Detection of Two Types of Glycated Tryptophan Compounds in the Plasma of Chickens Fed Tryptophan Excess Diets

Kita, Kazumi; Kawashima, Yoshimi; Makino, Ryosuke; Namauo, Toshiharu; Ogawa, Satoshi; Muraoka, Hiroyuki; Fujimura, Shigefumi

doi:10.2141/jpsa.0120150

Cited by 8 publications

(10 citation statements)

References 12 publications

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“…Previously, we successfully detected two types of glycated tryptophan compounds in the chicken plasma, but did not clearly distinguish glucose-tryptophan Amadori product from PHP-THβC (Kita et al, 2013). In the present study, as shown in Table 4, glucose-tryptophan Amadori product and PHP-THβC could be successfully detected in the plasma.…”

Section: Discussioncontrasting

confidence: 64%

“…Because of hyperglycemia and high temperature in avian species, glycation of glucose and tryptophan has to be easily proceeded compared to mammals (Klandorf et al, 1995;Iqbal et al, 1999). Recently, we have detected two types of glycated tryptophan compounds in the plasma of chickens fed tryptophan excess diets (Kita et al, 2013). But, in our previous study, glucose-tryptophan Amadori product and PHP-THβC were not identified separately.…”

Section: Introductionmentioning

confidence: 70%

“…The method to remove protein and lipid was described previously (Kita et al, 2013). Briefly, frozen plasma samples were thawed, and 500 μl of plasma was mixed with 2 ml of acetonitrile for deproteinization.…”

Section: Deprotenization Delipidization Of Plasma Samplesmentioning

confidence: 99%

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Glycated Tryptophan in the Plasma of Chickens Fed Tryptophan-excess Diets

et al. 2015

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When tryptophan is glycated with glucose, it results in forming two types of glycated tryptophan, glucosetryptophan 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). Hyperglycemia and high body temperature in avian species are supposed to elevate the concentration of glycated tryptophan in the plasma of chickens fed tryptophan-excess diets. However, plasma concentrations of both glucose-tryptophan Amadori product and PHP-THβC have not been determined so far. Young chickens were fed tryptophan-excess diets (1, 2 or 3% excess) for 14 or 21 days, and plasma concentrations of two types of glycated tryptophan were measured using liquid chromatograph mass spectrometer (LC/MS). In the present study, we successfully detected and quantified both glucose-tryptophan Amadori product and PHP-THβC in the plasma, which revealed that plasma concentrations of glucose-tryptophan Amadori product and PHP-THβC were approximately 1 and 2-4 μM, respectively. Furthermore, plasma concentrations of glycated tryptophan compounds significantly correlated to that of plasma tryptophans, and total amount of both glycated tryptophan compounds was almost 10% of plasma tryptophan.

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Section: Discussioncontrasting

confidence: 64%

Section: Introductionmentioning

confidence: 70%

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Glycated Tryptophan in the Plasma of Chickens Fed Tryptophan-excess Diets

et al. 2015

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“…However, it has not been elucidated whether Amadori products (glycated amino acids), which are the precursors of AGEs, can be also incorporated into cells or not. Previously, we could successfully synthesize Amadori products from glucose and tryptophan, and measured the plasma concentrations of glycated-tryptophan (Kita et al, 2013;Makino et al, 2015). Furthermore, we have been able to synthesize glycated-valine (Takahashi and Kita, 2016).…”

Section: Introductionmentioning

confidence: 99%

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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“…The protocol used to remove protein and lipid from plasma samples was based on a previous report by Kita et al (2013), with small modification. Briefly, before deproteinization and delipidation, 62.5 μL of 0.33 mM N-α-acetyl-L-tryptophan (Watanabe Chemical Industries, Ltd., Hiroshima, Japan) was added into 500 μL of plasma as internal standard.…”

Section: Deproteinization and Delipidation Of Plasma Samplesmentioning

confidence: 99%

Half-life of Glycated Tryptophan in the Plasma of Chickens

Makino

Kita

2018

J. Poult. Sci.

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Tryptophan, an essential amino acid, is enzymatically metabolized to two compounds, kynurenine and serotonin, and 95% of tryptophan is metabolized to kynurenine. As chickens have hyperglycemia and high temperature, tryptophan glycation occurs more easily in chickens than in mammals. Part of tryptophan is non-enzymatically converted to two types of glycated tryptophan, 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 these compounds are detected in the plasma of chickens, information on the half-life of PHP-THβC in the blood circulation is limited. Therefore, the present study aimed to measure the half-life of plasma PHP-THβC in chickens. PHP-THβC (114 nmol/0.2 mL/70 g body weight) was intravenously administered to chickens via the wing vein, and blood samples were collected at 0, 15, 30, 60, 180, 360, 720, and 1440 min after administration. Plasma concentrations of PHP-THβC were measured by liquid chromatography-mass spectrometry. Plasma PHP-THβC reached to a peak concentration of 16.1 μM at 30 min after administration, and then decreased rapidly to return to the physiological level (0 min) at 360 min after administration. The half-life of plasma PHP-THβC was calculated by non-linear regression analysis, and it was found to be 107 min. This study was the first to measure plasma half-life of glycated tryptophan.

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Detection of Two Types of Glycated Tryptophan Compounds in the Plasma of Chickens Fed Tryptophan Excess Diets

Cited by 8 publications

References 12 publications

Glycated Tryptophan in the Plasma of Chickens Fed Tryptophan-excess Diets

Glycated Tryptophan in the Plasma of Chickens Fed Tryptophan-excess Diets

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

Half-life of Glycated Tryptophan in the Plasma of Chickens

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