Biomedical subjects

T E Chapman

Publications and source records attributed to T E Chapman.

At least 19 recordsLinked to original sources

PubMed2001

Performance characteristics of a carbon isotope ratio method for detecting doping with testosterone based on urine diols: controls and athletes with elevated testosterone/epitestosterone ratios.

BACKGROUND: Carbon isotope ratio methods are used in doping control to determine whether urinary steroids are endogenous or pharmaceutical. METHODS: Gas chromatography-combustion-isotope ratio mass spectrometry (GC-C-IRMS) was used to determine the delta(13)C values for 5 beta-androstane-3 alpha,17 beta-diyl diacetate (5 beta A), 5 alpha-androstane-3 alpha,17 beta-diyl diacetate (5 alpha A), and 5 beta-pregnane-3 alpha,20 alpha-diyl diacetate (5 beta P) in a control group of 73 healthy males and 6 athletes with testosterone/epitestosterone ratios (T/E) >6. RESULTS: The within-assay precision SDs for 5 beta A, 5 alpha A, and 5 beta P were +/- 0.27 per thousand, +/- 0.38 per thousand, and +/- 0.28 per thousand, respectively. The between-assay precision SDs ranged from +/- 0.40 per thousand to +/- 0.52 per thousand. The system suitability and batch acceptance scheme is based on SDs. For the control group, the mean delta(13)C (SD) values were -25.69 per thousand (+/- 0.92 per thousand), -26.35 per thousand (+/- 0.68 per thousand), and -24.26 per thousand (+/- 0.70 per thousand), for 5 beta A, 5 alpha A, and 5 beta P, respectively. 5 beta P was greater than 5 beta A and 5 alpha A (P <0.01), and 5 beta A was greater than 5 alpha A (P <0.01). The means - 3 SD were -28.46 per thousand, -28.39 per thousand, and -26.37 per thousand for 5 beta A, 5 alpha A, and 5 beta P, respectively. The maximum difference between 5 beta P and 5 beta A was 3.2 per thousand, and the maximum 5 beta A/5 beta P was 1.13. Three athletes with chronically elevated T/Es had delta(13)C values consistent with testosterone administration and three did not. CONCLUSIONS: This GC-C-IRMS assay of urine diols has low within- and between-assay SDs; therefore, analysis of one urine sample suffices for doping control. The means, SDs, +/-3 SDs, and ranges of delta(13)C values in a control group are established. In comparison, testosterone users have low 5 beta A and 5 alpha A, large differences between 5 beta A or 5 alpha A and 5 beta P, and high 5 beta A/5 beta P and 5 alpha A/5 beta P ratios.

Androstane-3,17-diol↗

PubMed2000

A rapid screening assay for measuring urinary androsterone and etiocholanolone delta(13)C ( per thousand) values by gas chromatography/combustion/isotope ratio mass spectrometry.

A gas chromatography/combustion/isotope ratio mass spectrometry (GC/C/IRMS) method is described and validated for measurement of delta(13)C values of the acetate derivatives of urinary etiocholanolone and androsterone. The analysis was performed with only 2 mL of urine. The sample preparation consisted of deconjugation with beta-glucuronidase, solid phase extraction, and derivatization with acetic anhydride and pyridine. The within-assay precision of two quality control (QC) urine samples ranged from 0.5 to 2.1 CV%. The between-assay precision in the same QC urines ranged from 1.7 to 3.4 CV%. Administration of testosterone enanthate to a subject resulted in a 6 per thousand decrease in delta(13)C values from -25 per thousand (baseline) to -31 per thousand. Two weeks after testosterone administration was discontinued, the delta(13)C values remained abnormally low while the urine testosterone/epitestosterone (T/E) ratio returned to less than 6. This relatively simple method is useful for rapidly screening a large number of urine samples, including those with T/E <6.

Adult↗

PubMed1996

Twenty-four-hour intravenous and oral tracer studies with L-[1-13C]phenylalanine and L-[3,3-2H2]tyrosine at a tyrosine-free, generous phenylalanine intake in adults.

