title: Evidence that phenylalanine hydroxylation rates are overestimated in neonatal subjects receiving total parenteral nutrition with a high phenylalanine content.
abstract: Recent publications have indicated that the parenterally fed neonate has a substantial ability to hydroxylate phenylalanine. Examination of these data suggests that, at high phenylalanine intakes, estimated rates of hydroxylation exceed rates of intake. This implies significant net tissue breakdown. However, the quantitative validity of the estimates of phenylalanine hydroxylation cannot be assessed without nitrogen balance data. We have recently developed a parenterally fed neonatal piglet model and have used this to study aromatic amino acid metabolism in piglets fed different amino acid solutions. Reappraisal of the data from these studies has allowed us to estimate both phenylalanine hydroxylation and tissue protein accretion. Piglets were parenterally fed Vamin [292 micromol of Phe x kg(-1) x h(-1), 26 micromol of Tyr x kg(-1) x h(-1)], Vaminolact + Phe [VLP, 277 micromol of Phe x kg(-1) x h(-1), 26 micromol Tyr x kg(-1) x h(-1)], or Vaminolact + glycyl-L-tyrosine [VLGT, 152 micromol of Phe x kg(-1) x h(-1), 159 micromol of Tyr x kg(-1) x h(-1)] for 8 d. Nitrogen balance was measured over the last 5 study d, and aromatic amino acid kinetics were determined using a primed continuous infusion of L-[1-4C]phenylalanine on d 8. Average body protein gain, derived from nitrogen balance, was 11 g x kg(-1) x d(-1). For the Vamin and VLP groups, the rates of phenylalanine hydroxylation were estimated to be 139 and 90% of intake, respectively. However, phenylalanine hydroxylation was only 16% of intake for the VLGT group. In view of the tissue protein accretion data, it appears that the rate of phenylalanine hydroxylation may be overestimated in neonates fed high phenylalanine parenteral nutrition. The extent to which the parenterally fed neonate can adapt to a high phenylalanine intake, by increasing the rate of phenylalanine hydroxylation, remains to be determined.
authors.affiliation: Department of Animal and Poultry Science, University of Guelph, Ontario, Canada.
authors.forename: J D
authors.initials: JD
authors.lastname: House
authors.forename: J M
authors.initials: JM
authors.lastname: Thorpe
authors.forename: L J
authors.initials: LJ
authors.lastname: Wykes
authors.forename: P B
authors.initials: PB
authors.lastname: Pencharz
authors.forename: R O
authors.initials: RO
authors.lastname: Ball
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D000831:Animals, Newborn / Q000378:metabolism*; D004527:Egg Proteins; D004573:Electrolytes; D005526:Food, Formulated; D005947:Glucose; D006801:Humans; D006900:Hydroxylation; D007225:Infant Food; D007700:Kinetics; D008297:Male; D008894:Milk Proteins; D008954:Models, Biological; D057947:Parenteral Nutrition Solutions; D010289:Parenteral Nutrition, Total; D010649:Phenylalanine / Q000032:analysis / Q000378:metabolism*; D011492:Protein Hydrolysates / Q000737:chemistry / Q000378:metabolism*; D012189:Retrospective Studies; D012996:Solutions; D013552:Swine
chemical_list: D000596:Amino Acids; D004527:Egg Proteins; D004573:Electrolytes; D008894:Milk Proteins; D057947:Parenteral Nutrition Solutions; D011492:Protein Hydrolysates; D012996:Solutions; C545824:amino-acid, glucose, and electrolyte solution; D010649:Phenylalanine; D005947:Glucose