Plasma Amino Acid Response in Young Men Given Diets Devoid of Single Essential Amino Acids

Ozalp, I; Young, Vernon R.; Nagchaudhuri, J; Tontisirin, Kraisid; Scrimshaw, Nevin S.

doi:10.1093/jn/102.9.1147

Cited by 32 publications

(9 citation statements)

References 27 publications

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“…However, blood phenylalanine concentrations in HT1 have previously been reported to show a large diurnal variation, consistently being lower in the afternoon (Daly et al 2012), while previous reports showed that detection of deficient intake of essential amino acids can best be detected by comparing an overnight fasting and postprandial blood sample (Ozalp et al 1972). Further studies may therefore best include a differential overnight fasting to postprandial measurement.…”

Section: Discussionmentioning

confidence: 96%

Infants with Tyrosinemia Type 1: Should phenylalanine be supplemented?

et al. 2014

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Tyrosinemia type 1 (HT1) is an inborn error of tyrosine catabolism caused by fumarylacetoacetase deficiency. Biochemically, this results in accumulation of toxic metabolites including succinylacetone. Clinically, HT1 is characterized by severe liver, kidney, and neurological problems. Treatment with NTBC and dietary restriction of tyrosine and phenylalanine have strongly improved outcome, but impaired neurocognitive development has been reported. Whether impaired neurocognitive outcome results from high blood tyrosine or low blood phenylalanine concentrations is currently unknown. In this report, two HT1 newborns, diagnosed by neonatal screening, are presented. The first patient showed low phenylalanine concentrations, growth retardation, neurological impairments, and skin problems, clearly improving after institution of phenylalanine supplementation (~30 mg/kg/ day) at age 6 months, while both blood phenylalanine and tyrosine concentrations increased. In the second patient, phenylalanine supplementation (~20 mg/kg/day) was initiated as soon as low phenylalanine concentrations were observed at age 19 days. On this regimen, blood phenylalanine concentrations increased, and hypophenylalaninemia was less frequently observed than in the first patient, whereas blood tyrosine concentrations tended to increase. Clinically, no growth, neurological, or skin problems have been observed. The combination of knowledge obtained from these cases suggests that hypophenylalaninemia rather than hypertyrosinemia during the first months of life may impair neurocognitive development in young HT1 infants. Phenylalanine supplementation should really be considered in HT1 patients with consistently low blood phenylalanine concentrations during the first months of life. However, the minimal phenylalanine concentrations acceptable and the optimal phenylalanine supplementation regimen require further investigation.

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Section: Discussionmentioning

confidence: 96%

Infants with Tyrosinemia Type 1: Should phenylalanine be supplemented?

et al. 2014

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“…The shape of the response curve differed from those obtained previously (4) in rats fed by 10% casein diet containing graded levels of methionine and glycine singly. Many studies on animals (1-3, 7, 12-15) and men (16)(17)(18) have demonstrated that plasma amino acid concentrations can be utilized as response criteria for estimating the amino acid requirements. ZIMMERMAN and SCOTT (2) reported that plasma lysine of chicks does not accumulate when the dietary lysine is less than that required for maximum weight gain, at which point the plasma lysine level rises linearly.…”

Section: Discussionmentioning

confidence: 99%

The Relationship Between Weight Gain and Free Amino Acid Concentration of Plasma and Liver in Rats Fed a Diet Supplemented With Various Amounts of Lysine

Muramatsu

Takeuchi

Sakurai

1973

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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This study was conducted to determine the effect of feeding graded levels of dietary lysine on weight gain and free amino acid concentra tions in blood plasma and liver of weanling rats. Animals were fed on diets containing 11.6% wheat gluten (equivalent in nitrogen to a 10% casein diet) supplemented with graded levels of L-lysine HCl (0 to 10%) for 14 days. An outline of the results obtained follows: 1) Maximum weight gain was observed with the groups fed the lysine supplement in the 0.64 to 1.8% range. Growth declined with further in crease of dietary lysine.2) Blood and liver were sampled after decapitation 6 hr after the fi nal feeding on the 14th day, and amino acid concentrations were determined. Plasma lysine concentrations rose rapidly as dietary lysine increased and reached the maximum level with the 1.8% lysine supplementation. With the large supplement diet, the lysine con centrations maintained a plateau. Plasma threonine levels were high when dietary lysine was low.3) Similar responses of lysine and threonine concentrations in liver to the increase of dietary lysine was also observed, but the effect was markedly less than those of plasma. Most other amino acids in plasma and liver were nearly unchanged even when the dietary lysine was varied over a wide range.Extensive studies (1-3) have been made on the relationship between weight gain and the concentration of free lysine in the blood plasma of animals fed 277

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“…In mammals, the plasma concentration of free amino acids is markedly affected by nutritional conditions [24][25][26] ; this is particularly evident in portal blood. Therefore liver cells are in contact with highly variable concentrations of amino acids.…”

Section: Introductionmentioning

confidence: 99%

Physiological concentration of amino acids regulates insulin-like-growth-factor-binding protein 1 expression

Jousse

Bruhat

Ferrara

et al. 1998

Biochemical Journal

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Protein undernutrition is characterized by growth failure in young growing animals. Current evidence suggests that biosynthesis of insulin-like growth factor (IGF)-I and IGF-binding protein 1 (IGFBP-1) are key control points for nutritional regulation of growth. Here we examined the role of amino acid limitation in regulating the IGFBP-1 expression in the hepatic cell line. Our data show that leucine limitation strongly induces IGFBP-1 without affecting IGF-I and IGF-II expression in human HepG2 cells and in isolated rat hepatocytes. Depletion of arginine, cystine and all essential amino acids leads to induction of IGFBP-1 mRNA and protein expression in a dose-dependent manner. IGFBP-1 expression is significantly induced by leucine concentration in the range of that observed in the blood of rats fed a low-protein diet or in humans affected by kwashiorkor. Moreover, treatment of HepG2 cells with amino acids at a concentration reproducing the amino acid concentration found in portal blood of rats fed a low-protein diet leads to a significantly higher expression of IGFBP-1. These data represent the first demonstration that an amino acid limitation, as occurs during dietary protein deficiency, induces IGFBP-1 expression in hepatic cells. Therefore, amino acids by themselves can play, in concert with hormones, an important role in the control of gene expression.

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Plasma Amino Acid Response in Young Men Given Diets Devoid of Single Essential Amino Acids

Cited by 32 publications

References 27 publications

Infants with Tyrosinemia Type 1: Should phenylalanine be supplemented?

Infants with Tyrosinemia Type 1: Should phenylalanine be supplemented?

The Relationship Between Weight Gain and Free Amino Acid Concentration of Plasma and Liver in Rats Fed a Diet Supplemented With Various Amounts of Lysine

Physiological concentration of amino acids regulates insulin-like-growth-factor-binding protein 1 expression

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