The daily rates of whole-body phenylalanine oxidation and hydroxylation were determined in young men receiving [1-13C]phenylalanine and [2H2]tyrosine via primed, constant intravenous (n=3) or oral (n=5) infusion for 24 consecutive hours (12-h fast followed by 12-h fed period), and given a generous phenylalanine (100 mg.kg-1.d-1), tyrosine-free, but otherwise adequate L-amino acid-based diet for 6 d before the tracer study. Our hypothesis was that subjects would be in whole-body phenylalanine equilibrium. Estimates of the daily rates of phenylalanine oxidation (phe-ox) and hydroxylation (phe-OH) were significantly higher for the subjects receiving the oral compared with intravenous tracer (P<0.01 for both comparisons), with the estimates of phe-ox obtained with oral tracer during the 12-h fast period being close to those predicted from similar 24-h leucine kinetic studies. The precision of the agreement between the measured 24-h rates of phe-ox and phe-OH compared with the predicted daily rates by extrapolation from the last hour of the 12-h fast and fifth hour of the fed period was poor. From the 24-h data, daily phenylalanine balances were estimated to be positive for both the intravenous and oral tracer protocols, although it was less positive for the oral tracer group. These results imply that the [13C]phenylalanine probe underestimated whole-body irreversible loss of phenylalanine, and suggest that daily phenylalanine balance in earlier 24-h phenylalanine-tyrosine tracer studies at low phenylalanine intakes may have been overestimated. Studies involving [13C]tyrosine as tracer will be required to further assess whole-body aromatic amino acid balance.

Administration, Oral↗

PubMed1996

Kinetics of plasma arginine and leucine in pediatric burn patients.

The dynamic status of whole-body arginine and leucine was investigated in eight severely burned (mean 55% of body surface area) pediatric patients (mean age 5.3 y) at a mean of 16 d after their initial injury. Plasma amino acid kinetics were estimated by using primed constant intravenous infusions of L-[13C-guanidino]arginine and L-[I-13C]leucine given for 4 h. Each patient was studied twice within 2 d. The patients were studied either in a "basal" state, which involved removal of amino acids from the total parenteral nutrition (TPN) solution for 8 h before the tracer study, or while receiving complete TPN. Nitrogen intake was 0.58 +/- 0.08 g.kg-1.d-1 with nonprotein energy intake equivalent to 197 +/- 29 kJ.kg-1.d-1. Plasma leucine and arginine fluxes (mumol.kg-1.h-1) were 208 +/- 35 and 108 +/- 18 for basal and 290 +/- 38 and 195 +/- 22 for TPN periods, respectively. Leucine oxidation was 42 +/- 7 and 59 +/- 9 mumol.kg-1.h-1 for basal and TPN periods, respectively, indicating a higher rate of leucine loss in the absence of a leucine intake than that expected for healthy individuals. The arginine kinetic data implied little net de novo arginine synthesis and further suggested increased rates of arginine degradation from burn injury. The expected rate of urea excretion, based on the basal rate of leucine oxidation, agreed closely with the measured output of urinary urea. These findings suggest that arginine is a conditionally indispensable amino acid for maintaining body protein homeostasis and nutrition in severely burned pediatric patients. The metabolic response of these children appears to be quantitatively similar to that for severely burned adult patients.

Amino Acids↗

PubMed1996

Diurnal pattern of the interrelationships among leucine oxidation, urea production, and hydrolysis in humans.

