15N-tracer kinetic studies regarding whole body protein metabolism in very small preterm infants for evaluation of human milk fortifier

1988 ◽  
Vol 7 ◽  
pp. 11
1983 ◽  
Vol 64 (6) ◽  
pp. 611-616 ◽  
Author(s):  
P. B. Pencharz ◽  
L. Farri ◽  
A. Papageorgiou

1. The effects of human milk and two low-protein formulae on the protein metabolism of 30 preterm appropriate for gestational age infants, birth weight 1.5-2.0 kg, were studied. The compositions of the two formulae were identical except for the protein source, with either casein or whey predominant. 2. The three diet groups all received similar nitrogen (390 mg of N day−1 kg−1) and energy intakes (500 kJ day−1 kg−1). 3. Growth rates for length and weight were comparable and approximated to intrauterine growth. Nitrogen absorption and net nitrogen utilization were enhanced in the human-milk-fed group. However, there were no differences in nitrogen retention, which averaged 274 mg day−1 kg−1 and approximated to intrauterine accretion rates. 4. Rates of whole-body nitrogen flux, protein synthesis and breakdown in the human-milk group were increased by 43–54% over the values seen in either of the two formula-fed groups (P < 0.01). No differences were seen between the two formula groups. 5. No differences were seen in urine 3-methylhistidine excretion between the three study groups. 6. Our results suggest significant differences in the whole-body protein metabolism of formula-fed infants compared with human-milk-fed infants.


Author(s):  
Jorn Trommelen ◽  
Andrew M. Holwerda ◽  
Philippe J. M. Pinckaers ◽  
Luc J. C. van Loon

All human tissues are in a constant state of remodelling, regulated by the balance between tissue protein synthesis and breakdown rates. It has been well-established that protein ingestion stimulates skeletal muscle and whole-body protein synthesis. Stable isotope-labelled amino acid methodologies are commonly applied to assess the various aspects of protein metabolism in vivo in human subjects. However, to achieve a more comprehensive assessment of post-prandial protein handling in vivo in human subjects, intravenous stable isotope-labelled amino acid infusions can be combined with the ingestion of intrinsically labelled protein and the collection of blood and muscle tissue samples. The combined application of ingesting intrinsically labelled protein with continuous intravenous stable isotope-labelled amino acid infusion allows the simultaneous assessment of protein digestion and amino acid absorption kinetics (e.g. release of dietary protein-derived amino acids into the circulation), whole-body protein metabolism (whole-body protein synthesis, breakdown and oxidation rates and net protein balance) and skeletal muscle metabolism (muscle protein fractional synthesis rates and dietary protein-derived amino acid incorporation into muscle protein). The purpose of this review is to provide an overview of the various aspects of post-prandial protein handling and metabolism with a focus on insights obtained from studies that have applied intrinsically labelled protein under a variety of conditions in different populations.


1981 ◽  
Vol 61 (2) ◽  
pp. 217-228 ◽  
Author(s):  
E. B. Fern ◽  
P. J. Garlick ◽  
Margaret A. McNurlan ◽  
J. C. Waterlow

1. Four normal adults were given [15N]-glycine in a single dose either orally or intravenously. Rates of whole-body protein turnover were estimated from the excretion of 15N in ammonia and in urea during the following 9 h. The rate derived from urea took account of the [15N]urea retained in body water. 2. In postabsorptive subjects the rates of protein synthesis given by ammonia were equal to those from urea, when the isotope was given orally, but lower when an intravenous dose was given. 3. In subjects receiving equal portions of food every 2 h rates of synthesis calculated from ammonia were much lower than those from urea whether an oral or intravenous isotope was given. Comparison of rates obtained during the post-absorptive and absorptive periods indicated regulation by food intake primarily of synthesis when measurements were made on urea, but regulation primarily of breakdown when measurements were made on ammonia. 4. These inconsistencies suggest that changes in protein metabolism might be assessed better by correlating results given by different end-products, and it is suggested that the mean value given by urea and ammonia will be useful for this purpose.


1987 ◽  
Vol 43 (6) ◽  
pp. 505-512 ◽  
Author(s):  
Anthony P. Borzotta ◽  
Malcolm B. Clague ◽  
Ivan D.A. Johnston

PEDIATRICS ◽  
2012 ◽  
Vol 130 (4) ◽  
pp. e928-e935 ◽  
Author(s):  
F. Moya ◽  
P. M. Sisk ◽  
K. R. Walsh ◽  
C. L. Berseth

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