Ractopamine [l-(4-hydroxyphenyl-2-(l-methyl-3-(4-hydroxyphenyl)propylamino)ethanol] enhances protein accretion in skeletal muscle (sm) of pigs. Experiments were conducted to elucidate fractional protein synthesis (FSR) and mRNA abundance for α-actin in sm of pigs fed a 16% protein diet containing 20 parts/million ractopamine for 21 days. Pigs were infused for 6 h with [14C]lysine (80 μCi/h.pig); after infusion pigs were killed, and longissimus dorsi muscle samples were obtained for RNA isolation and measurement of [14C]lysine incorporation. FSR was determined in vivo by incorporation of [14C]lysine from the muscle free amino acid pool into purified sm α-actin. FSR of sm α-actin was 55% greater in ractopamine-treated pigs than in controls. Relative mRNA abundance of α-actin was determined by dot blot hybridization of 0.1-0.4 μg RNA to human sm α-actin [32P]cDNA probe. Longissimus dorsi α-actin mRNA abundance was 2-fold greater in pigs fed ractopamine. Sm RNA was translated in vitro using a cell-free assay to determine pretranslational effects on other muscle proteins. Effects of ractopamine on muscle protein synthesis are not specific to sm α-actin, because other muscle proteins also were increased using the in vitro translation assay. These results indicate that the increase in sm accretion in pigs fed ractopamine is due in part to an increase in myofibrillar protein synthesis and that some of the increase can be accounted for by an increase in mRNA abundance for sm α-actin. (Endocrinology 126: 30963100, 1990).
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