Co-dependence of genotype and dietary protein intake to affect expression on amino acid/peptide transporters in porcine skeletal muscle

Amino Acids ◽  
2015 ◽  
Vol 48 (1) ◽  
pp. 75-90 ◽  
Author(s):  
Y. Liu ◽  
X. Kong ◽  
F. Li ◽  
B. Tan ◽  
Y. Li ◽  
...  
1981 ◽  
Vol 240 (6) ◽  
pp. E712-E721 ◽  
Author(s):  
K. J. Motil ◽  
D. E. Matthews ◽  
D. M. Bier ◽  
J. F. Burke ◽  
H. N. Munro ◽  
...  

Whole-body leucine and lysine metabolism was explored in young adult men by a primed constant intravenous infusion of a mixture of L-[1–13C]leucine and L-[alpha-15N]lysine over a 4-h period. Subjects were studied after an overnight fast (postabsorptive state) or while consuming hourly meals (fed state) after adaptation to diets providing either a surfeit level of protein (1.5 g.kg body-1.day-1), a level approximating maintenance requirements (marginal intake) (0.6 g.kg body wt-1.day-1), or a grossly inadequate level (0.1 g.kg-1.day-1). The change in protein intake from a marginal to a surfeit level was associated with an increased leucine flux and incorporation of leucine into body protein. In the fed state, oxidation of leucine increased sharply and release of leucine from tissue protein diminished. When dietary protein intake was reduced from the requirement to inadequate level, leucine flux and body protein synthesis and protein breakdown were reduced, together with a smaller reduction in leucine oxidation. The response of the metabolism of [15N]lysine was responsible for maintenance of leucine and other essential amino acid economy, and they appear to be related to the nitrogen and amino acid requirements of the subject. These findings also demonstrate an effect of meals, modulated by their protein content, on the dynamics of whole-body amino acid metabolism.


2019 ◽  
Vol 109 (3) ◽  
pp. 517-525 ◽  
Author(s):  
Casey M Rebholz ◽  
Zihe Zheng ◽  
Morgan E Grams ◽  
Lawrence J Appel ◽  
Mark J Sarnak ◽  
...  

ABSTRACT Background Accurate assessment of dietary intake is essential, but self-report of dietary intake is prone to measurement error and bias. Discovering metabolic consequences of diets with lower compared with higher protein intake could elucidate new, objective biomarkers of protein intake. Objectives The goal of this study was to identify serum metabolites associated with dietary protein intake. Methods Metabolites were measured with the use of untargeted, reverse-phase ultra-performance liquid chromatography–tandem mass spectrometry quantification in serum specimens collected at the 12-mo follow-up visit in the Modification of Diet in Renal Disease (MDRD) Study from 482 participants in study A (glomerular filtration rate: 25–55 mL · min−1 · 1.73 m−2) and 192 participants in study B (glomerular filtration rate: 13–24 mL · min−1 · 1.73 m−2). We used multivariable linear regression to test for differences in log-transformed metabolites (outcome) according to randomly assigned dietary protein intervention groups (exposure). Statistical significance was assessed at the Bonferroni-corrected threshold: 0.05/1193 = 4.2 × 10−5. Results In study A, 130 metabolites (83 known from 28 distinct pathways, including 7 amino acid pathways; 47 unknown) were significantly different between participants randomly assigned to the low-protein diet compared with the moderate-protein diet. In study B, 32 metabolites (22 known from 8 distinct pathways, including 4 amino acid pathways; 10 unknown) were significantly different between participants randomly assigned to the very-low-protein diet compared with the low-protein diet. A total of 11 known metabolites were significantly associated with protein intake in the same direction in both studies A and B: 3-methylhistidine, N-acetyl-3-methylhistidine, xanthurenate, isovalerylcarnitine, creatine, kynurenate, 1-(1-enyl-palmitoyl)-2-arachidonoyl-GPE (P-16:0/20:4), 1-(1-enyl-stearoyl)-2-arachidonoyl-GPE (P-18:0/20:4), 1-(1-enyl-palmitoyl)-2-arachidonoyl-GPC (P-16:0/20:4), sulfate, and γ-glutamylalanine. Conclusions Among patients with chronic kidney disease, an untargeted serum metabolomics platform identified multiple pathways and metabolites associated with dietary protein intake. Further research is necessary to characterize unknown compounds and to examine these metabolites in association with dietary protein intake among individuals without kidney disease. This trial was registered at clinicaltrials.gov as NCT03202914.


