Impact of prolonged leucine supplementation on protein synthesis and lean growth in neonatal pigs

Daniel A. Columbus, Julia Steinhoff-Wagner, Agus Suryawan, Hanh V. Nguyen, Adriana Hernandez-Garcia, Marta L. Fiorotto, Teresa A. Davis

Research output: Contribution to journalArticlepeer-review

35 Scopus citations

Abstract

Most low-birth weight infants experience extrauterine growth failure due to reduced nutrient intake as a result of feeding intolerance. The objective of this study was to determine whether prolonged enteral leucine supplementation improves lean growth in neonatal pigs fed a restricted protein diet. Neonatal pigs (n = 14–16/diet, 5 days old, 1.8 ± 0.3 kg) were fed by gastric catheter a whey-based milk replacement diet with either a high protein (HP) or restricted protein (RP) content or RP supplemented with leucine to the same level as in the HP diet (RPL). Pigs were fed 40 ml·kg body wt-1·meal-1 every 4 h for 21 days. Feeding the HP diet resulted in greater total body weight and lean body mass compared with RP-fed pigs (P < 0.05). Masses of the longissimus dorsi muscle, heart, and kidneys were greater in the HP- than RP-fed pigs (P < 0.05). Body weight, lean body mass, and masses of the longissimus dorsi, heart, and kidneys in pigs fed the RPL diet were intermediate to RP- and HP-fed pigs. Protein synthesis and mTOR signaling were increased in all muscles with feeding (P < 0.05); leucine supplementation increased mTOR signaling and protein synthesis rate in the longissimus dorsi (P< 0.05). There was no effect of diet on indices of protein degradation signaling in any tissue (P < 0.05). Thus, when protein intake is chronically restricted, the capacity for leucine supplementation to enhance muscle protein accretion in neonatal pigs that are meal-fed milk protein-based diets is limited.

Original languageEnglish
Pages (from-to)E601-E610
JournalAmerican Journal of Physiology - Endocrinology and Metabolism
Volume309
Issue number6
DOIs
StatePublished - 15 Sep 2015
Externally publishedYes

Keywords

  • Mammalian target of rapamycin
  • Muscle
  • Newborn
  • Protein degradation
  • Protein synthesis

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