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Somatotropin regulation of protein metabolism in pigs^1,2

USDA/ARS Children’s Nutrition Research Center, Department of Pediatrics, Baylor College of Medicine, Houston, TX 77030 and Department of Cellular and Molecular Physiology, Pennsylvania State University College of Medicine, Hershey 17033

³ Correspondence: 1100 Bates Str. (phone: 713-798-7169; fax: 713-798-7171; e-mail: tdavis{at}bcm.tmc.edu).

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.

Key Words: Muscle • Pigs • Protein Synthesis • Proteolysis • Somatotropin

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