We investigated in six healthy adult men, who received an adequate intake of protein (1 g.kg-1.day-1), the relationship among urea production, excretion, and hydrolysis. At the end of a 6-day diet-adjustment period, subjects were studied using a 24-h continuous intravenous [1-13C]leucine and [15N,15N]urea tracer protocol (A. E. El-Khoury, N. K. Fukagawa, M. Sánchez, R. H. Tsay, R. E. Gleason, T. E. Chapman, and V. R. Young. Am. J. Clin. Nutr. 59: 1000-1011, 1994) to determine rates of irreversible protein nitrogen loss and urea kinetics. By combining leucine and urea kinetic data, we found a significant degree of urea hydrolysis over the 24-h period but no evidence to support the thesis that there is a net retention or "salvage" of the urea nitrogen liberated. Our measurements revealed little or no urea hydrolysis during the fed 12-h period of the 24-h tracer protocol but substantial hydrolysis during the 12-h fasting phase. Furthermore, a mass balance model and calculations (APPENDIX) indicated that nitrogen salvage, if any, is quantitatively indistinguishable from insensible nitrogen losses and aggregate estimation errors, accounting for no more than 5% of the nitrogen intake. We conclude that urea hydrolysis, via the intestinal microflora, although representing a component of the overall cycles of nitrogen flow within the body, does not contribute via a net retention of amino nitrogen to the maintenance of body nitrogen homeostasis in healthy adults consuming an adequate diet.

Adult↗

PubMed1995

Plasma arginine and leucine kinetics and urea production rates in burn patients.

We measured plasma arginine and leucine kinetics and rates of urea production (appearance) in 12 severely burned patients (mean body surface burn area, 48%) during a basal state (low-dose intravenous glucose) and while receiving routine, total parenteral nutrition ([TPN] fed state) including an L-amino acid mixture, supplying a generous level of nitrogen (mean, 0.36 g N.kg-1.d-1). The two nutritional states were studied in random order using a primed 4-hour constant intravenous tracer infusion protocol. Stable-nuclide-labeled tracers were L-[guanidino-13C]arginine, L-[1-13C]leucine, [18O]urea, and NaH13CO3 (prime only), with blood and expired air samples drawn at intervals to determine isotopic abundance of arginine, citrulline, ornithine, alpha-ketoisocaproate ([KIC] for leucine), and urea in plasma and 13CO2 in breath. Results are compared with data obtained in these laboratories in healthy adults. Leucine kinetics (flux and disappearance into protein synthesis) indicated the expected higher turnover in burn patients than in healthy controls. Mean leucine oxidation rates are also higher and compared well with values predicted from urea production rates, provided that urea nitrogen recycling via intestinal hydrolysis is taken into account. The plasma urea flux was also higher than for normal subjects. Arginine fluxes as measured in the systemic whole body, via the plasma pool, were correspondingly higher in burned patients than in healthy controls and were in good agreement with values predicted from leucine-KIC kinetics. However, systemic whole-body arginine flux measured via the plasma pool was only 20% of the arginine flux estimated from the urea flux plus the rate of protein synthesis.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗

PubMed1995

Phenylalanine and tyrosine kinetics in young men throughout a continuous 24-h period, at a low phenylalanine intake.

We determined the daily rates of whole-body phenylalanine oxidation (phe-Ox) and hydroxylation (phe-OH) in young men receiving [1-13C]phenylalanine and [2H2]tyrosine via primed, constant intravenous (n = 5) or oral (n = 7) infusions for a consecutive 24 h (12-h fast followed by 12-h fed period), and given a low-phenylalanine (21.9 mg.kg-1.d-1), no-tyrosine, but otherwise adequate L-amino acid-based diet for 6 d before the tracer study. Estimates of the daily rates of phe-Ox and phe-OH were significantly higher (P < 0.001) for the subjects receiving the oral tracer, with estimates of phe-Ox obtained with the oral tracer during the 12-h fast period being close to those predicted from similar 24-h leucine kinetic studies (Am J Clin Nutr 1994;59:1000-11). There was generally poor agreement between the measured 24-h rates of phe-Ox and phe-OH compared with the daily rates as predicted from the last hour of the 12-h fast and 5th hour of feeding. From the 24-h data, daily phenylalanine balances were estimated to be positive with the intravenous-tracer protocol and negative with the oral-tracer group. Our results question the adequacy of current international recommendations for aromatic amino acid requirements in healthy adults.

