Forty crossbred barrows (average initial weight, 66.4 kg) were utilized to determine the effects of ractopamine (a phenethanolamine/beta adrenergic agonist) on protein accretion and synthesis, activities of cathepsins B, H, L and calcium-dependent proteinase and nucleic acid content of semitendinosus muscle (ST). All pigs were offered a 16% protein, mineral and vitamin fortified corn-soybean meal diet supplemented with either 0 or 20 ppm ractopamine for 14, 21, 28, 35 or 42 d. Protein synthesis (fractional rates) was studied in pigs at d 21 and 35; ST protease activities, protein and nucleic acid content were measured on d 14, 28 and 42. Ractopamine increased (P less than .01) ST total protein content and maintained RNA muscle concentration and total ST muscle RNA content. DNA content (mg/g ST) declined (P less than .05) upon ractopamine feeding, but total DNA per muscle remained unchanged except for d 42, when the ST muscles were largest. Fractional accretion rates (FAR) were 1.0 and 1.2% for control and ractopamine-fed pigs, respectively. Fractional protein synthesis rate (FSR) was higher (P less than .06) in ractopamine-fed pigs (6.1%/d) than in control pigs (4.4%/d). Fractional protein synthesis rate could account for the observed muscle hypertrophy and increased FAR. Estimated fractional breakdown rates (FBR = FSR - FAR) were 3.4%/d and 4.9%/d for control and ractopamine-fed pigs, respectively. The activities of the catheptic proteases and calcium-dependent proteinase were not affected by the treatments.

No abstract

Ractopamine [1-(4-hydroxyphenyl-2-(1-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 alpha-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 microCi/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 alpha-actin. FSR of sm alpha-actin was 55% greater in ractopamine-treated pigs than in controls. Relative mRNA abundance of alpha-actin was determined by dot blot hybridization of 0.1-0.4 microgram RNA to human sm alpha-actin [32P]cDNA probe. Longissimus dorsi alpha-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 alpha-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 alpha-actin.