine). In marked contrast, normoinsulinemic hyperglycemia (D), with or without lipid infusion, caused no change in the blood level of any measured amino acid. We conclude that lipid infusion has a hypoaminoacidemic action. We also suggest that this action is permitted by insulin and may involve specific metabolic interactions (e.g., reduced availability of glucose-derived pyruvate or glycerophosphate) as well as enhanced uptake by the liver.

scholarly journals Targeted Metabolomic Analysis of a Mucopolysaccharidosis IIIB Mouse Model Reveals an Imbalance of Branched-Chain Amino Acid and Fatty Acid Metabolism

2020 ◽  
Vol 21 (12) ◽  
pp. 4211 ◽  
Author(s):  
Valeria De Pasquale ◽  
Marianna Caterino ◽  
Michele Costanzo ◽  
Roberta Fedele ◽  
Margherita Ruoppolo ◽  
...  
Keyword(s):  
Amino Acids ◽  
Fatty Acid ◽  
Amino Acid ◽  
Mouse Model ◽  
Molecular Mechanisms ◽  
Clinical Manifestations ◽  
Neurological Impairment ◽  
Genetic Mutation ◽  
Inherited Disorders ◽  
Branched Chain

Mucopolysaccharidoses (MPSs) are inherited disorders of the glycosaminoglycan (GAG) metabolism. The defective digestion of GAGs within the intralysosomal compartment of affected patients leads to a broad spectrum of clinical manifestations ranging from cardiovascular disease to neurological impairment. The molecular mechanisms underlying the progression of the disease downstream of the genetic mutation of genes encoding for lysosomal enzymes still remain unclear. Here, we applied a targeted metabolomic approach to a mouse model of PS IIIB, using a platform dedicated to the diagnosis of inherited metabolic disorders, in order to identify amino acid and fatty acid metabolic pathway alterations or the manifestations of other metabolic phenotypes. Our analysis highlighted an increase in the levels of branched-chain amino acids (BCAAs: Val, Ile, and Leu), aromatic amino acids (Tyr and Phe), free carnitine, and acylcarnitines in the liver and heart tissues of MPS IIIB mice as compared to the wild type (WT). Moreover, Ala, Met, Glu, Gly, Arg, Orn, and Cit amino acids were also found upregulated in the liver of MPS IIIB mice. These findings show a specific impairment of the BCAA and fatty acid catabolism in the heart of MPS IIIB mice. In the liver of affected mice, the glucose-alanine cycle and urea cycle resulted in being altered alongside a deregulation of the BCAA metabolism. Thus, our data demonstrate that an accumulation of BCAAs occurs secondary to lysosomal GAG storage, in both the liver and the heart of MPS IIIB mice. Since BCAAs regulate the biogenesis of lysosomes and autophagy mechanisms through mTOR signaling, impacting on lipid metabolism, this condition might contribute to the progression of the MPS IIIB disease.

In Vitro adsorption Spectrum of Plasma Amino Acids by Coated Charcoal Hemoperfusion

1983 ◽  
Vol 6 (5) ◽  
pp. 267-270 ◽  
Author(s):  
Z.Q. Shi ◽  
T.M.S. Chang
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Hepatic Coma ◽  
Aromatic Amino Acids ◽  
Molar Ratio ◽  
Adsorption Experiment ◽  
Preferential Adsorption ◽  
Branched Chain ◽  
Charcoal Hemoperfusion

In order to clarify wether coated charcoal hemoperfusion is capable of normalizing amino acid disturbances in hepatic coma, in vitro adsorption and in vitro hemoperfusion studies were carried out. We have found that collodion-coated activated charcoal beads preferentially removed much more aromatic acids (AAA) than branched chain amino acids (BCAA). In the in vitro adsorption experiment with 50 μM amino acid standards aqueous solution, 99% of AAAs were removed by charcoal while only 50 to 81% of BCAAs were removed. As the concentration of amino acids in solution was doubled from μM to 100 μM, BCAA removal was halved while about 90% of AAA was still being removed. In vitro hemoperfusion with heparinized blood from hepatic failure rats, the clearance and the removal of AAAs were significantly greater than those of BCAAs. Consequently, the molar ratio of BCAA over AAA was markedly improved from the initial 1.09 to 3.87 after 60 min of hemoperfusion. Thus, we have demonstrated the preferential adsorption of aromatic amino acids by collodion-coated charcoal beads. The correction of BCAA/AAA molar ratio is also demonstrated.

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