Influence of Valine Analogues on Protein Synthesis of Chicken Embryo Myoblasts

Kita, Kazumi; Makino, Ryosuke

doi:10.2141/jpsa.0130162

Cited by 3 publications

(4 citation statements)

References 11 publications

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“…Thirty fertilized eggs of Single Comb White Leghorn chickens were purchased from a local hatchery (Koiwai Farm Co., Ltd, Shizukuishi, Iwate, Japan). Embryonic cells from various tissues were prepared as described previously ( Kita and Makino, 2014 ). Briefly, fertilized eggs were incubated for 19 days, and embryos were taken from eggs.…”

Section: Methodsmentioning

confidence: 99%

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Incorporation of Glycated-Tryptophan and -Valine into Various Cells Derived from Chicken Embryos

2016

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Avian species including chickens are known to be hyperglycemic animals. Hyperglycemia promotes the glycation which at first forms Amadori products undergoing further complex reaction to form advanced glycation end products (AGEs). Our previous study revealed that AGEs derived from glucose and amino acids were predominantly incorporated into spleen, kidney and liver. However, it has not been elucidated whether Amadori products (glycated amino acids) can also be incorporated into cells or not. Therefore, in the present study, radioactive glycated-tryptophan and -valine were prepared and the incorporation of these glycated amino acids into various chicken embryonic cells was studied. Various embryonic cells prepared from muscle, liver, spleen and kidney of chicken embryos were incubated in Medium 199 supplemented with 14 C-labeled glycated-tryptophan or -valine. After incubation, embryonic cells were well-rinsed and then the radioactivity incorporated into cells was measured. It was revealed that both glycated amino acids were incorporated into embryonic cells derived from muscle, liver, spleen and kidney. In muscular cells, the incorporation of glycated-tryptophan was higher than that of glycated-valine. On the other hand, in embryonic cells derived from liver and kidney, the amount of glycated-tryptophan incorporated into cells was almost the same to that of glycated-valine. In conclusion, it was supposed that both glycated-tryptophan and -valine could be incorporated into various cells derived from muscle, liver, spleen and kidney of chicken embryos and that the incorporation might have the organ specificity.

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Section: Methodsmentioning

confidence: 99%

“…Embryonic cells from various tissues were prepared as described previously (Kita and Makino, 2014). Briefly, fertilized eggs were incubated for 19 days, and embryos were taken from eggs.…”

Section: Preparation Of Cells From Various Tissues Of Chicken Embryosmentioning

confidence: 99%

Incorporation of Glycated-Tryptophan and -Valine into Various Cells Derived from Chicken Embryos

2016

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“…Thirty fertilized eggs of single comb White Leghorn chickens were purchased from a local hatchery (Koiwai Farm Co., Ltd, Shizukuishi, Iwate, Japan). Myoblasts from embryos were prepared as described previously (Kita and Makino, 2014). Briefly, fertilized eggs were incubated for 19 days, and embryos were taken from eggs.…”

Section: Methodsmentioning

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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“…Thirty fertilized eggs of Single Comb White Leghorn chickens were purchased from a local hatchery (Koiwai Farm Co., Ltd, Shizukuishi, Iwate, Japan). Embryonic cells from various tissues were prepared as previously described (Kita and Makino, 2014). In brief, fertilized eggs were incubated for 17 days, and embryos were obtained from eggs.…”

Section: Preparation Of Cells From Various Tissues Of Chicken Embryosmentioning

confidence: 99%

Glycated Tryptophan PHP-TH<i>β</i>C Incorporated into Various Chicken Embryonic Cells Constitutes Cellular Proteins

Makino

Kita

2021

J. Poult. Sci.

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Glycation is a non-enzymatic reaction, and amino acids are glycated by glucose in vivo. Tryptophan is glycated with glucose to form two types of glycated compounds, tryptophan-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). Although PHP-THβC can be incorporated into various chicken embryonic cells, the mechanism of its incorporation into intracellular fluids has not been clarified. In this study, we examined whether PHP-THβC once incorporated into various chicken embryonic cells can combine with proteins. Embryonic cells from the breast muscle, liver, spleen, kidney, proventriculus, gizzard, and skin were prepared and 3 H-PHP-THβC was added to the culture medium at final concentrations of 0, 200, 400, 600, and 800 μM to examine the incorporation of PHP-THβC. After 18 h of incubation, radioactivity was measured in the whole-cell and protein fractions of the chicken embryonic cells. As PHP-THβC concentration increased from 0 to 600 μM, its accumulation in the whole-cell fractions of all types of chicken embryonic cells linearly increased and reached the maximum level. The saturated PHP-THβC accumulation in the whole-cell fractions suggests that PHP-THβC could be incorporated into intracellular fluids across cellular membranes by some transporter proteins. As PHP-THβC concentration increased from 0 to 800 μM, its accumulation in the protein fractions of all types of chicken embryonic cells increased in a linear manner and reached a maximum level in the 800-μM PHP-THβC treatment group. This is the first study to indicate that a part of PHP-THβC incorporated into the whole-cell fraction was detected in the protein fraction of various chicken embryonic cells.

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Influence of Valine Analogues on Protein Synthesis of Chicken Embryo Myoblasts

Cited by 3 publications

References 11 publications

Incorporation of Glycated-Tryptophan and -Valine into Various Cells Derived from Chicken Embryos

Incorporation of Glycated-Tryptophan and -Valine into Various Cells Derived from Chicken Embryos

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

Glycated Tryptophan PHP-TH<i>β</i>C Incorporated into Various Chicken Embryonic Cells Constitutes Cellular Proteins

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