2019 ◽  
Vol 97 (Supplement_3) ◽  
pp. 275-275
Author(s):  
Xinyu Li ◽  
Guoyao Wu

Abstract Largemouth bass (LMB, Micropterus salmoides) is a carnivorous fish. This study was conducted to test the hypothesis that dietary intakes of protein and starch affect the oxidation of nutrients in the intestine, liver, skeletal muscle and kidneys of LMB. Juvenile LMB (average initial weight = 18 g) were fed, for 8 weeks, fish meal- and soy protein concentrate-based diets containing 40%, 45% and 50% crude protein. The three isocaloric diets contained 22.3%, 15.78% and 9.2% dextrinized starch, respectively. The growth performance, energy retention, and lipid retention in LMB increased (P < 0.05) with increasing dietary protein levels, but the efficiency of nitrogen retention did not differ (P > 0.05) among the three groups of fish. Rates of oxidation of 2 mM glutamate and glutamine in the intestine were reduced (P < 0.05) in response to increased dietary protein intake. This adaptive metabolic change likely helps to prevent excessive production of ATP by the gut when the dietary provision of glutamate and glutamine was increased. Increasing dietary protein intake did not affect (P > 0.05) glutamate oxidation in the liver, kidneys or skeletal muscle, or glutamine oxidation in the muscle. In contrast, the rate of glutamine oxidation was increased (P < 0.05) in the liver but decreased (P < 0.05) in the kidneys as dietary protein intake was elevated from 40% to 50%. Rates of oxidation of 5 mM glucose were reduced (P < 0.05) in the liver, kidneys and intestine, but were not altered in skeletal muscle, in response to reduced starch intake. Rates of oxidation of 2 mM palmitate were reduced (P < 0.05) in the kidneys but were not influenced (P > 0.05) in the intestine, skeletal muscle or liver. We conclude that oxidation of energy substrates in LMB tissues is regulated by dietary protein and starch intake in a tissue-specific manner.


Author(s):  
Jenna B. Gillen ◽  
Jorn Trommelen ◽  
Floris C. Wardenaar ◽  
Naomi Y.J. Brinkmans ◽  
Joline J. Versteegen ◽  
...  

Dietary protein intake should be optimized in all athletes to ensure proper recovery and enhance the skeletal muscle adaptive response to exercise training. In addition to total protein intake, the use of specific proteincontaining food sources and the distribution of protein throughout the day are relevant for optimizing protein intake in athletes. In the present study, we examined the daily intake and distribution of various proteincontaining food sources in a large cohort of strength, endurance and team-sport athletes. Well-trained male (n=327) and female (n=226) athletes completed multiple web-based 24-hr dietary recalls over a 2-4 wk period. Total energy intake, the contribution of animal- and plant-based proteins to daily protein intake, and protein intake at six eating moments were determined. Daily protein intake averaged 108±33 and 90±24 g in men and women, respectively, which corresponded to relative intakes of 1.5±0.4 and 1.4±0.4 g/kg. Dietary protein intake was correlated with total energy intake in strength (r=0.71, p <.001), endurance (r=0.79, p <.001) and team-sport (r=0.77, p <.001) athletes. Animal and plant-based sources of protein intake was 57% and 43%, respectively. The distribution of protein intake was 19% (19±8 g) at breakfast, 24% (25±13 g) at lunch and 38% (38±15 g) at dinner. Protein intake was below the recommended 20 g for 58% of athletes at breakfast, 36% at lunch and 8% at dinner. In summary, this survey of athletes revealed they habitually consume > 1.2 g protein/kg/d, but the distribution throughout the day may be suboptimal to maximize the skeletal muscle adaptive response to training.