Administration, Oral↗

PubMed1995

Plasma arginine, citrulline, and ornithine kinetics in adults, with observations on nitric oxide synthesis.

The plasma fluxes of ornithine (Orn), arginine (Arg), and citrulline (Cit) and rate of conversion of labeled ornithine-to-citrulline (QOrn-->Cit) were estimated in six healthy adult men receiving an arginine-rich or arginine-free L-amino acid-based diet, each for 6 days. On day 7 an 8-h (3-h fast, 5-h fed) primed continuous intravenous infusion of L-[guanido-15N,15N] arginine, L-[ureido-13C]citrulline, L-[5,5,2H2]ornithine, and L-[5,5,5-2H3]leucine was conducted. Mean citrulline fluxes (mumol.kg-1.h-1) were 10.4-13.6 for the various conditions and/or diets and remained unchanged (P > 0.05). Arginine flux was lowered (P < 0.01) by 38% for fed state during arginine-free period. Ornithine fluxes for arginine-rich were (P < 0.01) reduced with the arginine-free diet. Rates of QOrn-->Cit declined by 30% (P < .05) during the fed arginine-free period. Short-term restriction in the dietary supply of arginine did not alter the rate of whole body nitric oxide synthesis. One subject showed a very high output of nitrate on arginine-free diet (6 times average for remaining subjects).

Adult↗

PubMed1995

Whole body arginine metabolism and nitric oxide synthesis in newborns with persistent pulmonary hypertension.

Despite the potential relevance of the L-arginine-nitric oxide (NO) pathway in the pathophysiology of pulmonary hypertension, no in vivo studies of the kinetics of arginine and NO have been conducted previously in this population. The terminal guanidino N-atom of L-arginine is the precursor for NO, which is oxidized to the stable inorganic nitrogen oxides, nitrite (NO2-) and nitrate (NO3-). Thus, synthesized NO is detected in serum or urine as NO2- and NO3-. The purpose of this investigation was to compare studies of whole body arginine metabolism twice in nine patients with persistent pulmonary hypertension of the newborn (PPHN), using a primed constant i.v. infusion of L-[guanidino-15N2,5,5(2)H2]arginine and L-[5,5,5(2)H3]leucine, first during acute pulmonary vasoconstriction and again during convalescence, and thereby to characterize quantitative aspects of whole body arginine kinetics and NO production, as estimated from the rate of transfer of the 15N-guanidino-label of arginine to urinary nitrate (15NO3-). Arginine flux rates were 84.1 +/- 8.6 mumol.kg-1 h-1 (mean +/- SEM) during acute pulmonary hypertension and increased to 125 +/- 13.2 (p < 0.05) during convalescence, whereas leucine fluxes were unchanged (168.5 +/- 15 versus 178.8 +/- 10.2 mumol.kg-1 h-1), and comparable to those reported in healthy newborns. During convalescence total urinary nitrate excreted increased by 66% (p < 0.05), urinary 15NO3- increased from 0.29 +/- 0.07 to 0.74 +/- 0.15 mumol.d-1 (p < 0.05), and the rate of plasma arginine conversion to NO increased from 10.3 +/- 2.2 to 45.6 +/- 13 mumol.d-1 (p < 0.05).(ABSTRACT TRUNCATED AT 250 WORDS)

Arginine↗

PubMed1994

The plasma flux and oxidation rate of ornithine adaptively decline with restricted arginine intake.

