Influence of Leucine on Protein Metabolism of Chicken Embryo Myoblasts is Modulated by Varying Serum Concentrations in the Medium

Oki, Mai; Sato, Hiroyuki; Nakagawa, Kazuki; Kita, Kazumi

doi:10.2141/jpsa.44.161

Cited by 3 publications

(3 citation statements)

References 16 publications

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“…Leucine can directly activate the signaling pathway of mammalian target of rapamycin complex 1 (mTORC1) (Dodd and Tee, 2012). In chickens, we also reported that leucine could stimulate protein synthesis of chicken embryo myoblasts (Oki et al, 2007). Compared to leucine, the information about the influence of other BCAA, isoleucine and valine, on embryo growth of chickens has been limited.…”

Section: Introductionmentioning

confidence: 99%

Effect of In Ovo Administration of Branched-Chain Amino Acids on Embryo Growth and Hatching Time of Chickens

et al. 2015

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The effect of various branched-chain amino acids (BCAA : isoleucine, leucine, valine) on embryo growth and the hatching time of fertilized eggs of chickens was examined. Before the onset of egg incubation, one of BCAA was injected into fertilized eggs. The amount of each BCAA administrated into eggs was equal to 1% of each amino acid exits in the egg. On day 14 of incubation, the weight of embryos was measured. On day 21, the hatching time was recorded, and body weight of chicks at birth was measured. The in ovo administration of BCAA increased the weight of whole embryo compared to the control. Compared to the control, the in ovo administration of leucine and valine significantly accelerated the hatching time. There were no significant differences in body weight of newly hatched chicks among all treatments. It was concluded that the in ovo administration of BCAA, especially leucine and valine, could accelerate embryo growth resulting in the acceleration of hatching time of chicks.

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Section: Introductionmentioning

confidence: 99%

Effect of In Ovo Administration of Branched-Chain Amino Acids on Embryo Growth and Hatching Time of Chickens

et al. 2015

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“…Leucine can also directly activate the signaling pathway of mammalian target of rapamycin complex 1 (mTORC1) (Dodd and Tee, 2012). In chickens, we reported that leucine could increase protein synthesis of chicken embryo myoblasts as well as mammals (Oki et al, 2007). Compared to leucine, however, the information about valine, which is also one of branched amino acids, on protein synthesis of chicken embryo myoblasts has been limited.…”

Section: Introductionmentioning

confidence: 99%

Nutritional Evaluation of Glycated Valine and Tryptophan as a Precursor for Protein Synthesis in Chicken Embryo Myoblasts

2015

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Valine and Tryptophan play a role of being a precursor for protein synthesis. Glycation is a non-enzymatic reaction causing dehydrating condensation between the carbonyl group of glucose and the α-amino group of amino acids. Glycation of tryptophan forms two types of glycated compounds, Amadori product and (1R,3S)-1-(D-gluco-1, 2,3,4,5-pentahydroxypentyl)-1,2,3,4-tetrahydro-β-carboline-3-carboxylic acid (PHP-THβC). In case of valine, only Amadori product is formed by glycation. These compounds are lack of the α-amino group, which might not make glycated amino acids be a precursor for protein synthesis. It is known that glycation proceeds more readily in chickens than in mammals because hyperglycemia and high body temperature are features in avian species. In this study, therefore, we attempted to evaluate nutritional value of glycated valine and tryptophan as a precursor for protein synthesis. Myoblasts from chicken embryos were incubated in valine or tryptophan-free medium supplemented with or without insulin-like growth factor-I (IGF-I). In this cell culture system, the effect of glucose-valine Amadori product supplemented in the valine deficient medium was compared to that of supplemented valine. The effect of PHP-THβC supplementation was also examined. Protein synthesis and degradation of myoblasts were measured using a radioactive tracer, [ 3 H]-phenylalanine. Protein synthesis of chicken embryo myoblasts was not affected by the addition of glucose-valine Amadori product into valine-deficient medium. When IGF-I was added in the medium, and the addition of PHP-THβC into tryptophan-deficient medium increased protein synthesis of chicken embryo myoblasts, but the extent of elevation of protein synthesis was lower than that in case of tryptophan supplementation into tryptophan-deficient medium. In the absence of IGF-I, PHP-THβC did not increase protein synthesis. These results suggest that valine-glucose Amadori product and PHP-THβC does not have nutritional value for being a precursor of protein synthesis.

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“…In chickens, we have already reported that leucine could stimulate protein synthesis of chicken embryo myoblasts (Oki et al, 2007). Compared to leucine, the information about the influence of valine, which is also one of branched amino acids, on protein synthesis of chicken embryo myoblasts has been limited.…”

Section: Introductionmentioning

confidence: 99%

Influence of Valine Analogues on Protein Synthesis of Chicken Embryo Myoblasts

Kita

Makino

2014

J. Poult. Sci.

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The influence of various valine analogues on protein synthesis of chicken embryo myoblasts was examined. Valine and its analogues (D-valine, methylvaline, valinol) were supplemented into Medium 199 containing 20 ng/ml of chicken insulin-like growth factor-I (IGF-I) instead of fetal calf serum (FCS). Influence of branched chain amino acids (isoleucine, leucine, valine) on myoblast protein synthesis was also examined. The levels of valine analogue concentration were based on the valine concentration (213 μM) in Medium 199, and the concentrations of supplements were set at 213 μM (×1 of valine in Medium 199) and 2,130 μM (×10 of valine in Medium 199). Protein synthesis was measured by incorporation of 3 H-phenylalanine. Methylvaline, which is one of valine derivatives having a methylated amino group, and D-valine, which is an optical isomer of L-valine, had no influence on myoblast protein synthesis although the concentrations of these compounds were 10-times higher (2,130 μM) than that of valine in Medium 199. Leucine and valine had the potency to increase protein synthesis of chicken embryo myoblasts. The supplementation of valinol, which is one of valine derivatives having a hydrated carboxyl group, with 10-times higher concentration than that of valine in Medium 199, decreased myoblast protein synthesis. These results suggested that valinol could be used as an inhibitor of myoblast protein synthesis.

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Influence of Leucine on Protein Metabolism of Chicken Embryo Myoblasts is Modulated by Varying Serum Concentrations in the Medium

Cited by 3 publications

References 16 publications

Effect of In Ovo Administration of Branched-Chain Amino Acids on Embryo Growth and Hatching Time of Chickens

Effect of In Ovo Administration of Branched-Chain Amino Acids on Embryo Growth and Hatching Time of Chickens

Nutritional Evaluation of Glycated Valine and Tryptophan as a Precursor for Protein Synthesis in Chicken Embryo Myoblasts

Influence of Valine Analogues on Protein Synthesis of Chicken Embryo Myoblasts

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