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ARS Home » Plains Area » Houston, Texas » Children's Nutrition Research Center » Research » Publications at this Location » Publication #167713
Title: SOMATOTROPIN REGULATION OF PROTEIN METABOLISM IN PIGS

Author
item Davis, Teresa
item BUSH, JILL - BAYLOR COLL OF MEDICINE
item VANN, RHONDA - PENN ST UNIV COL OF MED
item SURYAWAN, AGUS - BAYLOR COLL OF MEDICINE
item KIMBALL, SCOT - PENN ST UNIV COL OF MED
item Burrin, Douglas - Doug

Submitted to: Journal of Animal Science Supplement
Publication Type: Review Article
Publication Acceptance Date: 9/27/2003
Publication Date: 9/27/2004
Citation: Davis, T.A., Bush, J.A., Vann, R.C., Suryawan, A., Kimball, S.R., Burrin, D.G. 2004. Somatotropin regulation of protein metabolism in pigs. Journal of Animal Science. 82(E. Suppl.):E207-E213.

Interpretive Summary: Not necessary for a Review

Technical Abstract: A primary goal of exogenous somatotropin treatment is to increase lean body mass. This is accomplished, in part, by increasing the efficiency with which dietary amino acids are used for protein deposition. Somatotropin administration also improves protein balance by minimizing the loss of protein during fasting and maximizing the protein gained during meal absorption. Amino acid catabolism is decreased by somatotropin treatment, as indicated by decreases in blood urea nitrogen, urea synthesis, hepatic urea cycle enzyme activity, and amino acid oxidation. Stable isotope tracer/mass transorgan balance studies have recently demonstrated that somatotropin treatment increases protein anabolism in young, growing swine by increasing protein synthesis in the hind limb and portal-drained viscera in the fed state, with little effect on protein degradation. Detailed study of the tissue-specific responses indicates that somatotropin treatment increases protein synthesis in skeletal muscle by increasing the efficiency of the translational process, but only in the fed state. The somatotropin-induced stimulation of skeletal muscle protein synthesis involves mechanisms that enhance the binding of both mRNA and initiator methionyl-tRNA to the 40S ribosomal subunit. Somatotropin increases protein synthesis in the liver in both the fasted and fed states by increasing ribosome number, with no change in translation initiation. Thus, the protein synthetic response to somatotropin treatment is tissue-specific and dependent on nutritional state.