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Published on: June 25, 2010
Metabolism of threonine in newborn infants
Prabhu S Parimi1, Lourdes L Gruca, Satish C Kalhan
1Schwartz Center for Metabolism & Nutrition, Bell Greve Bldg., Room G-735, MetroHealth Medical Center, 2500 MetroHealth Drive, Cleveland, OH 44109, USA. pparimi@metrohealth.org
Insights
Newborn infants show higher threonine kinetics than adults. Threonine metabolism is linked to protein turnover, with oxidation increasing after feeding.
Area of Science:
- Biochemistry
- Human Physiology
- Nutritional Science
Background:
- Threonine is an essential amino acid crucial for protein synthesis and metabolism.
- Understanding threonine kinetics in newborns is vital for assessing nutritional status and growth.
- Limited data exists on threonine metabolism and its relationship to protein turnover in early infancy.
Purpose of the Study:
- To quantify threonine kinetics, its oxidative pathway, and its relationship with whole-body protein turnover in healthy term infants within the first 48 hours of life.
- To investigate the impact of fasting and formula feeding on threonine metabolism.
- To elucidate the primary pathway for threonine degradation in neonates.
Main Methods:
- Utilized stable isotope tracers ([U-(13)C(4),(15)N]threonine, [(2)H(5)]phenylalanine, and [(15)N]glycine) to measure threonine kinetics.
- Quantified threonine oxidation by measuring expired carbon dioxide (CO(2)) and (13)C enrichment.
- Assessed protein turnover by measuring the rate of appearance (R(a)) of threonine and phenylalanine.
Main Results:
- Threonine R(a) was significantly higher in newborns compared to adults (136 +/- 37 micromol.kg(-1).h(-1)).
- Formula feeding decreased threonine R(a) (P < 0.05), while increasing threonine oxidation (20% fasting vs. 26% fed, P < 0.05).
- A strong positive correlation existed between threonine and phenylalanine R(a) (r(2) = 0.65), suggesting linked protein turnover.
Conclusions:
- Newborns exhibit a higher threonine flux relative to phenylalanine, indicating increased turnover of threonine-enriched proteins.
- Threonine is primarily degraded via the glycine-independent serine/threonine dehydratase pathway.
- These findings provide critical insights into neonatal amino acid metabolism and nutritional requirements.
Abstract:
Threonine kinetics, threonine oxidative pathway, and the relationship between threonine and whole body protein turnover were quantified in 10 healthy term infants during the first 48 h after birth. The kinetic data were obtained 6 h after the last feed (fasting) and in response to formula feeding, using [U-(13)C(4),(15)N]threonine, [(2)H(5)]phenylalanine, and [(15)N]glycine tracers. The rate of carbon dioxide production (Vco(2)) and (13)C enrichment of the expired CO(2) were measured to quantify the rate of oxidation of threonine. The rate of appearance (R(a)) of threonine (136 +/- 37 micromol.kg(-1).h(-1)) was higher in newborn infants than that reported in adults. Formula feeding resulted in a significant decrease in threonine R(a) (P < 0.05). A significant positive correlation was seen between phenylalanine R(a) and threonine R(a), both during fasting and after formula feeding (r(2) = 0.65). In contrast to a 1:1 ratio of threonine and phenylalanine in mixed muscle protein, threonine R(a) relative to phenylalanine R(a) was 2.2 +/- 0.4. The fractional rate of threonine flux oxidized was 20% during fasting and 26% (P < 0.05) in response to nutrient administration. There was a significant correlation between plasma threonine concentration and threonine oxidation (r(2) = 0.75). No measurable incorporation of threonine in plasma glycine was seen. These data suggest that threonine is exclusively degraded by the glycine-independent serine/threonine dehydratase pathway. A higher flux of threonine relative to phenylalanine indicates higher turnover of threonine enriched proteins.
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