scholarly journals Expression of cationic amino acid transporters, carcass traits, and performance of growing pigs fed low-protein amino acid-supplemented versus high protein diets

2013 ◽  
Vol 12 (4) ◽  
pp. 4712-4722 ◽  
Author(s):  
A. Morales ◽  
F. Grageola ◽  
H. García ◽  
A. Araiza ◽  
R.T. Zijlstra ◽  
...  
Keyword(s):  
Amino Acid ◽  
Carcass Traits ◽  
Growing Pigs ◽  
Amino Acid Transporters ◽  
Protein Amino Acid ◽  
Cationic Amino Acid ◽  
Low Protein ◽  
And Performance ◽  
High Protein Diets ◽  
Protein Diets

scholarly journals Industrial amino acids in diets for piglets and growing pigs

1988 ◽  
Vol 60 (7) ◽  
pp. 673-683
Author(s):  
J. Inborr ◽  
K. Suomi
Keyword(s):  
Amino Acids ◽  
Health Status ◽  
Protein Content ◽  
Crude Protein ◽  
Control Diet ◽  
Growing Pigs ◽  
Protein Amino Acid ◽  
Low Protein ◽  
Slaughter Pigs ◽  
Protein Diets

Two production trials with piglets and one with slaughter pigs were carried out in order to investigate the effects of reducing the protein content in the diets followed by an addition of industrial amino acids on performance and health status. In the first piglet trial the crude protein content of the control diet was decreased from 20 to 18.3 % and in the second from 18.3 to 16.7 %. In the trial with growing pigs, the protein content of the control diet was decreased from 17.0 to 15.5 %. Industrial L-lysine, DL-methionine and L-threonine were added to the low protein diets to get the same levels of these amino acids as in the control diets. Piglet performance was similar on all treatments indicating equal availability of added and protein-bound amino acids. Health status of piglets on the low protein diets was considerably improved, indicating less predisposition to post weaning diarrhoea. Pigs on the low protein amino acid fortified diet tended to gain weight faster (788 vs. 743 g/day; p

scholarly journals Alteration of muscle fiber characteristics and the AMPK-SIRT1-PGC-1α axis in skeletal muscle of growing pigs fed low-protein diets with varying branched-chain amino acid ratios

Oncotarget ◽  
2017 ◽  
Vol 8 (63) ◽  
pp. 107011-107021 ◽  
Author(s):  
Yehui Duan ◽  
Fengna Li ◽  
Wenlong Wang ◽  
Qiuping Guo ◽  
Chaoyue Wen ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Muscle Fiber ◽  
Growing Pigs ◽  
Low Protein ◽  
Branched Chain Amino Acid ◽  
Branched Chain ◽  
Protein Diets

Effects of dietary protein and amino acid levels on the expression of selected cationic amino acid transporters and serum amino acid concentration in growing pigs

2012 ◽  
Vol 66 (4) ◽  
pp. 257-270 ◽  
Author(s):  
Héctor García-Villalobos ◽  
Adriana Morales-Trejo ◽  
Benedicto A. Araiza-Piña ◽  
John K. Htoo ◽  
Miguel Cervantes-Ramírez
Keyword(s):  
Amino Acid ◽  
Acid Concentration ◽  
Dietary Protein ◽  
Growing Pigs ◽  
Amino Acid Concentration ◽  
Amino Acid Transporters ◽  
Cationic Amino Acid ◽  
Amino Acid Levels

Dietary protein paradox: decrease of amino acid availability induced by high-protein diets

1993 ◽  
Vol 264 (6) ◽  
pp. G1057-G1065 ◽  
Author(s):  
C. Moundras ◽  
C. Remesy ◽  
C. Demigne
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Dietary Protein ◽  
High Protein ◽  
Glutamine Metabolism ◽  
Metabolic Adaptation ◽  
Casein Diet ◽  
Serine Dehydratase ◽  
High Protein Diets ◽  
Protein Diets

The aim of the present study was to evaluate the effect of changes in dietary protein level on overall availability of amino acids for tissues. For this purpose, rats were adapted to diets containing various concentrations of casein (7.5, 15, 30, and 60%) and were sampled either during the postprandial or postabsorptive period. In rats fed the protein-deficient diet, glucogenic amino acids (except threonine) tended to accumulate in plasma, liver, and muscles. In rats fed high-protein diets, the hepatic balance of glucogenic amino acids was markedly enhanced and their liver concentrations were consistently depressed. This response was the result of a marked induction of amino acid catabolism (a 45-fold increase of liver threonine-serine dehydratase activity was observed with the 60% casein diet). The muscle concentrations of threonine, serine, and glycine underwent changes parallel to plasma and liver concentrations, and a significant reduction of glutamine was observed. During the postabsorptive period, adaptation to high-protein diets resulted in a sustained catabolism of most glucogenic amino acids, which accentuated the drop in their concentrations (especially threonine) in all the compartments studied. The time course of metabolic adaptation from a 60 to a 15% casein diet has also been investigated. Adaptation of alanine and glutamine metabolism was rapid, whereas that of threonine, serine, and glycine was delayed and required 7-11 days. This was paralleled by a relatively slow decay of liver threonine-serine dehydratase (T-SDH) activity in contrast to the rapid adaptation of pyruvate kinase activity after refeeding a high-carbohydrate diet.(ABSTRACT TRUNCATED AT 250 WORDS)

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