We hypothesized recently that arginine homeostasis is achieved in humans largely by modulating the rate of arginine degradation. We have tested this hypothesis further by measuring in vivo the whole body rate of conversion of arginine to ornithine and ornithine oxidation in six healthy young adults. Subjects received for 6 days an L-amino acid-based diet supplying an arginine-rich or arginine-free intake and on day 7, following an overnight fast, an 8-h tracer protocol (first 3 h, fast state; next 5 h, fed state) was conducted; L-[guanidino-15N2; 5,5-2H]arginine and L-[5-13C]ornithine were given as primed, constant intravenous tracers; measurements of the abundances of various isotopologs of arginine, ornithine, and citrulline in plasma were made, and from these the various kinetic parameters of the metabolism of these amino acids were derived. Arginine and ornithine fluxes were significantly (P < 0.001) reduced in the fed state with arginine-free feeding. The rates of conversion (mumol.kg-1.h-1; mean +/- SD) of plasma arginine to ornithine for arginine-rich were 12.9 +/- 2.6 and 24.7 +/- 4.8 for fast and fed states. These values were 11.1 +/- 3.5 and 9.6 +/- 1.2 (P > 0.05 and P < 0.001), respectively, with an arginine-free diet. [13C]Ornithine oxidation was reduced (P < 0.001) by 46% during the fed state when the arginine-free diet was given. The findings strengthen our hypothesis that homeostasis of arginine metabolism in the human host depends importantly upon a regulation in the rate of arginine degradation with, perhaps, little involvement in the de novo net rate of arginine synthesis.

Adult↗

PubMed1994

Plasma arginine kinetics in adult man: response to an arginine-free diet.

To explore the response of whole-body arginine metabolism to a change in arginine intake, plasma arginine kinetics were investigated in eight healthy adult men who received an L-amino acid diet supplying an Arg-rich or Arg-free intake for 6 days before undergoing a tracer study on day 7. The tracer protocol lasted for 8 hours. For the first 3 hours subjects remained in the postabsorptive (fasted) state, and during the following 5 hours they consumed small meals at 30-minute intervals. Primed continuous intravenous infusions of L-[guanidino-13C]arginine, L-[5,5,5-2H3]leucine, and [15N2]urea were administered to estimate plasma amino acid fluxes and the rate of urea production. For the fasted and fed states, plasma arginine fluxes (mumol.kg-1.h-1, mean +/- SD) were 69 +/- 8 and 87 +/- 12 (P < .01), respectively, for the Arg-rich diet and 63 +/- 14 and 51 +/- 7 (P < .01, from Arg-rich) for the Arg-free diet. Compared with the Arg-rich results, fed-state plasma arginine and ornithine concentrations were decreased (P < .01) and citrulline concentration was increased (P < .01) during the Arg-free diet period. Leucine fluxes and rates of urea production did not differ between the diet groups. The lower fed-state arginine flux in subjects receiving the Arg-free compared with the Arg-rich diet appears to be entirely due to the decreased rate of entry of arginine from the intestine in the former group.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗

PubMed1994

Validation of the tracer-balance concept with reference to leucine: 24-h intravenous tracer studies with L-[1-13C]leucine and [15N-15N]urea.

The validity of tracer-derived estimates of whole-body leucine balance was investigated. Seven healthy young adult subjects received an adequate protein diet for 6 d; at 1800 on the last day, L-[1-13C]leucine and [15N-15N]urea were given as primed, continuous intravenous infusions for 24 h. Subjects were in a fasting state for the first 12 h and at 0600 on day 7 they then received hourly 10 equal meals to achieve a fed state. Total leucine intake (diet plus tracer) was 89.4 mg.kg-1.d-1. Mean daily leucine oxidation was equivalent to 89.5 +/- 3.3 mg leucine/kg. The predicted daily oxidation rate, from measurements made during the last hour of the fast and the fifth hour of the fed period, was 91.2 +/- 5.8 mg/kg (P = 0.25 from measured). Measured and predicted whole-body leucine balances were 0.76 +/- 2.99 and -0.98 +/- 5.54 mg/kg, respectively (P = 0.25). Urea production exceeded urea excretion by 20%; daily protein oxidation was the same when estimated from leucine oxidation or nitrogen excretion. Thus, the tracer-balance concept is valid, and reliable predictions of total daily leucine oxidation and whole-body leucine balance can be obtained from short-term measurements of leucine oxidation during fasted and fed states.

