Journal of Animal Science, Vol 70, Issue 6 1801-1805, Copyright © 1992 by American Society of Animal Science

JOURNAL ARTICLE

Characterization of somatotropin binding sites in pig skeletal muscle

I. Louveau and T. D. Etherton
Institut National de la Recherche Agronomique, L'Hermitage, France.

The present study was conducted to determine whether somatotropin (ST) binding sites are present in crude membrane preparations containing sarcolemma of pig skeletal muscle. Initial characterization experiments indicated that binding of bovine ST (bST) was time- and temperature-dependent and that binding was reversible. At 23 degrees C, binding was maximized between 36 and 48 h, whereas at 4 degrees C binding had not reached a maximum by 96 h. Somatotropin binding was stable between pH 5.5 and 8.5 and increased linearly between 100 and 600 micrograms of membrane protein. Addition of unlabeled bST decreased specific binding of [125I]bST in a dose-dependent manner (ED50: 1 to 1.6 ng/mL). The binding sites for bST were specific because porcine prolactin poorly inhibited bST binding. Scatchard analysis revealed the presence of a single class of binding sites (Ka: 9 to 15 x 10(9)M-1; Bmax: 5 to 6 fmol/mg of protein). In summary, the present report is the first to demonstrate that specific ST receptors are present in pig skeletal muscle. The role that ST plays in directly stimulating muscle growth and(or) muscle synthesis of insulin-like growth factor I (IGF-I) in pST-treated pigs as opposed to changes that occur as the result of an increase in plasma IGF-I concentration remains to be resolved.