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. 2009 May;37(1):97-104.
doi: 10.1007/s00726-008-0149-z. Epub 2008 Aug 6.

Differential regulation of protein synthesis by amino acids and insulin in peripheral and visceral tissues of neonatal pigs

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Differential regulation of protein synthesis by amino acids and insulin in peripheral and visceral tissues of neonatal pigs

Agus Suryawan et al. Amino Acids. 2009 May.

Abstract

The high efficiency of protein deposition during the neonatal period is driven by high rates of protein synthesis, which are maximally stimulated after feeding. In the current study, we examined the individual roles of amino acids and insulin in the regulation of protein synthesis in peripheral and visceral tissues of the neonate by performing pancreatic glucose-amino acid clamps in overnight-fasted 7-day-old pigs. We infused pigs (n = 8-12/group) with insulin at 0, 10, 22, and 110 ng kg(-0.66) min(-1) to achieve approximately 0, 2, 6 and 30 muU ml(-1) insulin so as to simulate below fasting, fasting, intermediate, and fed insulin levels, respectively. At each insulin dose, amino acids were maintained at the fasting or fed level. In conjunction with the highest insulin dose, amino acids were also allowed to fall below the fasting level. Tissue protein synthesis was measured using a flooding dose of L: -[4-(3)H] phenylalanine. Both insulin and amino acids increased fractional rates of protein synthesis in longissimus dorsi, gastrocnemius, masseter, and diaphragm muscles. Insulin, but not amino acids, increased protein synthesis in the skin. Amino acids, but not insulin, increased protein synthesis in the liver, pancreas, spleen, and lung and tended to increase protein synthesis in the jejunum and kidney. Neither insulin nor amino acids altered protein synthesis in the stomach. The results suggest that the stimulation of protein synthesis by feeding in most tissues of the neonate is regulated by the post-prandial rise in amino acids. However, the feeding-induced stimulation of protein synthesis in skeletal muscles is independently mediated by insulin as well as amino acids.

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References

    1. Anthony JC, Lang CH, Crozier SJ, Anthony TG, MacLean DA, Kimball SR, Jefferson LS. Contribution of insulin to the translational control of protein synthesis in skeletal muscle by leucine. Am J Physiol Endocrinol Metab. 2002;282:E1092–E1101. - PubMed
    1. Attaix D, Aurousseau E, Manghebati A, Arnal M. Contribution of liver, skin, and skeletal muscle to whole-body protein synthesis in the young lamb. Br J Nutr. 1988;60:77–84. - PubMed
    1. Balage M, Sinaud S, Prod’Homme M, Dardevet D, Vary T, Kimball SR, Jefferson LS, Grizard J. Amino acids and insulin are both required to regulate assembly of the eIF4E IF4G complex in rat skeletal muscle. Am J Physiol Endocrinol Metab. 2001;281:E565–E574. - PubMed
    1. Beckett PR, Hardin DS, Davis TA, Nguyen HV, Wray-Cahen D, Copeland KC. Spectrophometric assay for measuring branched chain amino acid concentrations: application for measuring the sensitivity of protein metabolism to insulin. Anal Biochem. 1996;240:48–53. - PubMed
    1. Biolo G, Gastaldelli M, Zhang XJ, Wolfe RR. Protein synthesis and breakdown in skin and muscle: a leg model of amino acid kinetics. Am J Physiol Endocrinol Metab. 1994;267:E467–E474. - PubMed

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