Adult↗

PubMed1994

The 24-h pattern and rate of leucine oxidation, with particular reference to tracer estimates of leucine requirements in healthy adults.

Daily leucine oxidation and derived values for whole-body leucine balance, obtained by continuous measurement throughout a 24-h period, were compared with those predicted from short-term measurements during fasted and fed states in five healthy adults studied during two 6-d experimental diet periods, each immediately followed by a 24-h continuous intravenous tracer infusion of L-[1-13C]leucine. Leucine intake was either 14 or 38.3 mg.kg-1.d-1. Mean measured daily leucine oxidation (mg leucine.kg-1.d-1) was 27.8 and 45.2 for the 14- and 38.3-mg intakes, respectively. Oxidation rates predicted by extrapolation of rates measured during the final hour of fasting (15 h after last meal) and the 5th h of feeding were approximately 12% higher (P < 0.01) than measured rates for both diets. For the prediction based on the 12th h of fasting and 5th h of feeding, it was 4% higher or 0.4% lower than measured rates for the 38.3- and 14- mg intakes, respectively. Hence, relatively small differences exist between measured vs predicted estimates of daily leucine oxidation and balance. These studies support previous conclusions that the current, international requirement value for leucine in healthy adults is far too low.

Adult↗

PubMed1994

Source and amount of dietary nonspecific nitrogen in relation to whole-body leucine, phenylalanine, and tyrosine kinetics in young men.

We studied the effects of amount and source of nonspecific nitrogen (NSN) on the oxidation of leucine and hydroxylation of phenylalanine. In phase 1, seven adult males received for 6 d diets providing indispensable amino acid intakes to meet the 1985 FAO/WHO/UNU (FAO) requirements or our proposed requirement values (MIT). During one diet period with each diet, the NSN of the basal diets (total nitrogen intake: 107 mg N.kg-1.d-1) was increased to a total of 160 mg N.kg-1.d-1. On the morning of day 7, an 8-h constant intravenous tracer-infusion protocol (3-h fast; 5-h fed state) was conducted with L-[1-13C]leucine, L-[ring-2H5]phenylalanine, and L-[3,3,2H2]-tyrosine as tracers. In phase 2, six subjects were given three diets for 6 d, supplying 107 mg N.kg-1.d-1; NSN was a mixture of dispensable amino acids in which glutamine accounted for 0%, 12.5%, and 100% of total NSN. Leucine oxidation and phenylalanine hydroxylation rates and whole-body leucine and phenylalanine balances were unaffected by addition of supplemental NSN to the diets in phase 1 or by amino acid source of NSN in phase 2. Leucine and phenylalanine balances were lower (P < 0.05) for FAO compared with MIT diets.

Adult↗

PubMed1994

Phenylalanine and tyrosine kinetics for different patterns and indispensable amino acid intakes in adult humans.

In a previous paper (Am J Clin Nutr 1993;58:670-83) we described results for plasma amino acid changes, leucine kinetics, and body leucine and nitrogen balance in 20 young men receiving diets for 3 wk. The diets were based on the 1985 FAO/WHO/UNU amino acid requirement pattern (modified FAO diet; n = 7), the Massachusetts Institute of Technology (MIT) requirement pattern (MIT diet; n = 7), or the egg-protein pattern (Egg diet; n = 6). It was concluded, in comparison with the MIT and Egg diets, that the modified FAO diet was not capable of maintaining body amino acid homeostasis or balance. Here we report results from tracer studies with L-[O-2H5]phenylalanine and [2H2]tyrosine that were carried out within the same experiment. The modified FAO diet failed to maintain a mean body phenylalanine balance as determined from rates of phenylalanine hydroxylation (corrected for deuterium-isotopekinetic effects); balance was achieved with the MIT and Egg diets. These results further underscore the inadequacy of the internationally proposed amino acid requirement pattern for healthy adults. We recommend interim use of the MIT, tentative amino acid requirement values in all considerations of adult human amino acid requirements and nutrition.