2016 ◽  
Vol 53 (4) ◽  
pp. 380
Author(s):  
Sarita Devi ◽  
Tinku Thomas ◽  
Pratibha Dwarkanath ◽  
Annamma Thomas ◽  
C. N. Sheela ◽  
...  

Low intakes of quality dietary protein could affect the methionine cycle during pregnancy, which is important for fetal growth and epigenetic regulations. Since low quality protein intake is prevalent in India, it is important to define biomarkers of the low protein intake, specifically of methyl cycle homeostasis. A secondary analysis of data was performed, from a randomized intervention trial with 500 ml milk/d on south Indian pregnant women, to examine the association of dietary protein intake with concentrations of specific amino acids (methionine, glycine and serine). The subjects also underwent isotopic infusions (n = 52) for the measurement of amino acid kinetics. Dietary intakes were measured each week by multiple 24 h recall until delivery. The plasma concentrations of amino acids (methionine, serine and glycine) were compared with kinetics of methionine i.e. transmethylation, remethylation and transulfuration (TM, RM, TS) and serine to glycine conversion rates, as measured by stable isotope labeled amino acid infusion. Dietary protein intake in the 3<sup>rd</sup> trimester correlated positively with intakes of milk and milk based food products (ρ=0.52, p&lt;0.001) and methionine (ρ=0.97, p&lt;0.001) and with gestational weight gain (GWG, ρ=0.32, p=0.044). While the methionine concentration did not correlate with methyl cycle flux parameters (TM, RM and TS), the plasma concentrations of conditionally essential serine and glycine were positively correlated with their respective flux rate and with RM, TM and TS rates. Further, glycine concentrations specifically correlated positively with serine to glycine conversion rates (ρ=0.32, p=0.027). Dietary protein and methionine supply are important for the conservation of methionine during pregnancy. This had an effect on GWG, but not on birth weight, though this may have been due to the relatively small sample size. The plasma concentration of glycine was correlated with the serine-glycine conversion, which affords methyl groups for the body and supplies these when dietary protein/methionine is in poor supply. This indicates that itcan act as a biomarker of the serine-glycine conversion flux rate, which increases in the presence of a poor protein supply. In general, the plasma concentrations of these conditionally essential amino acids may be biomarkers of the methyl cycle during pregnancy, but this needs to be tested in a larger sample.


2005 ◽  
Vol 289 (4) ◽  
pp. E678-E683 ◽  
Author(s):  
Douglas R. Bolster ◽  
Matthew A. Pikosky ◽  
P. Courtney Gaine ◽  
William Martin ◽  
Robert R. Wolfe ◽  
...  

This investigation evaluated the physiological impact of different dietary protein intakes on skeletal muscle protein synthesis postexercise in endurance runners. Five endurance-trained, male runners participated in a randomized, crossover design diet intervention, where they consumed either a low (0.8 g/kg; LP)-, moderate (1.8 g/kg; MP)-, or high (3.6 g/kg; HP)-protein diet for 4 wk. Diets were designed to be eucaloric with carbohydrate, fat, and protein approximating 60, 30, and 10%; 55, 30, and 15%; and 40, 30, and 30% for LP, MP, and HP, respectively. Substrate oxidation was assessed via indirect calorimetry at 3 wk of the dietary interventions. Mixed-muscle protein fractional synthetic rate (FSR) was measured after an endurance run (75 min at 70% V̇o2 peak) using a primed, continuous infusion of [2H5]phenylalanine. Protein oxidation increased with increasing protein intake, with each trial being significantly different from the other ( P < 0.01). FSR after exercise was significantly greater for LP (0.083%/h) and MP (0.078%/h) than for HP (0.052%/h; P < 0.05). There was no difference in FSR between LP and MP. This is the first investigation to establish that habitual dietary protein intake in humans modulates skeletal muscle protein synthesis after an endurance exercise bout. Future studies directed at mechanisms by which level of protein intake influences skeletal muscle turnover are needed.


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