Protein synthesis and eukaryotic initiation factor (eIF) activation are increased in skeletal muscle of neonatal pigs parenterally infused with amino

Studies were carried out to determine the effect of beta-glucanase supplementation to hulless barley-soybean meal (HB+SBM) or wheat-soybean meal (W+SBM) diets on the digestibilities of GE, CP, beta-glucans, and amino acids. Twelve barrows, average BW 7.3 kg, were fitted with a simple T-cannula at the distal ileum, approximately 5 cm from the ileo-cecal sphincter. After a 7-d recuperation period, six pigs were allotted to each dietary treatment according to a two-period crossover design. Both diets were formulated to contain 20% CP without and with supplementation of .2% beta-glucanase. beta-glucanase refers to a mixture of enzymes with endo- and exo-beta-glucanase and beta-glucosidase activities. Chromic oxide was included as a digestibility marker. The pigs were fed three times daily at 0800, 1600, and 2400 and the daily allowance was offered at a rate of 5% of BW. Each experimental period lasted 9 d. Feces were collected for 48 h on d 6 and 7 and ileal digesta for a total of 24 h on d 8 and 9. beta-glucanase supplementation to the HB+SBM diet increased (P < .05 or P < .01) the ileal digestibilities of GE, CP, beta-glucans, and the majority of the amino acids and the fecal digestibilities of GE, CP, and all amino acids measured; the fecal digestibility of beta-glucans in the HB+SBM diet was not affected by beta-glucanase supplementation. There was no effect (P > .05) of beta-glucanase supplementation to the W+SBM diet on the ileal digestibilities of any criteria measured except for beta-glucans (P < .05). The supplementation of beta-glucanase to the W+SBM diet increased (P < .05) the fecal digestibility of energy but not (P > .05) the other criteria measured. Copyright © . .

Orogastric tube feeding, using either continuous or intermittent bolus delivery, is common in infants for whom normal feeding is contraindicated. To

Genomic investigations in animals have begun to reveal the metabolic and physiological functions of genes and protein products. However, a thorough understanding of the genomic roadmaps will require investigative approaches that yield qualitative and quantitative information on the activities, fluxes, and connectivity of pathways involved in nutrient use in farm animals; that is, the metabolic phenotype. Recently, the commercial availability of stable isotope (¹³C, ¹⁵N, ²H)-labeled compounds and highly accurate mass spectrometers has made it possible to probe the details of metabolic pathways involved in macronutrient use. For years, the biological sciences have exploited uniformly ¹³C-labeled substrates (e.g., glucose, amino acids, nucleic acids) and ¹³C-mass isotopomer distribution (MID) in their metabolic investigations, whereas their use in the animal sciences is very limited. When [U-¹³C] substrates are fed, infused, or added to cell incubations, the ¹³C-skeletons distribute throughout metabolic networks. ¹³C-Mass isotopomer distribution in intermediates and end products of the pathways provides a signature of the fluxes and activities of pathway enzymes traveled by the precursor molecule. This paper highlights aspects of animal nutrition and metabolism in which [U-¹³C] substrates and MID can be applied to investigations of amino acid, carbohydrate, and fat metabolism. We will focus on [U-¹³C] glucose as a tracer in chickens, fish, sheep, and cell cultures to investigate the interconnectivity of the pathways of macronutrient and nucleic acid metabolism, and provide demonstration of the central position of the Krebs cycle in preserving metabolic flexibility via anaplerotic and cataplerotic sequences. Exploitation of this approach in animal sciences offers endless opportunities to provide missing details of the biochemical networks of nutrient use that may prove to be strictly under genomic control.

Orogastric tube feeding is indicated for neonates with impaired ability to ingest and can be administered by intermittent bolus or continuous schedule. Our aim was to determine whether feeding modalities affect muscle protein deposition and to identify mechanisms involved. Neonatal pigs were overnight fasted (FAS) or fed the same amount of food continuously (CON) or intermittently (INT; 7 × 4 h meals) for 29 h. For 8 h, between hours 20 and 28, pigs were infused with [²H₅]phenylalanine and [²H₂]tyrosine, and amino acid (AA) net balances were measured across the hindquarters. Insulin, branched-chain AA, phenylalanine, and tyrosine arterial concentrations and whole body phenylalanine and tyrosine fluxes were greater for INT after the meal than for CON or FAS. The activation of signaling proteins leading to initiation of mRNA translation, including eukaryotic initiation factor (eIF)4E·eIF4G complex formation in muscle, was enhanced by INT compared with CON feeding or FAS. Signaling proteins of protein degradation were not affected by feeding modalities except for microtubule-associated protein light chain 3-II, which was highest in the FAS. Across the hindquarters, AA net removal increased for INT but not for CON or FAS, with protein deposition greater for INT. This was because protein synthesis increased following feeding for INT but remained unchanged for CON and FAS, whereas there was no change in protein degradation across any dietary treatment. These results suggest that muscle protein accretion in neonates is enhanced with intermittent bolus to a greater extent than continuous feeding, mainly by increased protein synthesis.

Infants unable to maintain oral feeding can be nourished by orogastric tube. We have shown that orogastric continuous feeding restricts muscle protein synthesis compared with intermittent bolus feeding in neonatal pigs. To determine whether leucine infusion can be used to enhance protein synthesis during continuous feeding, neonatal piglets received the same amount of formula enterally by orogastric tube for 25.25 h continuously (CON) with or without LEU or intermittently by bolus every 4 h (BOL). For the CON+LEU group, leucine pulses were administered parenterally (800 μmol·kg⁻¹·h⁻¹) every 4 h. Insulin and glucose concentrations increased after the BOL meal and were unchanged in groups fed continuously. LEU infusion during CON feeding increased plasma leucine after the leucine pulse and decreased essential amino acids compared with CON feeding. Protein synthesis in longissimus dorsi (LD), gastrocnemius, and soleus muscles, but not liver or heart, were greater in CON+LEU and BOL than in the CON group. BOL feeding increased protein synthesis in the small intestine. Muscle S6K1 and 4E-BP1 phosphorylation and active eIF4E·eIF4G complex formation were higher in CON+LEU and BOL than in CON but AMPKα, eIF2α, and eEF2 phosphorylation were unchanged. LC3-II-to-total LC3 ratio was lower in CON+LEU and BOL than in CON, but there were no differences in atrogin-1 and MuRF-1 abundance and FoxO3 phosphorylation. In conclusion, administration of leucine pulses during continuous orogastric feeding in neonates increases muscle protein synthesis by stimulating translation initiation and may reduce protein degradation via the autophagy-lysosome, but not the ubiquitin-proteasome pathway.