Adult↗

PubMed1994

Plasma proline and leucine kinetics: response to 4 wk with proline-free diets in young adults.

The effects of removing proline from the diet on plasma leucine and proline kinetics were investigated. After a 1-wk control period, during which young adult men received a diet containing a complete L-amino acid mixture, seven subjects were given for 4 wk a diet devoid of proline (group 1); six received a diet devoid of proline, arginine, aspartate, glutamate, and serine (group 2); and seven continued with the complete diet (group 3). At the end of the control and 4-wk periods subjects were given a continuous, (3-h fast, 5-h fed) intravenous infusion of L-[1-13C]leucine and L-[5,5-2H]proline. Plasma proline was reduced significantly, especially during the fed state, in groups 1 and 2 after the 4-wk diet periods. Small but statistically significant (P < 0.05) reductions occurred in nonoxidative leucine disappearance and leucine appearance during the fasted state in group 2. Proline fluxes decreased by approximately 50% in fasted and fed states in groups 1 and 2. Mean de novo proline synthesis during the fasted state declined markedly (P < 0.05) after 4 wk in groups 1 and 2.

Adult↗

PubMed1994

Methionine and cysteine kinetics at different intakes of cystine in healthy adult men.

We investigated plasma methionine and cysteine kinetics in eight healthy adult men receiving for 6 d each of five L-amino acid diets supplying 13 mg methionine.kg-1.d-1 without cystine or 6.5 mg methionine.kg-1.d-1 plus 0, 5.2, 10.5, or 20.9 mg cystine.kg-1.d-1. On the morning of day 7, primed, constant intravenous infusions of L-[2H3-methyl, 1-13C]methionine and L-[3,3-2H]cysteine were given for 8 h (for the first 3 h subjects remained in a fasted state and for the next 5 h received small, equal meals at hourly intervals to achieve a fed state). Methionine and cysteine fluxes and rate of methionine oxidation were estimated from plasma methionine and cysteine labeling and 13C in expired air. Methionine oxidation declined (P < 0.05) with lowered methionine intake. Cysteine flux was similar across diets and dietary cystine did not affect tracer methionine oxidation. If there is a sparing effect of dietary cystine on the methionine requirement in adults, it probably takes place during the "first-pass" removal of these amino acids within the splanchnic region.

Adult↗

PubMed1994

Phenylalanine and tyrosine kinetics in critically ill children with sepsis.

To better understand the impact of severe illness on the amino acid economy and nutritional needs of pediatric patients, we studied plasma phenylalanine and tyrosine kinetics in eleven critically ill patients (six full-term newborns and five young infants). Within 48 h of the diagnosis of sepsis they were given primed constant i.v. infusions of L-[1-13C]phenylalanine and L-[3,3,2H2]tyrosine for 4 h. Routine nutritional support continued during this period by parenteral administration of dextrose, lipid emulsion, and an amino acid mixture low in tyrosine. Phenylalanine and tyrosine fluxes and rate of phenylalanine hydroxylation did not differ significantly between the two age groups, and so the data were combined for evaluation. For the entire group, values (mumol.kg-1.h-1; mean +/- SD) for phenylalanine and tyrosine fluxes and rate of phenylalanine hydroxylation were 132 +/- 24, 66 +/- 16, and 29 +/- 12, respectively. Plasma phenylalanine to tyrosine concentration ratio was 1.67 +/- 0.6. From a comparison of the rate of phenylalanine hydroxylation with measured phenylalanine intakes, it was concluded that their routine, clinical nutritional support was inadequate to achieve body phenylalanine balance. In comparison with published data, the relative rate of phenylalanine hydroxylation appears to be high. We speculate that tyrosine is a conditionally indispensable amino acid under these conditions; it would be desirable to establish the intake levels and ratio of phenylalanine to tyrosine that effectively support aromatic amino acid balance in these critically ill patients.

Bacterial Infections↗